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First published online December 17, 2008

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ERM – actin' in HIV-1 infection

Before HIV-1 can enter target cells, the viral envelope glycoprotein Env must first interact simultaneously with the cell-surface receptors CD4 and either CCR5 or CXCR4. Little is known about how HIV-1 induces CD4 and CXCR4 to redistribute and cluster together, although F-actin and its regulatory proteins are thought to have an important role. On page 103, Francisco Sánchez-Madrid and colleagues report on how ERM proteins – which link membrane-associated proteins and the actin cytoskeleton – function in HIV-1 attachment. The authors show that the ERM proteins ezrin and moesin are phosphorylated (and thereby activated) in response to viral particles or the envelope protein gp120. This phosphorylation is observed both in a CD4⁺ CXCR4⁺ T-cell line and in primary lymphocytes, and requires an interaction between gp120 and CD4 (but not CXCR4). The authors next report that activated moesin promotes CD4-CXCR4 interaction, as well as the redistribution of CD4-CXCR4 and F-actin to sites of contact between HIV-1 and target cells. Importantly, knocking down moesin or expressing a dominant-negative moesin mutant impedes F-actin reorganisation and HIV-1 infection. The authors conclude, therefore, that the activation of moesin is a key step in Env-mediated HIV-1 internalisation.

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Moesin is required for HIV-1-induced CD4-CXCR4 interaction, F-actin redistribution, membrane fusion and viral infection in lymphocytes

Marta Barrero-Villar, José Román Cabrero, Mónica Gordón-Alonso, Jonathan Barroso-González, Susana Álvarez-Losada, M. Ángeles Muñoz-Fernández, Francisco Sánchez-Madrid, and Agustín Valenzuela-Fernández
JCS 2009 122: 103-113. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?