Identification of amino acid substitutions associated with neutralization phenotype in the human immunodeficiency virus type-1 subtype C gp120

Kirchherr, Jennifer L. and Hamilton, Jennifer and Lu, Xiaozhi and Gnanakaran, S. and Muldoon, Mark and Daniels, Marcus and Kasongo, Webster and Chalwe, Victor and Mulenga, Chanda and Mwananyanda, Lawrence and Musonda, Rosemary M. and Yuan, Xing and Montefiori, David C. and Korber, Bette T. and Haynes, Barton F. and Gao, Feng (2011) Identification of amino acid substitutions associated with neutralization phenotype in the human immunodeficiency virus type-1 subtype C gp120. Virology, 409 (2). pp. 163-174.

[img] PDF
KirchherrHamiltonKorberHaynesGao_JVirol409.pdf
Restricted to Repository staff only

Download (1MB)

Abstract

Neutralizing antibodies (Nabs) are thought to play an important role in prevention and control of HIV-1 infection and should be targeted by an AIDS vaccine. It is critical to understand how HIV-1 induces Nabs by analyzing viral sequences in both tested viruses and sera. Neutralization susceptibility to antibodies in autologous and heterologous plasma was determined for multiple Envs (3�6) from each of 15 subtype-C- infected individuals. Heterologous neutralization was divided into two distinct groups: plasma with strong, cross-reactive neutralization (n = 9) and plasma with weak neutralization (n = 6). Plasma with cross-reactive heterologous Nabs also more potently neutralized contemporaneous autologous viruses. Analysis of Env sequences in plasma from both groups revealed a three-amino-acid substitution pattern in the V4 region that was associated with greater neutralization potency and breadth. Identification of such potential neutralization signatures may have important implications for the development of HIV-1 vaccines capable of inducing Nabs to subtype C HIV-1.

Item Type: Article
Subjects: MSC 2010, the AMS's Mathematics Subject Classification > 92 Biology and other natural sciences
Depositing User: Dr Mark Muldoon
Date Deposited: 24 Jan 2011
Last Modified: 20 Oct 2017 14:12
URI: http://eprints.maths.manchester.ac.uk/id/eprint/1570

Actions (login required)

View Item View Item