Functions of HIV envelope glycans

Fenouillet, Emmanuel; Gluckman, Jean Claude; Jones, Ian M.

doi:10.1016/0968-0004(94)90034-5

Cited by 86 publications

(52 citation statements)

References 38 publications

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“…PH S00 14-5793(96)009 1 2-X A second structural class of potentially neutralizing targets for immune intervention is the carbohydrate repertoire covalently attached to gpl20. The structure and function of these glycan chains have now been studied extensively ( [10] and references cited therein), however, the absolute roles of the many sugar chains are still under debate [11]. It has been shown that removal of N-linked glycans from gpl20 impairs binding of the protein to CD4 + cells [12].…”

Section: Introductionmentioning

confidence: 99%

Structural comparison of a 15 residue peptide from the V3 loop of HIV‐1_IIIb and an O‐glycosylated analogue

et al. 1996

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As part of a program to study the effect of glycosylation on the three-dimensional structures of HIV-ImB V3 peptide constructs, we have examined the solution structures of a 15 residue peptide (RIQRGPGRAFVTIGK, P18ms), originally mapped as an epitope recognized by CD8 + D u class I MHC-restricted murine cytotoxic T-lymphocytes (CTL), and an analogue (P18mB-g), O-glycosylated with an t~-galactosamine on Thr-12, using NMR, circular dichroism and molecular modeling methods. Our studies show that the peptides sample mainly random conformations in aqueous solution near 25°C and become more ordered by the addition of trifluoroethanol. Upon decreasing the temperature to 5°C, a reverse turn is formed around the immunodominant tip (GS-RS). Glycosylation on T Iz 'tightens' the turn slightly as suggested by NOE and CD analysis. In addition, the sugar has a defined conformation with respect to the peptide backbone and influences the local peptide conformation. These data suggest that simple glycosylation may influence the conformational equilibrium of a V3 peptide which contains a domain critical for antibody recognition and virus neutralization. We also show that the ability of cytotoxic Tlymphocytes (CTL) to lyse tumor cells presenting P18ttm was completely abrogated by threonine glycosylation.

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Section: Introductionmentioning

confidence: 99%

Structural comparison of a 15 residue peptide from the V3 loop of HIV‐1_IIIb and an O‐glycosylated analogue

et al. 1996

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“…Thus, when N-glycosylation is blocked by enzyme inhibitors or by eliminating the canonical sites, gp120 does not fold properly (8,(11)(12)(13). The modification or removal of carbohydrates from virions can affect Env function and virus infectivity (14 -17).…”

mentioning

confidence: 99%

Partial Enzymatic Deglycosylation Preserves the Structure of Cleaved Recombinant HIV-1 Envelope Glycoprotein Trimers

Depetris

Julien

Khayat

et al. 2012

Journal of Biological Chemistry

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“…The glycosylation as a feature of the virus greatly impacts the vaccine strategies and challenges the virologists [45]. The glycans shields the envelope glycoproteins that can be studied better by deglycosylation [46].…”

Section: Glycosylationmentioning

confidence: 99%

Conventional Vaccine to Prevent AIDS A Paradigm or A Paradox? A SWOT Analysis

Christdas¹

2016

HIV Curr Res

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AIDS as a disease afflicts mankind for more than 3 decades. HIV, the causative is not yet checked with a prophylactic vaccine. The plausibility of the prevention by conventional prophylactic strategies based on Jenner's conventional method of inducing memory response is reviewed here. In order to find the right direction towards achieving this goal, a SWOT analysis is represented here with a Venn diagram. Our increasing awareness on the viral genome and the antiviral treatment with the sensitive diagnostic tools strengthen the efforts, while the viral nature privileges its replenishment by hampering the host immune memory. Though antiviral drugs promise a notable degree of control, they render selection pressure favoring viral escapism with perking quasispecies or circulating recombinant forms (CRF). Few historical clinical trials teach us to frame new opportunities for the conduct of such trials that assures safety. The knowledge has exponentially increased on the host immune response, human genetics, retrovirology, drug development, gene delivery system to understand that HIV is the only pathogen that had the greatest consumption of our time and resources. The technological advancements add to our strength. However, the virus with its biological features proves its intrinsic competency for survival. Though the antiviral therapy confers some hope, the resistant forms pose a threat to their continuation. It emphasizes the need for prevention and suggests novel, unconventional prophylaxis. Treatment as a means of prevention and the use of immunomodulators to decrease the disease progression can help us to win the belligerence against AIDS.

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Functions of HIV envelope glycans

Cited by 86 publications

References 38 publications

Structural comparison of a 15 residue peptide from the V3 loop of HIV‐1_IIIb and an O‐glycosylated analogue

Structural comparison of a 15 residue peptide from the V3 loop of HIV‐1_IIIb and an O‐glycosylated analogue

Partial Enzymatic Deglycosylation Preserves the Structure of Cleaved Recombinant HIV-1 Envelope Glycoprotein Trimers

Conventional Vaccine to Prevent AIDS A Paradigm or A Paradox? A SWOT Analysis

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Functions of HIV envelope glycans

Cited by 86 publications

References 38 publications

Structural comparison of a 15 residue peptide from the V3 loop of HIV‐1IIIb and an O‐glycosylated analogue

Structural comparison of a 15 residue peptide from the V3 loop of HIV‐1IIIb and an O‐glycosylated analogue

Partial Enzymatic Deglycosylation Preserves the Structure of Cleaved Recombinant HIV-1 Envelope Glycoprotein Trimers

Conventional Vaccine to Prevent AIDS A Paradigm or A Paradox? A SWOT Analysis

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Product

Resources

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Structural comparison of a 15 residue peptide from the V3 loop of HIV‐1_IIIb and an O‐glycosylated analogue

Structural comparison of a 15 residue peptide from the V3 loop of HIV‐1_IIIb and an O‐glycosylated analogue