Exploring converse molecular mechanisms of anti-HIV-1 antibodies using a synthetic CXCR4 mimic

Different molecular mechanisms of the two broadly neutralizing anti-HIV-1 antibodies b12 and VRC01, as evidenced by their converse effects on the interaction of HIV-1 envelope glycoprotein gp120 with cellular coreceptors, were demonstrated using a synthetic CXCR4 mimetic peptide (CX4-M1) as corecept...

Full description

Saved in:
Bibliographic Details
Published in:Bioorganic & medicinal chemistry letters 2012-10, Vol.22 (19), p.6099-6102
Main Authors: Haußner, Christina, Möbius, Kalle, Eichler, Jutta
Format: Article
Language:English
Subjects:
Antibiotics. Antiinfectious agents. Antiparasitic agents
Antibodies
Antibody
Antiviral agents
Biological and medical sciences
Coreceptor
CXCR4 protein
Envelopes
Glycoprotein gp120
glycoproteins
HIV - immunology
HIV Antibodies - chemistry
HIV Antibodies - immunology
HIV Envelope Protein gp120 - chemistry
HIV Envelope Protein gp120 - immunology
HIV-1
Human immunodeficiency virus 1
Medical sciences
Models, Molecular
Molecular Mimicry - immunology
Molecular modelling
neutralization
Peptide
Peptides - chemical synthesis
Peptides - chemistry
Peptides - immunology
Pharmacology. Drug treatments
Receptor mimic
Receptors, CXCR4 - immunology
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Different molecular mechanisms of the two broadly neutralizing anti-HIV-1 antibodies b12 and VRC01, as evidenced by their converse effects on the interaction of HIV-1 envelope glycoprotein gp120 with cellular coreceptors, were demonstrated using a synthetic CXCR4 mimetic peptide (CX4-M1) as coreceptor surrogate. While the interaction of gp120 with CX4-M1 was distinctly enhanced by VRC01, b12 was shown to have the contrary effect, and also to inhibit the VRC01-induced enhancement of gp120 binding to the CXCR4 mimetic peptide.
ISSN:0960-894X
1464-3405
DOI:10.1016/j.bmcl.2012.08.035