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Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
- P. Kwong, R. Wyatt, James E. Robinson, R. Sweet, J. Sodroski, W. Hendrickson
- 18 June 1998
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.
Rational Design of Envelope Identifies Broadly Neutralizing Human Monoclonal Antibodies to HIV-1
Three broadly neutralizing antibodies are identified, isolated from an HIV-1–infected individual, that exhibited great breadth and potency of neutralization and were specific for the co-receptor CD4-binding site of the glycoprotein 120 (gp120), part of the viral Env spike.
Antibody neutralization and escape by HIV-1
The detection of autologous Nab as early as 52 days after detection of HIV-specific antibodies is reported, indicating a new mechanism contributing to HIV-1 persistence in the face of an evolving antibody repertoire.
Antibody Resistance of SARS-CoV-2 Variants B.1.351 and B.1.1.7
The recent emergence of new SARS-CoV-2 variants B.1.2.351 and emergent variants13,14 with similar spike mutations present new challenges for mAb therapy and threaten the protective efficacy of current vaccines.
Structural basis of cell-cell adhesion by cadherins
A linear zipper of molecules that mirrors the linear structure of the intracellular filaments with which cadherins associate may provide a mechanism to marshal individual molecular adhesive interactions into strong bonds between cells.
Structure of a V3-Containing HIV-1 gp120 Core
The third variable region (V3) of the HIV-1 gp120 envelope glycoprotein is immunodominant and contains features essential for coreceptor binding, which provides a structural rationale for the role of V3 in HIV entry and neutralization.
Broad and potent neutralization of HIV-1 by a gp41-specific human antibody
The structure of 10E8 in complex with the complete MPER revealed a site of vulnerability comprising a narrow stretch of highly conserved gp41-hydrophobic residues and a critical arginine or lysine just before the transmembrane region, suggesting the importance of these residues for neutralization.
Potent neutralizing antibodies against multiple epitopes on SARS-CoV-2 spike
A diverse collection of potent neutralizing antibodies against the SARS-CoV-2 spike protein have been isolated from five patients with severe COVID-19 and high serum neutralization titres, suggesting both of these regions at the top of the viral spike are immunogenic.
Structural Basis for Broad and Potent Neutralization of HIV-1 by Antibody VRC01
The identification of three broadly neutralizing antibodies, isolated from an HIV-1–infected individual, that exhibited great breadth and potency of neutralization and were specific for the co-receptor CD4-binding site of the glycoprotein 120 (gp120), part of the viral Env spike.
The antigenic structure of the HIV gp120 envelope glycoprotein
The spatial organization of conserved neutralization epitopes on gp120 is described, using epitope maps in conjunction with the X-ray crystal structure of a ternary complex that includes a gp120 core, CD4 and a neutralizing antibody.