Antibody responses to envelope glycoproteins in HIV-1 infection

• Published in: Nature immunology Vol. 16; no. 6; pp. 571 - 576
• Main Authors: Burton, Dennis R, Mascola, John R
• Format: Journal Article
• Language: English
• Published: New York Nature Publishing Group US 01.06.2015; Nature Publishing Group
• Subjects: 631/250/2152/2153/1291; 631/250/255/1901; AIDS Vaccines - immunology; Animal models; Animals; Antibodies; Antibodies, Neutralizing - immunology; Antibody Formation; Biomedicine; Disease Models, Animal; env Gene Products, Human Immunodeficiency Virus - immunology; Glycoproteins; Health aspects; HIV Antibodies - immunology; HIV infection; HIV Infections - immunology; HIV Infections - therapy; HIV-1 - immunology; Human immunodeficiency virus 1; Humans; Immunology; Immunotherapy; Infectious Diseases; Lentivirus; Physiological aspects; review-article; Viral antibodies
• ISSN: 1529-2908; 1529-2916
• DOI: 10.1038/ni.3158

Antibody responses to the HIV-1 envelope glycoproteins can be classified into three groups. Burton and Mascola discuss how recent insight into the structure and immunology of non-neutralizing, strain-specific and broadly neutralizing antibodies guide HIV-1 vaccine design and therapeutic strategies. Antibody responses to the HIV-1 envelope glycoproteins can be classified into three groups. Binding but non-neutralizing responses are directed to epitopes that are expressed on isolated envelope glycoproteins but not on the native envelope trimer found on the surface of virions and responsible for mediating the entry of virus into target cells. Strain-specific responses and broadly neutralizing responses, in contrast, target epitopes that are expressed on the native trimer, as revealed by recently resolved structures. The past few years have seen the isolation of many broadly neutralizing antibodies of remarkable potency that have shown prophylactic and therapeutic activities in animal models. These antibodies are helping to guide rational vaccine design and therapeutic strategies for HIV-1.