Citation: Fohona S. Coulibaly, Danielle N. Thomas, Bi-Botti C. Youan. Anti-HIV lectins and current delivery strategies[J]. AIMS Molecular Science, 2018, 5(1): 96-116. doi: 10.3934/molsci.2018.1.96
[1] | Churni Gupta, Necibe Tuncer, Maia Martcheva . Immuno-epidemiological co-affection model of HIV infection and opioid addiction. Mathematical Biosciences and Engineering, 2022, 19(4): 3636-3672. doi: 10.3934/mbe.2022168 |
[2] | Churni Gupta, Necibe Tuncer, Maia Martcheva . A network immuno-epidemiological model of HIV and opioid epidemics. Mathematical Biosciences and Engineering, 2023, 20(2): 4040-4068. doi: 10.3934/mbe.2023189 |
[3] | Hui Jiang, Ling Chen, Fengying Wei, Quanxin Zhu . Survival analysis and probability density function of switching heroin model. Mathematical Biosciences and Engineering, 2023, 20(7): 13222-13249. doi: 10.3934/mbe.2023590 |
[4] | Gerardo Chowell, Zhilan Feng, Baojun Song . From the guest editors. Mathematical Biosciences and Engineering, 2013, 10(5&6): i-xxiv. doi: 10.3934/mbe.2013.10.5i |
[5] | Xi-Chao Duan, Xue-Zhi Li, Maia Martcheva . Dynamics of an age-structured heroin transmission model with vaccination and treatment. Mathematical Biosciences and Engineering, 2019, 16(1): 397-420. doi: 10.3934/mbe.2019019 |
[6] | Christopher M. Kribs-Zaleta . Sociological phenomena as multiple nonlinearities: MTBI's new metaphor for complex human interactions. Mathematical Biosciences and Engineering, 2013, 10(5&6): 1587-1607. doi: 10.3934/mbe.2013.10.1587 |
[7] | Aditya S. Khanna, Dobromir T. Dimitrov, Steven M. Goodreau . What can mathematical models tell us about the relationship between circular migrations and HIV transmission dynamics?. Mathematical Biosciences and Engineering, 2014, 11(5): 1065-1090. doi: 10.3934/mbe.2014.11.1065 |
[8] | Cristian Tomasetti, Doron Levy . An elementary approach to modeling drug resistance in cancer. Mathematical Biosciences and Engineering, 2010, 7(4): 905-918. doi: 10.3934/mbe.2010.7.905 |
[9] | H. Thomas Banks, W. Clayton Thompson, Cristina Peligero, Sandra Giest, Jordi Argilaguet, Andreas Meyerhans . A division-dependent compartmental model for computing cell numbers in CFSE-based lymphocyte proliferation assays. Mathematical Biosciences and Engineering, 2012, 9(4): 699-736. doi: 10.3934/mbe.2012.9.699 |
[10] | Adam Peddle, William Lee, Tuoi Vo . Modelling chemistry and biology after implantation of a drug-eluting stent. Part Ⅱ: Cell proliferation. Mathematical Biosciences and Engineering, 2018, 15(5): 1117-1135. doi: 10.3934/mbe.2018050 |
Oil exploration and exploitation activities in addition to refining and distribution often lead to spillages that pollute the aquatic and terrestrial environment. The ecological impact of petroleum pollutants have been well documented [1,2,3,4]. Decontamination of oil-polluted environment involves mechanical, chemical and biological measures. Apart from cost, mechanical and chemical methods of treatment can lead to incomplete removal of the hydrocarbons [5] and the chemical dispersants and surfactants often used, may be toxic to the environment [6]. Microbiological techniques involve bioremediation which is a less expensive and ecologically friendly alternative for restoring the integrity of contaminated soils. It is a natural process that relies on the metabolic activities of microorganisms to degrade pollutants. A variety of microorganisms are known to be capable of degrading hydrocarbons [7], but the extent depends on the availability of nutrients such as nitrogen and phosphorus[8]. Studies have shown that addition of nitrogen and phosphorus in form of fertilizers enhances biodegradation of hydrocarbons [9]. Animal wastes (poultry droppings, cow and pig dung) as less costly source of nutrients [6] have also been used because they contain nitrogen, phosphorus and trace elements needed for microbial metabolism [10,11,12]. The animal wastes also contain a variety of microorganisms that may combine with the resident microflora of oil-polluted environment to degrade hydrocarbons.
However, researchers often ignore the possibility that the microflora of the animal may degrade hydrocarbon as much as the resident microflora of oil-polluted environments. This study was therefore designed to test two bacterial isolates from animal wastes (poultry and pig droppings) for crude oil degradation potential; and compare their crude oil degradation capability with that of the same bacterial species isolated from soil with history of petroleum contamination in the presence and absence of the animal wastes.
Soil samples were obtained from the oil-producing Niger Delta soil in an area with a history of petroleum spillage based on personal knowledge. The soil samples were collected with polythene bags that were previously sterilized by immersion in 3.5% (w/v) sodium hypochlorite solution for 12 hours. The soil was collected at depths of 5, 10 and 15 cm and bulked together for homogeneity. Thereafter, 1 mL aliquot of the serially diluted soil was used to streak mineral salts agar incorporated with crude oil (crude oil, 10 mL; KH2PO4, 1.0 g; K2HPO4, 1.0 g; NH4NO3, 0.2 g; MgSO4·7H2O, 0.2 g; FeCl2, 0.05 g; CaCl2·2H2O, 0.02 g; distilled water, 1000 mL, pH 7.0). The crude oil (Escravos light) used was obtained from Warri Refining and Petrochemical Company, Delta State, Nigeria. After 72 h incubation at room temperature (30 ± 2 ℃) emerging colonies were transferred to Nutrient Agar plates and further sub-cultured for purification. The same procedure was used to isolate hydrocarbon-utilizing bacteria from poultry and pig wastes collected from Mannes Farms, New-layout, Ekpan, Delta State, Nigeria.
The 2, 6-dichlorophenol indophenol method[13] was used to screen the crude oil degradation ability of the isolates. A loopful of each isolate was introduced into 7.5 mL of mineral salts medium containing 50 μL of crude oil before 40 μL of 2, 6-dichlorophenol indophenol (DCPIP) was added and incubated at room temperature (30 ± 2 ℃) for five days. The isolates, (two from each animal wastes and two from oil-polluted soil) that discoloured the medium in the shortest time were selected. The selection was confirmed by spectrophotometric analyses at 600 nm where the isolates that caused the lowest absorbance were matched with those selected by the visual method. The organisms were subsequently identified by cultural, microscopic and biochemical tests based on Bergeys Manual of Determinative Bacteriology [14]. For the purpose of the comparative experiment on biodegradation of crude oil in soil, two identical bacterial species from each of the animal wastes and oil-polluted soil were chosen. This brought the number of bacterial strains used for the experiment to six.
The pH of the garden soil and animal wastes used for the experiments was determined in distilled water using a digital pH meter. It was standardized with buffer solutions of pH 4, 7 and 9. Moisture content was determined by gravimetry based on oven dry weight. Total organic carbon, total nitrogen and phosphorus were analyzed by potassium dichromate, Kjeldhal and hypochlorate, methods, respectively [15].
Garden soil samples weighing 500 g were placed in flasks and sterilized by autoclaving at 121 ℃ for 30 mins. Upon cooling, the soil in six replicate flasks was mixed with filter-sterilized crude oil at 50 mL/flask. Thereafter, the flasks were inoculated with 10 mL normal saline suspension of 106 test bacterial isolate. This inoculum size was determined by plate count on Nutrient Agar plates. The set-up was repeated for each of the six test bacterial strains and set aside on the laboratory bench at room temperature for six weeks. The flasks were manually turned over for aeration and moistened with 10 mL sterile tap water at weekly intervals. The control flasks were not inoculated. After incubation for six weeks, the flask contents were extracted with hexane and subsequently analysed for TPH by gas chromatography. The concentrations were recorded in ppm. The reduction of TPH was calculated by subtracting the concentration (ppm) in test flasks from that of control and expressing it as % loss. The n-alkanes were quantified with a range of C8-C36 and the reduction of each chain was similarly expressed as % loss. The above experiment was repeated with soils mixed separately with 50 g poultry or pig wastes. The animal wastes were also sterilized by autoclave at 121 ℃ for 30 mins. The control flasks were not inoculated with the test bacterial strains. The differences in TPH concentrations in all inoculated flasks and un-inoculated control flask were analyzed by one-way Analysis of Variance (ANOVA) and Tukey post hoc multiple comparison tests using SPSS version 22.
Freshly obtained poultry and pig wastes samples were separately mixed with garden soil at a ratio of 1:1 and dispensed into 50 mL flasks in 10 g quantities before sterilisation by autoclave at 121 ℃ for 30 mins. The control flask contained garden soil only. Each of the six bacterial strains from the three sources was used to inoculate three separate flasks as illustrated in Table 1. This brought the total number of flasks inoculated to 18. A 1 mL normal saline suspension of 106bacterial strains served as inoculum. The flasks were manually shaken to ensure even mixture. The overall set up was in three replicates. The flasks were incubated at room temperature for 14 days and moistened with 1 mL sterile tap water on the 7th day. At intervals of two days, 1 g samples were aseptically withdrawn and analysed for bacterial population by plate counts on Nutrient Agar after appropriate serial dilutions.
Bacteria | Source of bacteria | Medium | ||
Soil + poultry waste | Soil + pig waste | Soil only (control) | ||
P.
vulgaris B. subtilis |
Petroleum-contaminated soil Poultry waste Pig waste Petroleum-contaminated soil Poultry waste Pig waste |
+ + + + + + |
+ + + + + + |
+ + + + + + |
+, present |
Over 35 bacterial isolates were screened for crude oil degradation ability and 12 were selected based on their high identical crude oil degradation ability. The identity of the 12 strains is presented in Table 2. However, Proteus vulgaris and Bacillus subtilis were the only strains selected for subsequent experiments because they were the only identical isolates encountered in both petroleum-polluted soil and animal wastes (Table 2). It was considered more reliable to use identical strains for the purpose of comparing the influence of their sources (animal waste, petroleum-contaminated soil) on their crude oil biodegradation potential.
Source of bacteria | Bacteria |
Oil-polluted soil |
Bacillus subtilis Proteus vulgaris |
Poultry waste Pig waste |
Acinetobacter sp. Arthrobacter sp. Bacillus cereus Klebsiella sp. Proteus vulgaris Bacillus subtilis Enterobacter aerogenes Bacillus subtilis Proteus vulgaris Enterococcus faecalis |
The degradation of crude oil by the three strains of Proteus vulgaris was significant when compared to control. However, there was no significant difference in the degradation caused by the three strains (poultry waste, pig waste, petroleum-polluted soil) in normal soil (Table 3). Over 75.5% of the total petroleum hydrocarbon (TPH) in both normal and amended soil was degraded by the bacterial strains. However, degradation of TPH in soil amended with animal wastes was significantly greater than in normal soil. This was not unexpected, because previous reports show that biodegradation of petroleum hydrocarbon is enhanced in soil treated with animal wastes [11,12,16,17]. The results in Table 3 further show that degradation of crude oil by animal waste strains of P. vulgaris was significantly enhanced in soil amended with animal wastes when compared to degradation by the strain from oil-polluted soil. Degradation of crude oil in poultry waste-amended soil by the poultry waste strain of P. vulgaris was significantly more enhanced than degradation by the pig waste strain. However, such significant difference did not occur in soil amended with pig waste. The above trend was similarly encountered in the degradation of crude oil by the three strains of Bacillus subtilis as shown in Table 4.
Crude oil medium | Source of P. v ulgaris | Mean TPH (ppm ± SD) after 6 weeks | Reduction of TPH (%) |
Normal soil | Petroleum-contaminated soil Poultry waste |
ab20.5 ± 0.1 ab19.2 ± 0.1 |
75.5 78.1 |
Poultry waste-amended soil Pig waste-amended soil |
Pig waste Control Petroleum-contaminated soil Poultry waste Pig waste Control Petroleum-contaminated soil Poultry waste Pig waste Control |
ab19.0 ± 0.1 104.5 ± 3.8 ac11.7 ± 0.02 ac2.8 ± 0.01 ac4.8 ± 0.01 102.5 ± 4.0 ac10.4 ± 0.05 abc4.5 ± 0.02 abc4.2 ± 0.03 a103.4 ± 3.6 |
8.8 0.0 88.6 97.3 95.3 0.0 89.9 95.6 95.9 0.0 |
Control = Not inoculated with P vulgaris (See Materials and Methods). Significant difference: from control, aP < 0.0001; between sources of P. vulgaris, bP > 0.05, cP < 0.001. |
The observation that degradation of crude oil by the animal waste isolates was enhanced in the presence of animal wastes when compared to strains from petroleum-polluted soil suggests the influence of ecological niche adaptation. Going by this concept, highly enhanced biodegradation ability was expected from the petroleum-polluted soil strains given their frequent exposure to petroleum contaminants. But it was not the case. The plausible explanation lies in the adaptation ability of the bacterial isolates to exact nutrients from the animal wastes as biostimulants. The attendant population growth would therefore, result in greater attack on the petroleum hydrocarbon. The animal waste strains can therefore, be seen as better placed to exact the nutrients. The observation that degradation of crude oil by animal waste strains was enhanced in soil amended with the wastes lends credence to this inference. This deduction is supported by the results presented in Figure 1, which showed that the growth of the animal waste bacterial strains was markedly greater than that of petroleum-polluted soil strains in soil mixed with animal wastes. The influence of the nutrients in animal wastes and the greater degradation ability of the bacterial strains from animal wastes were further demonstrated by the results of biodegradation of n-alkane chains (Figures 2). All the bacterial strains expectedly preferentially degraded the shorter chains (C8-C23) in normal and animal waste-amended soil as shown in Figure 2. The pattern of degradation of the alkane chains in normal soil by all the bacterial strains were not markedly different. However, there was marked increase in the degradation of the longer chains in soils amended with animal wastes when compared to biodegradation in normal soil. Compared to other strains, degradation of longer chains of n-alkane (C24-C36) by poultry waste strains in soil amended with poultry waste markedly increased. Degradation of longer chains by pig waste strains followed a similar pattern (Figures 2).
Crude oil medium | Source of B. subtilis | Mean TPH (ppm ± SD) after 6 weeks | Reduction of TPH (%) |
Normal soil | Petroleum-contaminated soil Poultry waste |
ab18.7 ± 0.4 ab17.9 ± 0.3 |
72.1 72.8 |
Poultry waste-amended soil Pig waste-amended soil |
Pig waste Control Petroleum-contaminated soil Poultry waste Pig waste Control Petroleum-contaminated soil Poultry waste Pig waste Control |
ab18.0 ± 0.3 104.5 ± 3.8 ac13.4 ± 0.1 ac3.4 ± 0.01 ac6.5 ± 0.01 102.5 ± 4.0 ac12.0 ± 0.1 ac4.3 ± 0.02 ac7.0 ± 0.03 103.4 ± 3.6 |
74.7 0.0 89.1 96.6 93.6 0.0 88.3 95.8 93.2 0.0 |
Control = Not inoculated with B. subtilis (See Materials and Methods). Significant difference from control: aP < 0.0001; between sources of B. subtilis, bP > 0.05, cP < 0.001. |
While it is acknowledged that preferential degradation of hydrocarbons by microorganisms depends on their metabolic machinery, inadequate or absence of vital nutrients (nitrogen and phosphorus) would generally impede their metabolism [18] irrespective of their hydrocarbon specificity. It is known that alkanes of C10-C24 length are more easily degraded [19] hence microorganisms tend to begin degradation with these intermediate chain lengths before the longer chains. Depending on the environment, the vital nutrients may become exhausted before the attack on the longer chain hydrocarbons begins. Thus the ability of the organism to exact nutrients from available sources such as animal wastes is likely to promote attack on longer chains as indicated by the results of this study. Some reports [10,11,12] have shown that animal wastes contain nitrogen, phosphorus and minerals that can act as biostimulants. The results of the analyses of some of the physical and chemical characteristics of the test garden soil and the animal wastes showed that concentrations of nitrogen and phosphorus were markedly higher in the animal wastes than in test soil (Table 5). Indeed phosphorus was not detected in the test soil. The alkaline pH of the animal wastes would be favorable to the strains than the acidic pH of the test soil, because bacteria tend to thrive better in neutral to alkaline environment.
Physico-chemical parameters | Soil | Source of animal waste | |
Poultry | Pig | ||
pH Moisture content (%) |
6.3 ± 0.11 3.1 ± 0.14 |
8.7 ± 0.57 20.9 ± 0.71 |
8.3 ± 0.13 23.7 ± 0.16 |
Total organic carbon (%) Total Nitrogen (%) |
27.1 ± 0.01 0.05 ± 0.00 |
44.5 ± 0.01 0.12 ± 0.01 |
44.6 ± 0.00 0.09 ± 0.01 |
Phosphorus (%) | 0.00 ± 0.00 | 0.01 ± 0.00 | 0.01 ± 0.00 |
Values in the table represent Mean ± SD |
The results indicated that the animal waste strains may have become adapted to the physical and chemical characteristics of the wastes (Table 5) hence they thrived better than the strains from soil polluted by petroleum hydrocarbon in the presence of the animal wastes. After all, the animal waste nutrients were also available to the petroleum-polluted soil strains. The specificity of adaptation was further indicated by the observation that each of the animal waste strains tended to degrade n-alkane better in the presence of the waste from which they originated. Adaptation is a natural phenomenon that ensures the survival and perpetuation of organisms in their habitats where they face physical and chemical challenges. Survival therefore depends on the ability of the organisms to develop appropriate metabolic mechanisms that will enable them overcome the physical and chemical hurdles in their environment [20].
The results of the investigation indicate that the microflora of animal wastes are prominent in biodegradation of hydrocarbon in polluted soils where animal wastes have been applied for biostimulation. The greater growth of the animal waste strains in animal waste-amended soil when compared to petroleum-polluted soil strains increased the attack on the crude oil. Thus bioaugmentation and biostimulation may be achieved in bioremediation of petroleum-polluted sites if it includes the use of animal wastes such as poultry droppings and pig dung.
The research was self-funded. The authors declare that there is no conflict of interest.
[1] | Hodder SL, Justman J, Haley DF, et al. (2010) Challenges of a hidden epidemic: HIV prevention among women in the United States. J Acquir Immune Defic Syndr 55 Suppl 2: S69–S73. |
[2] | Shattock RJ, Rosenberg Z (2012) Microbicides: Topical prevention against HIV. Cold Spring Harb Perspect Med 2: a007385. |
[3] | UNAIDS. Available from: http://www.unaids.org/en/resources/documents/2016/Global-AIDS-update-2016. |
[4] |
Swanson MD, Winter HC, Goldstein IJ, et al. (2010) A lectin isolated from bananas is a potent inhibitor of HIV replication. J Biol Chem 285: 8646–8655. doi: 10.1074/jbc.M109.034926
![]() |
[5] | Murphy EM, Greene ME, Mihailovic A, et al. (2006) Was the "ABC" approach (abstinence, being faithful, using condoms) responsible for Uganda's decline in HIV? PLoS Med 3: 1–5. |
[6] | Cohen SA. Available from: https://www.guttmacher.org/gpr/2004/11/promoting-b-abc-its-value-and-limitations-fostering-reproductive-health. |
[7] | Sovran S (2013) Understanding culture and HIV/AIDS in sub-Saharan Africa. Sahara J 10: 32–41. |
[8] |
Reniers G, Watkins S (2010) Polygyny and the spread of HIV in sub-Saharan Africa: A case of benign concurrency. Aids 24: 299–307. doi: 10.1097/QAD.0b013e328333af03
![]() |
[9] |
Helweglarsen M, Collins BE (1994) The UCLA Multidimensional Condom Attitudes Scale: Documenting the complex determinants of condom use in college students. Health Psychol 13: 224–237. doi: 10.1037/0278-6133.13.3.224
![]() |
[10] | UNAIDS. Available from: http://www.unaids.org/globalreport/Global_report.htm. |
[11] |
Qian K, Morris-Natschke SL, Lee KH (2009) HIV entry inhibitors and their potential in HIV therapy. Med Res Rev 29: 369–393. doi: 10.1002/med.20138
![]() |
[12] | Fohona S, Coulibaly BBC (2017) Current status of lectin-based cancer diagnosis and therapy. AIMS Mol Sci 4: 1–27. |
[13] | Hansen TK, Gall MA, Tarnow L, et al. (2007) Mannose-binding lectin and mortality in type 2 diabetes. Arch Intern Med 166: 2007–2013. |
[14] | Guan LZ, Tong Q, Xu J (2015) Elevated serum levels of mannose-binding lectin and diabetic nephropathy in type 2 diabetes. PLoS One 10: 1–10. |
[15] | Losin IE, Shakhnovich RM, Zykov KA, et al. (2014) Cardiovascular diseases and mannose-binding lectin. Kardiologiia 54: 64–70. |
[16] |
Kelsall A, Fitzgerald AJ, Howard CV, et al. (2002) Dietary lectins can stimulate pancreatic growth in the rat. Int J Exp Pathol 83: 203–208. doi: 10.1046/j.1365-2613.2002.00230.x
![]() |
[17] | Hoyem PH, Bruun JM, Pedersen SB, et al. (2012) The effect of weight loss on serum mannose-binding lectin levels. Clin Dev Immunol 2012: 1–5. |
[18] |
Akkouh O, Ng TB, Singh SS, et al. (2015) Lectins with anti-HIV activity: A review. Molecules 20: 648–668. doi: 10.3390/molecules20010648
![]() |
[19] |
Checkley MA, Luttge BG, Freed EO (2011) HIV-1 envelope glycoprotein biosynthesis, trafficking, and incorporation. J Mol Biol 410: 582–608. doi: 10.1016/j.jmb.2011.04.042
![]() |
[20] |
Balzarini J, Van LK, Hatse S, et al. (2004) Profile of resistance of human immunodeficiency virus to mannose-specific plant lectins. J Virol 78: 10617–10627. doi: 10.1128/JVI.78.19.10617-10627.2004
![]() |
[21] |
Huskens D, Van LK, Vermeire K, et al. (2007) Resistance of HIV-1 to the broadly HIV-1-neutralizing, anti-carbohydrate antibody 2G12. Virology 360: 294–304. doi: 10.1016/j.virol.2006.10.027
![]() |
[22] |
Blumenthal R, Durell S, Viard M (2012) HIV entry and envelope glycoprotein-mediated fusion. J Biol Chem 287: 40841–40849. doi: 10.1074/jbc.R112.406272
![]() |
[23] | Wilen CB, Tilton JC, Doms RW (2012) HIV: Cell binding and entry. Cold Spring Harb Perspect Med 2: 1–13 |
[24] |
Ratner L, Haseltine W, Patarca R, et al. (1985) Complete nucleotide sequence of the AIDS virus, HTLV-III. Nature 313: 277–284. doi: 10.1038/313277a0
![]() |
[25] |
Allan JS, Coligan JE, Barin F, et al. (1985) Major glycoprotein antigens that induce antibodies in AIDS patients are encoded by HTLV-III. Science 228: 1091–1094. doi: 10.1126/science.2986290
![]() |
[26] |
Montagnier L, Clavel F, Krust B, et al. (1985) Identification and antigenicity of the major envelope glycoprotein of lymphadenopathy-associated virus. Virology 144: 283–289. doi: 10.1016/0042-6822(85)90326-5
![]() |
[27] |
Wainhobson S, Sonigo P, Danos O, Cole S, et al. (1985) Nucleotide sequence of the AIDS virus, LAV. Cell 40: 9–17. doi: 10.1016/0092-8674(85)90303-4
![]() |
[28] |
Mizuochi T, Spellman MW, Larkin M, et al. (1988) Carbohydrate structures of the human-immunodeficiency-virus (HIV) recombinant envelope glycoprotein gp120 produced in Chinese-hamster ovary cells. Biochem J 254: 599–603. doi: 10.1042/bj2540599
![]() |
[29] | Mizuochi T, Spellman MW, Larkin M, et al. (1988) Structural characterization by chromatographic profiling of the oligosaccharides of human immunodeficiency virus (HIV) recombinant envelope glycoprotein gp120 produced in Chinese hamster ovary cells. Biomed Chromatogr 2: 260–270. |
[30] | Mizuochi T, Matthews TJ, Kato M, et al. (1990) Diversity of oligosaccharide structures on the envelope glycoprotein gp120 of human immunodeficiency virus 1 from the lymphoblastoid cell line H9. Presence of complex-type oligosaccharides with bisecting N-acetylglucosamine residues. J Biol Chem 265: 8519–8524. |
[31] | Geyer H, Holschbach C, Hunsmann G, et al. (1988) Carbohydrates of human immunodeficiency virus. Structures of oligosaccharides linked to the envelope glycoprotein 120. J Biol Chem 263: 11760–11767. |
[32] |
Go EP, Hewawasam G, Liao HX, et al. (2011) Characterization of glycosylation profiles of HIV-1 transmitted/founder envelopes by mass spectrometry. J Virol 85: 8270–8284. doi: 10.1128/JVI.05053-11
![]() |
[33] | Bonomelli C, Doores KJ, Dunlop DC, et al. (2011) The glycan shield of HIV is predominantly oligomannose independently of production system or viral clade. PLoS One 6: 1–7. |
[34] |
Go EP, Herschhorn A, Gu C, et al. (2015) Comparative Analysis of the Glycosylation Profiles of Membrane-Anchored HIV-1 Envelope Glycoprotein Trimers and Soluble gp140. J Virol 89: 8245–8257. doi: 10.1128/JVI.00628-15
![]() |
[35] |
Raska M, Takahashi K, Czernekova L, et al. (2010) Glycosylation patterns of HIV-1 gp120 depend on the type of expressing cells and affect antibody recognition. J Biol Chem 285: 20860–20869. doi: 10.1074/jbc.M109.085472
![]() |
[36] |
Zhu X, Borchers C, Bienstock RJ, et al. (2000) Mass spectrometric characterization of the glycosylation pattern of HIV-gp120 expressed in CHO cells. Biochemistry 39: 11194–11204. doi: 10.1021/bi000432m
![]() |
[37] |
Doores KJ, Bonomelli C, Harvey DJ, et al. (2010) Envelope glycans of immunodeficiency virions are almost entirely oligomannose antigens. Proc Natl Acad Sci U S A 107: 13800–13805. doi: 10.1073/pnas.1006498107
![]() |
[38] | Behrens AJ, Harvey DJ, Milne E, et al. (2017) Molecular Architecture of the Cleavage-Dependent Mannose Patch on a Soluble HIV-1 Envelope Glycoprotein Trimer. J Virol 91: 1–16. |
[39] | Sok D, Doores KJ, Briney B, et al. (2014) Promiscuous glycan site recognition by antibodies to the high-mannose patch of gp120 broadens neutralization of HIV. Sci Transl Med 6: 1–15. |
[40] | Pritchard LK, Spencer DI, Royle L, et al. (2015) Glycan clustering stabilizes the mannose patch of HIV-1 and preserves vulnerability to broadly neutralizing antibodies. Nat Commun 6: 1–11. |
[41] |
Coss KP, Vasiljevic S, Pritchard LK, et al. (2016) HIV-1 Glycan Density Drives the Persistence of the Mannose Patch within an Infected Individual. J Virol 90: 11132–11144. doi: 10.1128/JVI.01542-16
![]() |
[42] |
Raska M, Novak J (2010) Involvement of envelope-glycoprotein glycans in HIV-1 biology and infection. Arch Immunol Ther Exp 58: 191–208. doi: 10.1007/s00005-010-0072-3
![]() |
[43] |
Wang SK, Liang PH, Astronomo RD, et al. (2008) Targeting the carbohydrates on HIV-1: Interaction of oligomannose dendrons with human monoclonal antibody 2G12 and DC-SIGN. Proc Natl Acad Sci U S A 105: 3690–3695. doi: 10.1073/pnas.0712326105
![]() |
[44] |
Balzarini J (2005) Targeting the glycans of gp120: A novel approach aimed at the Achilles heel of HIV. Lancet Infect Dis 5: 726–731. doi: 10.1016/S1473-3099(05)70271-1
![]() |
[45] |
Koch M, Pancera M, Kwong PD, et al. (2003) Structure-based, targeted deglycosylation of HIV-1 gp120 and effects on neutralization sensitivity and antibody recognition. Virology 313: 387–400. doi: 10.1016/S0042-6822(03)00294-0
![]() |
[46] | Rathore U, Saha P, Kesavardhana S, et al. (2017) Glycosylation of the core of the HIV-1 envelope subunit protein gp120 is not required for native trimer formation or viral infectivity. J Biol Chem 24: 10197–10219. |
[47] |
Sanders RW, Anken EV, Nabatov AA, et al. (2008) The carbohydrate at asparagine 386 on HIV-1 gp120 is not essential for protein folding and function but is involved in immune evasion. Retrovirology 5: 1–15. doi: 10.1186/1742-4690-5-1
![]() |
[48] |
Montefiori DC, Jr RW, Mitchell WM (1988) Role of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1. Proc Natl Acad Sci U S A 85: 9248–9252. doi: 10.1073/pnas.85.23.9248
![]() |
[49] |
Francois KO, Balzarini J (2011) The highly conserved glycan at asparagine 260 of HIV-1 gp120 is indispensable for viral entry. J Biol Chem 286: 42900–42910. doi: 10.1074/jbc.M111.274456
![]() |
[50] | Mathys L, Francois KO, Quandte M, et al. (2014) Deletion of the highly conserved N-glycan at Asn260 of HIV-1 gp120 affects folding and lysosomal degradation of gp120, and results in loss of viral infectivity. PLoS One 9: 1–11. |
[51] |
Huang X, Jin W, Hu K, et al. (2012) Highly conserved HIV-1 gp120 glycans proximal to CD4-binding region affect viral infectivity and neutralizing antibody induction. Virology 423: 97–106. doi: 10.1016/j.virol.2011.11.023
![]() |
[52] |
Binley JM, Ban YE, Crooks ET, et al. (2010) Role of complex carbohydrates in human immunodeficiency virus type 1 infection and resistance to antibody neutralization. J Virol 84: 5637–5655. doi: 10.1128/JVI.00105-10
![]() |
[53] | Li Y, Luo L, Rasool N, et al. (1993) Glycosylation is necessary for the correct folding of human immunodeficiency virus gp120 in CD4 binding. J Virol 67: 584–588. |
[54] |
Li H, Jr CP, Tuen M, Visciano ML, et al. (2008) Identification of an N-linked glycosylation in the C4 region of HIV-1 envelope gp120 that is critical for recognition of neighboring CD4 T cell epitopes. J Immunol 180: 4011–4021. doi: 10.4049/jimmunol.180.6.4011
![]() |
[55] |
Behrens AJ, Vasiljevic S, Pritchard LK, et al. (2016) Composition and Antigenic Effects of Individual Glycan Sites of a Trimeric HIV-1 Envelope Glycoprotein. Cell Rep 14: 2695–2706. doi: 10.1016/j.celrep.2016.02.058
![]() |
[56] |
Pritchard LK, Vasiljevic S, Ozorowski G, et al. (2015) Structural Constraints Determine the Glycosylation of HIV-1 Envelope Trimers. Cell Rep 11: 1604–1613. doi: 10.1016/j.celrep.2015.05.017
![]() |
[57] |
Steckbeck JD, Craigo JK, Barnes CO, et al. (2011) Highly conserved structural properties of the C-terminal tail of HIV-1 gp41 protein despite substantial sequence variation among diverse clades: Implications for functions in viral replication. J Biol Chem 286: 27156–27166. doi: 10.1074/jbc.M111.258855
![]() |
[58] |
Dimonte S, Mercurio F, Svicher V, et al. (2011) Selected amino acid mutations in HIV-1 B subtype gp41 are associated with specific gp120v(3) signatures in the regulation of co-receptor usage. Retrovirology 8: 1–11. doi: 10.1186/1742-4690-8-1
![]() |
[59] |
Perrin C, Fenouillet E, Jones IM (1998) Role of gp41 glycosylation sites in the biological activity of human immunodeficiency virus type 1 envelope glycoprotein. Virology 242: 338–345. doi: 10.1006/viro.1997.9016
![]() |
[60] |
Johnson WE, Sauvron JM, Desrosiers RC (2001) Conserved, N-linked carbohydrates of human immunodeficiency virus type 1 gp41 are largely dispensable for viral replication. J Virol 75: 11426–11436. doi: 10.1128/JVI.75.23.11426-11436.2001
![]() |
[61] | Fenouillet E (1993) La N-glycosylation du VIH: Du modèle expérimental à l'application thérapeutique. J Libbery Eurotext Montrouge 9: 901–906. |
[62] |
Fenouillet E, Jones IM (1995) The glycosylation of human immunodeficiency virus type 1 transmembrane glycoprotein (gp41) is important for the efficient intracellular transport of the envelope precursor gp160. J Gen Virol 76: 1509–1514. doi: 10.1099/0022-1317-76-6-1509
![]() |
[63] | Lee WR, Yu XF, Syu WJ, et al. (1992) Mutational analysis of conserved N-linked glycosylation sites of human immunodeficiency virus type 1 gp41. J Virol 66: 1799–1803. |
[64] | Ma BJ, Alam SM, Go EP, et al. (2011) Envelope deglycosylation enhances antigenicity of HIV-1 gp41 epitopes for both broad neutralizing antibodies and their unmutated ancestor antibodies. PLoS Pathog 7: 1–16. |
[65] |
Wang LX, Song H, Liu S, et al. (2005) Chemoenzymatic synthesis of HIV-1 gp41 glycopeptides: Effects of glycosylation on the anti-HIV activity and alpha-helix bundle-forming ability of peptide C34. Chembiochem 6: 1068–1074. doi: 10.1002/cbic.200400440
![]() |
[66] |
Balzarini J, Van LK, Hatse S, et al. (2005) Carbohydrate-binding agents cause deletions of highly conserved glycosylation sites in HIV GP120: A new therapeutic concept to hit the achilles heel of HIV. J Biol Chem 280: 41005–41014. doi: 10.1074/jbc.M508801200
![]() |
[67] |
Van AE, Sanders RW, Liscaljet IM, et al. (2008) Only five of 10 strictly conserved disulfide bonds are essential for folding and eight for function of the HIV-1 envelope glycoprotein. Mol Biol Cell 19: 4298–4309. doi: 10.1091/mbc.E07-12-1282
![]() |
[68] |
Mathys L, Balzarini J (2014) The role of N-glycans of HIV-1 gp41 in virus infectivity and susceptibility to the suppressive effects of carbohydrate-binding agents. Retrovirology 11: 1–18. doi: 10.1186/1742-4690-11-1
![]() |
[69] | Fenouillet E, Jones I, Powell B, et al. (1993) Functional role of the glycan cluster of the human immunodeficiency virus type 1 transmembrane glycoprotein (gp41) ectodomain. J Virol 67: 150–160. |
[70] |
Yuste E, Bixby J, Lifson J, et al. (2008) Glycosylation of gp41 of simian immunodeficiency virus shields epitopes that can be targets for neutralizing antibodies. J Virol 82: 12472–12486. doi: 10.1128/JVI.01382-08
![]() |
[71] |
Tanaka H, Chiba H, Inokoshi J, et al. (2009) Mechanism by which the lectin actinohivin blocks HIV infection of target cells. Proc Natl Acad Sci U S A 106: 15633–15638. doi: 10.1073/pnas.0907572106
![]() |
[72] |
Hoorelbeke B, Huskens D, Ferir G, et al. (2010) Actinohivin, a broadly neutralizing prokaryotic lectin, inhibits HIV-1 infection by specifically targeting high-mannose-type glycans on the gp120 envelope. Antimicrob Agents Chemother 54: 3287–32301. doi: 10.1128/AAC.00254-10
![]() |
[73] |
Zhang F, Hoque MM, Jiang J, et al. (2014) The characteristic structure of anti-HIV actinohivin in complex with three HMTG D1 chains of HIV-gp120. Chembiochem 15: 2766–2773. doi: 10.1002/cbic.201402352
![]() |
[74] |
Bewley CA, Gustafson KR, Boyd MR, et al. (1998) Solution structure of cyanovirin-N, a potent HIV-inactivating protein. Nat Struct Biol 5: 571–578. doi: 10.1038/828
![]() |
[75] |
Barrientos LG, Louis JM, Ratner DM, et al. (2003) Solution structure of a circular-permuted variant of the potent HIV-inactivating protein cyanovirin-N: Structural basis for protein stability and oligosaccharide interaction. J Mol Biol 325: 211–223. doi: 10.1016/S0022-2836(02)01205-6
![]() |
[76] | Esser MT, Mori T, Mondor I, et al. (1999) Cyanovirin-N binds to gp120 to interfere with CD4-dependent human immunodeficiency virus type 1 virion binding, fusion, and infectivity but does not affect the CD4 binding site on gp120 or soluble CD4-induced conformational changes in gp120. J Virol 73: 4360–4371. |
[77] |
Alexandre KB, Gray ES, Mufhandu H, et al. (2012) The lectins griffithsin, cyanovirin-N and scytovirin inhibit HIV-1 binding to the DC-SIGN receptor and transfer to CD4(+) cells. Virology 423: 175–186. doi: 10.1016/j.virol.2011.12.001
![]() |
[78] |
Buffa V, Stieh D, Mamhood N, et al. (2009) Cyanovirin-N potently inhibits human immunodeficiency virus type 1 infection in cellular and cervical explant models. J Gen Virol 90: 234–243. doi: 10.1099/vir.0.004358-0
![]() |
[79] | Boyd MR, Gustafson KR, Mcmahon JB, et al. (1997) Discovery of cyanovirin-N, a novel human immunodeficiency virus-inactivating protein that binds viral surface envelope glycoprotein gp120: Potential applications to microbicide development. Antimicrob Agents Chemother 41: 1521–1530. |
[80] |
Hu Q, Mahmood N, Shattock RJ (2007) High-mannose-specific deglycosylation of HIV-1 gp120 induced by resistance to cyanovirin-N and the impact on antibody neutralization. Virology 368: 145–154. doi: 10.1016/j.virol.2007.06.029
![]() |
[81] |
Keeffe JR, Gnanapragasam PN, Gillespie SK, et al. (2011) Designed oligomers of cyanovirin-N show enhanced HIV neutralization. Proc Natl Acad Sci U S A 108: 14079–14084. doi: 10.1073/pnas.1108777108
![]() |
[82] |
Dey B, Lerner DL, Lusso P, et al. (2000) Multiple antiviral activities of cyanovirin-N: Blocking of human immunodeficiency virus type 1 gp120 interaction with CD4 and coreceptor and inhibition of diverse enveloped viruses. J Virol 74: 4562–4569. doi: 10.1128/JVI.74.10.4562-4569.2000
![]() |
[83] |
Férir G, Huskens D, Noppen S, et al. (2014) Broad anti-HIV activity of the Oscillatoria agardhii agglutinin homologue lectin family. J Antimicrob Chemother 69: 2746–2758. doi: 10.1093/jac/dku220
![]() |
[84] |
Koharudin LM, Gronenborn AM (2011) Structural basis of the anti-HIV activity of the cyanobacterial Oscillatoria Agardhii agglutinin. Structure 19: 1170–1181. doi: 10.1016/j.str.2011.05.010
![]() |
[85] |
Koharudin LM, Furey W, Gronenborn AM (2011) Novel fold and carbohydrate specificity of the potent anti-HIV cyanobacterial lectin from Oscillatoria agardhii. J Biol Chem 286: 1588–1597. doi: 10.1074/jbc.M110.173278
![]() |
[86] |
Carneiro MG, Koharudin LM, Ban D, et al. (2015) Sampling of Glycan-Bound Conformers by the Anti-HIV Lectin Oscillatoria agardhii agglutinin in the Absence of Sugar. Angew Chem 54: 6462–6465. doi: 10.1002/anie.201500213
![]() |
[87] |
Bokesch HR, O'Keefe BR, Mckee TC, et al. (2003) A potent novel anti-HIV protein from the cultured cyanobacterium Scytonema varium. Biochemistry 42: 2578–2584. doi: 10.1021/bi0205698
![]() |
[88] |
Adams EW, Ratner DM, Bokesch HR, et al. (2004) Oligosaccharide and glycoprotein microarrays as tools in HIV glycobiology; glycan-dependent gp120/protein interactions. Chem Biol 11: 875–881. doi: 10.1016/j.chembiol.2004.04.010
![]() |
[89] |
Mcfeeters RL, Xiong C, O'Keefe BR, et al. (2007) The novel fold of scytovirin reveals a new twist for antiviral entry inhibitors. J Mol Biol 369: 451–461. doi: 10.1016/j.jmb.2007.03.030
![]() |
[90] |
Alexandre KB, Gray ES, Lambson BE, et al. (2010) Mannose-rich glycosylation patterns on HIV-1 subtype C gp120 and sensitivity to the lectins, Griffithsin, Cyanovirin-N and Scytovirin. Virology 402: 187–196. doi: 10.1016/j.virol.2010.03.021
![]() |
[91] |
Williams DC, Lee JY, Cai M, et al. (2005) Crystal structures of the HIV-1 inhibitory cyanobacterial protein MVL free and bound to Man3GlcNAc2: Structural basis for specificity and high-affinity binding to the core pentasaccharide from n-linked oligomannoside. J Biol Chem 280: 29269–29276. doi: 10.1074/jbc.M504642200
![]() |
[92] | Ziółkowska NE, Wlodawer A (2006) Structural studies of algal lectins with anti-HIV activity. Acta Biochim Pol 53: 617–626. |
[93] |
Shahzadulhussan S, Gustchina E, Ghirlando R, et al. (2011) Solution structure of the monovalent lectin microvirin in complex with Man(alpha)(1–2)Man provides a basis for anti-HIV activity with low toxicity. J Biol Chem 286: 20788–20796. doi: 10.1074/jbc.M111.232678
![]() |
[94] |
Huskens D, Ferir G, Vermeire K, et al. (2010) Microvirin, a novel alpha(1,2)-mannose-specific lectin isolated from Microcystis aeruginosa, has anti-HIV-1 activity comparable with that of cyanovirin-N but a much higher safety profile. J Biol Chem 285: 24845–24854. doi: 10.1074/jbc.M110.128546
![]() |
[95] |
López S, Armandugon M, Bastida J, et al. (2003) Anti-human immunodeficiency virus type 1 (HIV-1) activity of lectins from Narcissus species. Planta Med 69: 109–112. doi: 10.1055/s-2003-37715
![]() |
[96] | Müller WEG, Forrest JMS, Chang SH, et al. (1991) Narcissus and Gerardia lectins: Tools for the development of a vaccine against AIDS and a new ELISA to quantify HIV-gp 120. Lectins Cancer 1991: 27–40. |
[97] |
Charan RD, Munro MH, O'Keefe BR, et al. (2000) Isolation and characterization of Myrianthus holstii lectin, a potent HIV-1 inhibitory protein from the plant Myrianthus holstii(1). J Nat Prod 63: 1170–1174. doi: 10.1021/np000039h
![]() |
[98] |
Coulibaly FS, Youan BB (2014) Concanavalin A-polysaccharides binding affinity analysis using a quartz crystal microbalance. Biosens Bioelectron 59: 404–411. doi: 10.1016/j.bios.2014.03.040
![]() |
[99] | Bhattacharyya L, Brewer CF (1989) Interactions of concanavalin A with asparagine-linked glycopeptides. Structure/activity relationships of the binding and precipitation of oligomannose and bisected hybrid-type glycopeptides with concanavalin A. Eur J Biochem 178: 721–726. |
[100] |
Witvrouw M, Fikkert V, Hantson A, et al. (2005) Resistance of human immunodeficiency virus type 1 to the high-mannose binding agents cyanovirin N and concanavalin A. J Virol 79: 7777–7784. doi: 10.1128/JVI.79.12.7777-7784.2005
![]() |
[101] |
Hansen JE, Nielsen CM, Nielsen C, et al. (1989) Correlation between carbohydrate structures on the envelope glycoprotein gp120 of HIV-1 and HIV-2 and syncytium inhibition with lectins. Aids 3: 635–641. doi: 10.1097/00002030-198910000-00003
![]() |
[102] | Matsui T, Kobayashi S, Yoshida O, et al. (1990) Effects of succinylated concanavalin A on infectivity and syncytial formation of human immunodeficiency virus. Med Microbiol Immunol 179: 225–235. |
[103] |
Pashov A, Macleod S, Saha R, et al. (2005) Concanavalin A binding to HIV envelope protein is less sensitive to mutations in glycosylation sites than monoclonal antibody 2G12. Glycobiology 15: 994–1001. doi: 10.1093/glycob/cwi083
![]() |
[104] |
Swanson MD, Boudreaux DM, Salmon L, et al. (2015) Engineering a therapeutic lectin by uncoupling mitogenicity from antiviral activity. Cell 163: 746–758. doi: 10.1016/j.cell.2015.09.056
![]() |
[105] |
Alexandre KB, Gray ES, Pantophlet R, et al. (2011) Binding of the mannose-specific lectin, griffithsin, to HIV-1 gp120 exposes the CD4-binding site. J Virol 85: 9039–9050. doi: 10.1128/JVI.02675-10
![]() |
[106] |
Mori T, O'Keefe BR, Bringans S, et al. (2005) Isolation and characterization of griffithsin, a novel HIV-inactivating protein, from the red alga Griffithsia sp. J Biol Chem 280: 9345–9353. doi: 10.1074/jbc.M411122200
![]() |
[107] |
Emau P, Tian B, O'Keefe BR, et al. (2007) Griffithsin, a potent HIV entry inhibitor, is an excellent candidate for anti-HIV microbicide. J Med Primatol 36: 244–253. doi: 10.1111/j.1600-0684.2007.00242.x
![]() |
[108] |
Moulaei T, Alexandre KB, Shenoy SR, et al. (2015) Griffithsin tandemers: Flexible and potent lectin inhibitors of the human immunodeficiency virus. Retrovirology 12: 1–14. doi: 10.1186/s12977-014-0129-1
![]() |
[109] | Zhou X, Liu J, Yang B, et al. (2013) Marine natural products with anti-HIV activities in the last decade. Curr Med Chem 20: 953–973. |
[110] |
Wang JH, Kong J, Li W, et al. (2006) A beta-galactose-specific lectin isolated from the marine worm Chaetopterus variopedatus possesses anti-HIV-1 activity. Comp Biochem Physiol C Toxicol Pharmacol 142: 111–117. doi: 10.1016/j.cbpc.2005.10.019
![]() |
[111] |
Bulgheresi S, Schabussova I, Chen T, et al. (2006) A new C-type lectin similar to the human immunoreceptor DC-SIGN mediates symbiont acquisition by a marine nematode. Appl Environ Microbiol 72: 2950–2956. doi: 10.1128/AEM.72.4.2950-2956.2006
![]() |
[112] |
Nabatov AA, Jong MAWPD, Witte LD, et al. (2008) C-type lectin Mermaid inhibits dendritic cell mediated HIV-1 transmission to CD4+ T cells. Virology 378: 323–328. doi: 10.1016/j.virol.2008.05.025
![]() |
[113] |
Molchanova V, Chikalovets I, Chernikov O, et al. (2007) A new lectin from the sea worm Serpula vermicularis: Isolation, characterization and anti-HIV activity. Comp Biochem Physiol C Toxicol Pharmacol 145: 184–193. doi: 10.1016/j.cbpc.2006.11.012
![]() |
[114] |
Vo TS, Kim SK (2010) Potential anti-HIV agents from marine resources: An overview. Mar Drugs 8: 2871–2892. doi: 10.3390/md8122871
![]() |
[115] |
Mahalingam A, Geonnotti AR, Balzarini J, et al. (2011) Activity and safety of synthetic lectins based on benzoboroxole-functionalized polymers for inhibition of HIV entry. Mol Pharmaceutics 8: 2465–2475. doi: 10.1021/mp2002957
![]() |
[116] |
Berube M, Dowlut M, Hall DG (2008) Benzoboroxoles as efficient glycopyranoside-binding agents in physiological conditions: Structure and selectivity of complex formation. J Org Chem 73: 6471–6479. doi: 10.1021/jo800788s
![]() |
[117] | Trippier PC, Mcguigan C, Balzarini J (2010) Phenylboronic-acid-based carbohydrate binders as antiviral therapeutics: Monophenylboronic acids. Antivir Chem Chemother 20: 249–257. |
[118] | Trippier PC, Balzarini J, Mcguigan C (2011) Phenylboronic-acid-based carbohydrate binders as antiviral therapeutics: Bisphenylboronic acids. Antivir Chem Chemother 21: 129–142. |
[119] | Khan JM, Qadeer A, Ahmad E, et al. (2013) Monomeric banana lectin at acidic pH overrules conformational stability of its native dimeric form. PLoS One 8: 1–12. |
[120] |
Suzuki K, Ohbayashi N, Jiang J, et al. (2012) Crystallographic study of the interaction of the anti-HIV lectin actinohivin with the alpha(1-2)mannobiose moiety of gp120 HMTG. Acta Crystallogr Sect F Struct Biol Cryst Commun 68: 1060–1063. doi: 10.1107/S1744309112031077
![]() |
[121] | Tevibénissan C, Bélec L, Lévy M, et al. (1997) In vivo semen-associated pH neutralization of cervicovaginal secretions. Clin Diagn Lab Immunol 4: 367–374. |
[122] |
Ballerstadt R, Evans C, Mcnichols R, et al. (2006) Concanavalin A for in vivo glucose sensing: A biotoxicity review. Biosens Bioelectron 22: 275–284. doi: 10.1016/j.bios.2006.01.008
![]() |
[123] |
Krauss S, Buttgereit F, Brand MD (1999) Effects of the mitogen concanavalin A on pathways of thymocyte energy metabolism. Biochim Biophys Acta 1412: 129–138. doi: 10.1016/S0005-2728(99)00058-4
![]() |
[124] |
Balzarini J, Laethem KV, Peumans WJ, et al. (2006) Mutational pathways, resistance profile, and side effects of cyanovirin relative to human immunodeficiency virus type 1 strains with N-glycan deletions in their gp120 envelopes. J Virol 80: 8411–8421. doi: 10.1128/JVI.00369-06
![]() |
[125] |
Gavrovicjankulovic M, Poulsen K, Brckalo T, et al. (2008) A novel recombinantly produced banana lectin isoform is a valuable tool for glycoproteomics and a potent modulator of the proliferation response in CD3+, CD4+, and CD8+ populations of human PBMCs. Int J Biochem Cell Biol 40: 929–941. doi: 10.1016/j.biocel.2007.10.033
![]() |
[126] |
Mahalingam A, Geonnotti AR, Balzarini J, et al. (2011) Activity and safety of synthetic lectins based on benzoboroxole-functionalized polymers for inhibition of HIV entry. Mol Pharm 8: 2465–2475. doi: 10.1021/mp2002957
![]() |
[127] |
Lam SK, Ng TB (2011) Lectins: Production and practical applications. Appl Microbiol Biotechnol 89: 45–55. doi: 10.1007/s00253-010-2892-9
![]() |
[128] |
Scanlan CN, Offer J, Zitzmann N, et al. (2007) Exploiting the defensive sugars of HIV-1 for drug and vaccine design. Nature 446: 1038–1045. doi: 10.1038/nature05818
![]() |
[129] | Gupta A, Gupta RK, Gupta GS (2009) Targeting cells for drug and gene delivery: Emerging applications of mannans and mannan binding lectins. J Sci Ind Res 68: 465–483. |
[130] |
Ghazarian H, Idoni B, Oppenheimer SB (2011) A glycobiology review: Carbohydrates, lectins and implications in cancer therapeutics. Acta Histochem 113: 236–247. doi: 10.1016/j.acthis.2010.02.004
![]() |
[131] |
Toda S, Ishii N, Okada E, et al. (1997) HIV-1-specific cell-mediated immune responses induced by DNA vaccination were enhanced by mannan-coated liposomes and inhibited by anti-interferon-gamma antibody. Immunology 92: 111–117. doi: 10.1046/j.1365-2567.1997.00307.x
![]() |
[132] |
Zelensky AN, Gready JE (2005) The C-type lectin-like domain superfamily. FEBS J 272: 6179–6217. doi: 10.1111/j.1742-4658.2005.05031.x
![]() |
[133] |
Cui Z, Hsu CH, Mumper RJ (2003) Physical characterization and macrophage cell uptake of mannan-coated nanoparticles. Drug Dev Ind Pharm 29: 689–700. doi: 10.1081/DDC-120021318
![]() |
[134] |
Espuelas S, Thumann C, Heurtault B, et al. (2008) Influence of ligand valency on the targeting of immature human dendritic cells by mannosylated liposomes. Bioconjugate Chem 19: 2385–2393. doi: 10.1021/bc8002524
![]() |
[135] |
Zhang Q, Su L, Collins J, et al. (2014) Dendritic cell lectin-targeting sentinel-like unimolecular glycoconjugates to release an anti-HIV drug. J Am Chem Soc 136: 4325–4332. doi: 10.1021/ja4131565
![]() |
[136] |
Hong PWP, Flummerfelt KB, Parseval AD, et al. (2002) Human immunodeficiency virus envelope (gp120) binding to DC-SIGN and primary dendritic cells is carbohydrate dependent but does not involve 2G12 or cyanovirin binding sites: Implications for structural analyses of gp120-DC-SIGN binding. J Virol 76: 12855–12865. doi: 10.1128/JVI.76.24.12855-12865.2002
![]() |
[137] |
Cruz LJ, Tacken PJ, Fokkink R, et al. (2010) Targeted PLGA nano- but not microparticles specifically deliver antigen to human dendritic cells via DC-SIGN in vitro. J Controlled Release 144: 118–126. doi: 10.1016/j.jconrel.2010.02.013
![]() |
[138] |
Ingale J, Stano A, Guenaga J, et al. (2016) High-Density Array of Well-Ordered HIV-1 Spikes on Synthetic Liposomal Nanoparticles Efficiently Activate B Cells. Cell Rep 15: 1986–1999. doi: 10.1016/j.celrep.2016.04.078
![]() |
[139] | He L, Val ND, Morris CD, et al. (2016) Presenting native-like trimeric HIV-1 antigens with self-assembling nanoparticles. Nat Commun 7: 1–15. |
[140] |
Akashi M, Niikawa T, Serizawa T, et al. (1998) Capture of HIV-1 gp120 and virions by lectin-immobilized polystyrene nanospheres. Bioconjugate Chem 9: 50–53. doi: 10.1021/bc970045y
![]() |
[141] |
Hayakawa T, Kawamura M, Okamoto M, et al. (1998) Concanavalin A-immobilized polystyrene nanospheres capture HIV-1 virions and gp120: Potential approach towards prevention of viral transmission. J Med Virol 56: 327–331. doi: 10.1002/(SICI)1096-9071(199812)56:4<327::AID-JMV7>3.0.CO;2-A
![]() |
[142] | Coulibaly FS, Ezoulin MJM, Purohit SS, et al. (2017) Layer-by-layer engineered microbicide drug delivery system targeting HIV-1 gp120: Physicochemical and biological properties. Mol Pharm 14: 3512–3527. |
[143] |
Takahashi K, Moyo P, Chigweshe L, et al. (2013) Efficacy of recombinant chimeric lectins, consisting of mannose binding lectin and L-ficolin, against influenza A viral infection in mouse model study. Virus Res 178: 495–501. doi: 10.1016/j.virusres.2013.10.001
![]() |
[144] |
Sato Y, Morimoto K, Kubo T, et al. (2015) Entry Inhibition of Influenza Viruses with High Mannose Binding Lectin ESA-2 from the Red Alga Eucheuma serra through the Recognition of Viral Hemagglutinin. Mar Drugs 13: 3454–3465. doi: 10.3390/md13063454
![]() |
[145] |
Kachko A, Loesgen S, Shahzad-Ul-Hussan S, et al. (2013) Inhibition of hepatitis C virus by the cyanobacterial protein Microcystis viridis lectin: Mechanistic differences between the high-mannose specific lectins MVL, CV-N, and GNA. Mol Pharmaceutics 10: 4590–4602. doi: 10.1021/mp400399b
![]() |
[146] |
Gadjeva M, Paludan SR, Thiel S, et al. (2004) Mannan-binding lectin modulates the response to HSV-2 infection. Clin Exp Immunol 138: 304–311. doi: 10.1111/j.1365-2249.2004.02616.x
![]() |
[147] |
Eisen S, Dzwonek A, Klein NJ (2008) Mannose-binding lectin in HIV infection. Future Virol 3: 225–233. doi: 10.2217/17460794.3.3.225
![]() |
[148] |
Ji X, Olinger GG, Aris S, et al. (2005) Mannose-binding lectin binds to Ebola and Marburg envelope glycoproteins, resulting in blocking of virus interaction with DC-SIGN and complement-mediated virus neutralization. J Gen Virol 86: 2535–2542. doi: 10.1099/vir.0.81199-0
![]() |
[149] |
Keyaerts E, Vijgen L, Pannecouque C, et al. (2007) Plant lectins are potent inhibitors of coronaviruses by interfering with two targets in the viral replication cycle. Antiviral Res 75: 179–187. doi: 10.1016/j.antiviral.2007.03.003
![]() |
[150] |
Hamel R, Dejarnac O, Wichit S, et al. (2015) Biology of Zika Virus Infection in Human Skin Cells. J Virol 89: 8880–8896. doi: 10.1128/JVI.00354-15
![]() |
[151] |
Clement F, Venkatesh YP (2010) Dietary garlic (Allium sativum) lectins, ASA I and ASA II, are highly stable and immunogenic. Int Immunopharmacol 10: 1161–1169. doi: 10.1016/j.intimp.2010.06.022
![]() |
[152] | Lusvarghi S, Bewley CA (2016) Griffithsin: An Antiviral Lectin with Outstanding Therapeutic Potential. Viruses 8: 1–18. |
Bacteria | Source of bacteria | Medium | ||
Soil + poultry waste | Soil + pig waste | Soil only (control) | ||
P.
vulgaris B. subtilis |
Petroleum-contaminated soil Poultry waste Pig waste Petroleum-contaminated soil Poultry waste Pig waste |
+ + + + + + |
+ + + + + + |
+ + + + + + |
+, present |
Source of bacteria | Bacteria |
Oil-polluted soil |
Bacillus subtilis Proteus vulgaris |
Poultry waste Pig waste |
Acinetobacter sp. Arthrobacter sp. Bacillus cereus Klebsiella sp. Proteus vulgaris Bacillus subtilis Enterobacter aerogenes Bacillus subtilis Proteus vulgaris Enterococcus faecalis |
Crude oil medium | Source of P. v ulgaris | Mean TPH (ppm ± SD) after 6 weeks | Reduction of TPH (%) |
Normal soil | Petroleum-contaminated soil Poultry waste |
ab20.5 ± 0.1 ab19.2 ± 0.1 |
75.5 78.1 |
Poultry waste-amended soil Pig waste-amended soil |
Pig waste Control Petroleum-contaminated soil Poultry waste Pig waste Control Petroleum-contaminated soil Poultry waste Pig waste Control |
ab19.0 ± 0.1 104.5 ± 3.8 ac11.7 ± 0.02 ac2.8 ± 0.01 ac4.8 ± 0.01 102.5 ± 4.0 ac10.4 ± 0.05 abc4.5 ± 0.02 abc4.2 ± 0.03 a103.4 ± 3.6 |
8.8 0.0 88.6 97.3 95.3 0.0 89.9 95.6 95.9 0.0 |
Control = Not inoculated with P vulgaris (See Materials and Methods). Significant difference: from control, aP < 0.0001; between sources of P. vulgaris, bP > 0.05, cP < 0.001. |
Crude oil medium | Source of B. subtilis | Mean TPH (ppm ± SD) after 6 weeks | Reduction of TPH (%) |
Normal soil | Petroleum-contaminated soil Poultry waste |
ab18.7 ± 0.4 ab17.9 ± 0.3 |
72.1 72.8 |
Poultry waste-amended soil Pig waste-amended soil |
Pig waste Control Petroleum-contaminated soil Poultry waste Pig waste Control Petroleum-contaminated soil Poultry waste Pig waste Control |
ab18.0 ± 0.3 104.5 ± 3.8 ac13.4 ± 0.1 ac3.4 ± 0.01 ac6.5 ± 0.01 102.5 ± 4.0 ac12.0 ± 0.1 ac4.3 ± 0.02 ac7.0 ± 0.03 103.4 ± 3.6 |
74.7 0.0 89.1 96.6 93.6 0.0 88.3 95.8 93.2 0.0 |
Control = Not inoculated with B. subtilis (See Materials and Methods). Significant difference from control: aP < 0.0001; between sources of B. subtilis, bP > 0.05, cP < 0.001. |
Physico-chemical parameters | Soil | Source of animal waste | |
Poultry | Pig | ||
pH Moisture content (%) |
6.3 ± 0.11 3.1 ± 0.14 |
8.7 ± 0.57 20.9 ± 0.71 |
8.3 ± 0.13 23.7 ± 0.16 |
Total organic carbon (%) Total Nitrogen (%) |
27.1 ± 0.01 0.05 ± 0.00 |
44.5 ± 0.01 0.12 ± 0.01 |
44.6 ± 0.00 0.09 ± 0.01 |
Phosphorus (%) | 0.00 ± 0.00 | 0.01 ± 0.00 | 0.01 ± 0.00 |
Values in the table represent Mean ± SD |
Bacteria | Source of bacteria | Medium | ||
Soil + poultry waste | Soil + pig waste | Soil only (control) | ||
P.
vulgaris B. subtilis |
Petroleum-contaminated soil Poultry waste Pig waste Petroleum-contaminated soil Poultry waste Pig waste |
+ + + + + + |
+ + + + + + |
+ + + + + + |
+, present |
Source of bacteria | Bacteria |
Oil-polluted soil |
Bacillus subtilis Proteus vulgaris |
Poultry waste Pig waste |
Acinetobacter sp. Arthrobacter sp. Bacillus cereus Klebsiella sp. Proteus vulgaris Bacillus subtilis Enterobacter aerogenes Bacillus subtilis Proteus vulgaris Enterococcus faecalis |
Crude oil medium | Source of P. v ulgaris | Mean TPH (ppm ± SD) after 6 weeks | Reduction of TPH (%) |
Normal soil | Petroleum-contaminated soil Poultry waste |
ab20.5 ± 0.1 ab19.2 ± 0.1 |
75.5 78.1 |
Poultry waste-amended soil Pig waste-amended soil |
Pig waste Control Petroleum-contaminated soil Poultry waste Pig waste Control Petroleum-contaminated soil Poultry waste Pig waste Control |
ab19.0 ± 0.1 104.5 ± 3.8 ac11.7 ± 0.02 ac2.8 ± 0.01 ac4.8 ± 0.01 102.5 ± 4.0 ac10.4 ± 0.05 abc4.5 ± 0.02 abc4.2 ± 0.03 a103.4 ± 3.6 |
8.8 0.0 88.6 97.3 95.3 0.0 89.9 95.6 95.9 0.0 |
Control = Not inoculated with P vulgaris (See Materials and Methods). Significant difference: from control, aP < 0.0001; between sources of P. vulgaris, bP > 0.05, cP < 0.001. |
Crude oil medium | Source of B. subtilis | Mean TPH (ppm ± SD) after 6 weeks | Reduction of TPH (%) |
Normal soil | Petroleum-contaminated soil Poultry waste |
ab18.7 ± 0.4 ab17.9 ± 0.3 |
72.1 72.8 |
Poultry waste-amended soil Pig waste-amended soil |
Pig waste Control Petroleum-contaminated soil Poultry waste Pig waste Control Petroleum-contaminated soil Poultry waste Pig waste Control |
ab18.0 ± 0.3 104.5 ± 3.8 ac13.4 ± 0.1 ac3.4 ± 0.01 ac6.5 ± 0.01 102.5 ± 4.0 ac12.0 ± 0.1 ac4.3 ± 0.02 ac7.0 ± 0.03 103.4 ± 3.6 |
74.7 0.0 89.1 96.6 93.6 0.0 88.3 95.8 93.2 0.0 |
Control = Not inoculated with B. subtilis (See Materials and Methods). Significant difference from control: aP < 0.0001; between sources of B. subtilis, bP > 0.05, cP < 0.001. |
Physico-chemical parameters | Soil | Source of animal waste | |
Poultry | Pig | ||
pH Moisture content (%) |
6.3 ± 0.11 3.1 ± 0.14 |
8.7 ± 0.57 20.9 ± 0.71 |
8.3 ± 0.13 23.7 ± 0.16 |
Total organic carbon (%) Total Nitrogen (%) |
27.1 ± 0.01 0.05 ± 0.00 |
44.5 ± 0.01 0.12 ± 0.01 |
44.6 ± 0.00 0.09 ± 0.01 |
Phosphorus (%) | 0.00 ± 0.00 | 0.01 ± 0.00 | 0.01 ± 0.00 |
Values in the table represent Mean ± SD |