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By comparing HIV-1 variants from people who became infected at the beginning of the epidemic and from people who have recently contracted the virus, we observed an enhanced resistance of the virus to antibody neutralization over time, accompanied by an increase in the length of the variable loops and in the number of potential N-linked glycosylation sites on the HIV-1 envelope gp120 subunit. The enhanced neutralization resistance of HIV-1 in contemporary seroconverters coincided with the poorer elicitation of neutralizing antibody responses, which may have implications for vaccine design.

Original publication

DOI

10.1038/nm.2203

Type

Journal

Nature medicine

Publication Date

09/2010

Volume

16

Pages

995 - 997

Addresses

Department of Experimental Immunology, Sanquin Research, Landsteiner Laboratory, Center for Infection and Immunity Amsterdam, Academic Medical Center, University of Amsterdam, Amsterdam, The Netherlands.

Keywords

Humans, HIV, HIV Infections, Immunoglobulins, Intravenous, HIV Envelope Protein gp120, Viral Envelope Proteins, AIDS Vaccines, HIV Antibodies, Neutralization Tests, Antibody Formation, Genetic Variation, Immunity, Humoral