Maturation-Dependent HIV-1 Surface Protein Redistribution Revealed by Fluorescence Nanoscopy

Author:

Chojnacki Jakub1,Staudt Thorsten2,Glass Bärbel1,Bingen Pit2,Engelhardt Johann2,Anders Maria1,Schneider Jale2,Müller Barbara1,Hell Stefan W.23,Kräusslich Hans-Georg1

Affiliation:

1. Department of Infectious Diseases, Virology, Heidelberg University, Im Neuenheimer Feld 324, 69120 Heidelberg, Germany.

2. Optical Nanoscopy Division, German Cancer Research Center (DKFZ), Im Neuenheimer Feld 280, 69120 Heidelberg, Germany, and BIOQUANT, Im Neuenheimer Feld 267, 69120 Heidelberg, Germany.

3. Department of NanoBiophotonics, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany.

Abstract

Switching on HIV Newly assembled human immunodeficiency virus (HIV) virions bud from the host cell as immature particles. Proteolysis of the Gag protein, which forms a structural lattice below the viral membrane, leads to the formation of mature infectious HIV. Fusion of mature HIV virions with a target cell is mediated by viral envelope (Env) proteins that occur in trimeric “spikes” on the surface of the virion. Chojnacki et al. (p. 524 ) used subdiffraction microscopy to show that the spikes were dispersed on the immature virion but clustered into a single focus on the mature virion. The clustering was important for infectivity. Coupling Gag proteolysis with clustering may ensure that only particles whose interior has switched to the entry mode are competent for membrane fusion.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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