Annexin 2: a Novel Human Immunodeficiency Virus Type 1 Gag Binding Protein Involved in Replication in Monocyte-derived Macrophages.
From: Department of Neurology and Microbiology, University of Pennsylvania, 3 W. Gates, 3400 Spruce Street, Philadelphia, Pennsylvania 19104-4283, USA.
Journal of virology
- Publish Date: Mar 2006
- ISSN: 0022-538X
- Volume: 80
- Issue: 6
- Pages: 2694-704
- Medium: Print
- Language: English
- Citation (JAMA): Ryzhova Elena V, Vos Robin M, Albright Andrew V, et al. Annexin 2: a Novel Human Immunodeficiency Virus Type 1 Gag Binding Protein Involved in Replication in Monocyte-derived Macrophages.. J. Virol. Mar 2006;80:2694-704
Abstract
Human immunodeficiency virus (HIV) replication in the major natural target cells, CD4+ T lymphocytes and macrophages, is parallel in many aspects of the virus life cycle. However, it differs as to viral assembly and budding, which take place on plasma membranes in T cells and on endosomal membranes in macrophages. It has been postulated that cell type-specific host factors may aid in directing viral assembly to distinct destinations. In this study we defined annexin 2 (Anx2) as a novel HIV Gag binding partner in macrophages. Anx2-Gag binding was confined to productively infected macrophages and was not detected in quiescently infected monocyte-derived macrophages (MDM) in which an HIV replication block was mapped to the late stages of the viral life cycle (A. V. Albright, R. M. Vos, and F. Gonzalez-Scarano, Virology 325:328-339, 2004). We demonstrate that the Anx2-Gag interaction likely occurs at the limiting membranes of late endosomes/multivesicular bodies and that Anx2 depletion is associated with a significant decline in the infectivity of released virions; this coincided with incomplete Gag processing and inefficient incorporation of CD63. Cumulatively, our data suggest that Anx2 is essential for the proper assembly of HIV in MDM.
Mesh Headings (Keywords): Annexin A2, Antigens, CD, Cells, Cultured, Gene Products, gag, Genes, gag, HIV-1, Humans, Macrophages, Platelet Membrane Glycoproteins, Protein Precursors, Virus Assembly, Virus Replication
Check for Full Text / PubMed Unique Identifier (PMID): 16501079
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