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How HIV-1 hijacks ALIX

Nature Structural & Molecular Biology volume 14, pages 254–256 (2007)Cite this article

Two new crystal structures shed light on how a component of the endosomal budding machinery is co-opted by human immunodeficiency virus-1 to facilitate virus budding from the cell surface.

Whereas some viruses rely on host-cell lysis for their release, retroviruses such as human immunodeficiency virus-1 (HIV-1) are released by budding through a cellular membrane, typically the plasma membrane. Over the last couple of years, it has become clear that retroviral budding depends on the engagement of a complex network of host endosomal sorting proteins that includes TSG101 and ALIX (also called AIP1)1,2. Two recent papers now provide insights at the structural level as to how ALIX binds HIV-1 and connects to downstream components of the cellular budding machinery3,4.

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Figure 1: Domain organization and structure of ALIX.

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Authors and Affiliations

  1. Heinrich G. Göttlinger is in the Program in Gene Function and Expression, Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, Massachusetts 01605, USA. heinrich.gottlinger@umassmed.edu,

    Heinrich G Göttlinger

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Göttlinger, H. How HIV-1 hijacks ALIX. Nat Struct Mol Biol 14, 254–256 (2007). https://doi.org/10.1038/nsmb0407-254

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