The Role of Antibody Polyspecificity and Lipid Reactivity in Binding of Broadly Neutralizing Anti-HIV-1 Envelope Human Monoclonal Antibodies 2F5 and 4E10 to Glycoprotein 41 Membrane Proximal Envelope Epitopes-Reference-Cited by-同舟云学术

The Role of Antibody Polyspecificity and Lipid Reactivity in Binding of Broadly Neutralizing Anti-HIV-1 Envelope Human Monoclonal Antibodies 2F5 and 4E10 to Glycoprotein 41 Membrane Proximal Envelope Epitopes

Published:2007-03-19 Issue:7 Volume:178 Page:4424-4435
ISSN:0022-1767
Container-title:The Journal of Immunology
language:en
Short-container-title:J Immunol

Author:

Alam S. Munir,McAdams Mildred,Boren David,Rak Michael,Scearce Richard M.,Gao Feng,Camacho Zenaido T.,Gewirth Daniel,Kelsoe Garnett,Chen Pojen,Haynes Barton F.

Publisher

The American Association of Immunologists

Subject

Immunology,Immunology and Allergy

Reference56 articles.

1. Structure and Mechanistic Analysis of the Anti-Human Immunodeficiency Virus Type 1 Antibody 2F5 in Complex with Its gp41 Epitope

2. Broadly Neutralizing Anti-HIV Antibody 4E10 Recognizes a Helical Conformation of a Highly Conserved Fusion-Associated Motif in gp41

3. A Potent Cross-Clade Neutralizing Human Monoclonal Antibody against a Novel Epitope on gp41 of Human Immunodeficiency Virus Type 1

4. Evaluation of Monoclonal Antibodies to Human Immunodeficiency Virus Type 1 Primary Isolates by Neutralization Assays: Performance Criteria for Selecting Candidate Antibodies for Clinical Trials

5. Structural Analysis of the Epitope of the Anti-HIV Antibody 2F5 Sheds Light into Its Mechanism of Neutralization and HIV Fusion

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