The antigenic structure of the HIV gp120 envelope glycoprotein

@article{Wyatt1998TheAS,
  title={The antigenic structure of the HIV gp120 envelope glycoprotein},
  author={Richard T. Wyatt and Peter D. Kwong and Elizabeth Desjardins and Raymond W. Sweet and James E. Robinson and Wayne A. Hendrickson and Joseph G. Sodroski},
  journal={Nature},
  year={1998},
  volume={393},
  pages={705-711}
}
The human immunodeficiency virus HIV-1 establishes persistent infections in humans which lead to acquired immunodeficiency syndrome (AIDS). The HIV-1 envelope glycoproteins, gp120 and gp41, are assembled into a trimeric complex that mediates virus entry into target cells. HIV-1 entry depends on the sequential interaction of the gp120 exterior envelope glycoprotein with the receptors on the cell, CD4 and members of the chemokine receptor family. The gp120 glycoprotein, which can be shed from the… 
Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
TLDR
The structure reveals a cavity-laden CD4–gp120 interface, a conserved binding site for the chemokine receptor, evidence for a conformational change upon CD4 binding, the nature of a CD4-induced antibody epitope, and specific mechanisms for immune evasion.
Structures of HIV-1 gp120 envelope glycoproteins from laboratory-adapted and primary isolates.
TLDR
Despite dramatic antigenic differences between primary and laboratory-adapted HIV-1, the gp120 cores from these isolates are remarkably similar, which indicates that neutralization resistance is specified by quaternary interactions involving the major variable loops and thus affords a mechanism for viral adaptation.
Structural Basis of Immune Evasion at the Site of CD4 Attachment on HIV-1 gp120
TLDR
Co-crystal structures for two poorly neutralizing, CD4–binding site (CD4BS) antibodies, F105 and b13, in complexes with gp120 are determined, finding these conformations to be poorly compatible with the viral spike.
Asymmetric Structures and Conformational Plasticity of the Uncleaved Full-Length Human Immunodeficiency Virus Envelope Glycoprotein Trimer
  • Shijian Zhang, Kunyu Wang, +10 authors Youdong Mao
  • Medicine
    Journal of virology
  • 2021
TLDR
Cryo-electron microscopy of the purified BMS-806-bound gp160 revealed two hitherto unknown asymmetric trimer conformations, providing insights into the allosteric coupling between trimer opening and structural variation in the gp41 HR1N region.
Structural definition of a conserved neutralization epitope on HIV-1 gp120
TLDR
A site of vulnerability, related to a functional requirement for efficient association with CD4, can therefore be targeted by antibody to neutralize HIV-1.
Gp41-targeted antibodies restore infectivity of a fusion-deficient HIV-1 envelope glycoprotein
TLDR
An HIV-1 Env variant with impaired infectivity whose Env functionality is restored through the binding of host antibodies is identified, contributing to the understanding of gp41 residues involved in membrane fusion and identifying a mechanism by which host factors can alleviate a viral defect.
Characterization of the Outer Domain of the gp120 Glycoprotein from Human Immunodeficiency Virus Type 1
TLDR
The results underscore the qualitatively different humoral immune responses elicited during natural infection and after gp120 vaccination and help to explain the failure of gp120 as an effective vaccine.
Molecular architecture of native HIV-1 gp120 trimers
TLDR
It is demonstrated that CD4 binding results in a major reorganization of the Env trimer, causing an outward rotation and displacement of each gp120 monomer, leading to closer contact between the viral and target cell membranes.
Conformational Differences between Functional Human Immunodeficiency Virus Envelope Glycoprotein Trimers and Stabilized Soluble Trimers
TLDR
Evidence is presented that stabilized versions of HIV-1 Env trimers stabilized by a gp120-gp41 disulfide bond and a change (I559P) in gp41 have been structurally characterized and can guide the improvement of envelope glycoprotein preparations to achieve greater similarity to the viral envelope Glycoprotein spike, potentially increasing their effectiveness as a vaccine.
Isolate-Specific Differences in the Conformational Dynamics and Antigenicity of HIV-1 gp120
TLDR
Four full-length, glycosylated gp120 monomers from diverse HIV-1 isolates are studied by using small-angle X-ray scattering to probe the overall subunit morphology and hydrogen/deuterium-exchange with mass spectrometry to characterize the local structural order of each gp120, providing additional insight into the structural determinants of gp120 antigenicity.
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 30 REFERENCES
Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
TLDR
The structure reveals a cavity-laden CD4–gp120 interface, a conserved binding site for the chemokine receptor, evidence for a conformational change upon CD4 binding, the nature of a CD4-induced antibody epitope, and specific mechanisms for immune evasion.
Antibody cross-competition analysis of the human immunodeficiency virus type 1 gp120 exterior envelope glycoprotein
Forty-six monoclonal antibodies (MAbs) able to bind to the native, monomeric gp120 glycoprotein of the human immunodeficiency virus type 1 (HIV-1) LAI (HXBc2) strain were used to generate a
Human immunodeficiency virus type 1 neutralization is determined by epitope exposure on the gp120 oligomer
TLDR
With the exception of the hypervariable V3 loop, regions of HIV-1 gp120 with the potential to induce a neutralization response are likely to be poorly presented for antibody recognition on the surface of cell line-adapted virions.
Analysis of the interaction of the human immunodeficiency virus type 1 gp120 envelope glycoprotein with the gp41 transmembrane glycoprotein
TLDR
The gp41 interface on the HIV-1 gp120 glycoprotein, which elicits nonneutralizing antibodies, can be removed while retaining immunologically desirable gp120 structures.
Discontinuous, conserved neutralization epitopes overlapping the CD4-binding region of human immunodeficiency virus type 1 gp120 envelope glycoprotein
TLDR
Results indicate that the CD4 receptor and this group of broadly neutralizing antibodies recognize distinct but overlapping gp120 determinants.
Involvement of the V1/V2 variable loop structure in the exposure of human immunodeficiency virus type 1 gp120 epitopes induced by receptor binding.
TLDR
The results suggest that the V1/V2 loops, which have been previously implicated in CD4-modulated, postattachment steps in HIV-1 entry, contribute toCD4-induced gp120 conformational changes detected by the 17b, 48d, and A32 antibodies.
Characterization of conserved human immunodeficiency virus type 1 gp120 neutralization epitopes exposed upon gp120-CD4 binding
TLDR
Results suggest that discontinuous, conserved epitopes proximal to the binding sites for both CD4 and anti-CD4 binding antibodies become better exposed upon CD4 binding and can serve as targets for neutralizing antibodies.
Conformational epitope on gp120 important in CD4 binding and human immunodeficiency virus type 1 neutralization identified by a human monoclonal antibody.
TLDR
Characterization of the 15e epitope shows that it is conformation dependent and is distinct from previously recognized functional domains of gp120, suggesting that this epitope represents a novel site important for HIV-1 neutralization and CD4 binding.
Human monoclonal antibody 2G12 defines a distinctive neutralization epitope on the gp120 glycoprotein of human immunodeficiency virus type 1
TLDR
Human monoclonal antibody 2G12 to the gp120 surface glycoprotein of human immunodeficiency virus type 1 (HIV-1) potently and broadly neutralizes primary and T-cell line-adapted clade B strains of HIV-1 and inhibits syncytium formation in the AA-2 cell line.
Functional and immunologic characterization of human immunodeficiency virus type 1 envelope glycoproteins containing deletions of the major variable regions
TLDR
The results indicate that, in addition to playing essential roles in the induction of membrane fusion, the major variable regions mask conserved neutralization epitopes of the HIV-1 gp120 glycoprotein from antibodies.
...
1
2
3
...