Distinct conformational states of HIV-1 gp41 are recognized by neutralizing and non-neutralizing antibodies

A number of antibodies against the membrane-proximal region of HIV-1 gp41 cannot neutralize the virus, despite their high affinity. Now binding studies along with a crystal structure indicate that these non-neutralizing antibodies recognize gp41 in a post-fusion conformation. HIV-1 envelope glycopro...

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Veröffentlicht in:	Nature structural & molecular biology 2010-12, Vol.17 (12), p.1486-1491
Hauptverfasser:	Frey, Gary, Chen, Jia, Rits-Volloch, Sophia, Freeman, Michael M, Zolla-Pazner, Susan, Chen, Bing
Format:	Artikel
Sprache:	eng
Schlagworte:	631/45/612/1256 631/535 631/57/2272/2273 Antibodies, Monoclonal - chemistry Antibodies, Monoclonal - physiology Antibodies, Neutralizing - chemistry Antibodies, Neutralizing - immunology Antibodies, Viral - chemistry Antibodies, Viral - immunology Biochemistry Biological Microscopy Biomedical and Life Sciences Care and treatment Cellular biology Crystallography, X-Ray Genetic aspects Glycoproteins HIV HIV Envelope Protein gp41 - chemistry HIV Envelope Protein gp41 - immunology HIV infection HIV-1 - immunology Human immunodeficiency virus Human immunodeficiency virus 1 Humans Immunity, Humoral Immunoglobulin Fab Fragments - chemistry Immunoglobulin Fab Fragments - physiology Life Sciences Membrane Biology Membranes Models, Molecular Molecular structure Physiological aspects Protein Structure Protein Structure, Tertiary Risk factors Vaccines Virus Internalization
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