Literature DB >> 31055063

HIV-1 matrix mutations that alter gag membrane binding modulate mature core formation and post-entry events.

Yuta Hikichi1, Eri Takeda2, Masayuki Fujino3, Emi Nakayama4, Tetsuro Matano5, Tsutomu Murakami6.   

Abstract

The matrix (MA) domain of HIV-1 Gag directs membrane binding of the Gag precursor polyprotein during the late events of virus replication. However, the effects of alteration in Gag membrane binding early post-infection are not well understood. To investigate impacts of MA mutations that alter Gag membrane binding on the phenotypes of newly produced virus particles, we extensively characterized two MA mutants by virological, biochemical, and morphological approaches. The V6R mutation, which decreases Gag membrane binding, modified Gag processing and core morphogenesis and impaired core uncoating, reverse transcription, and viral DNA integration. On the other hand, the L20K mutation, which increases Gag membrane binding, primarily decreased integrated DNA levels without affecting the viral components and morphology. These data suggest that HIV-1 MA plays roles in functional core formation and the following post-entry steps of the virus replication cycle. (140/150 words).
Copyright © 2019 Elsevier Inc. All rights reserved.

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Keywords:  Core formation; Gag; HIV-1; Integration; Matrix; Membrane binding; Post entry; Reverse transcription; Uncoating

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Year:  2019        PMID: 31055063     DOI: 10.1016/j.virol.2019.04.013

Source DB:  PubMed          Journal:  Virology        ISSN: 0042-6822            Impact factor:   3.616


  1 in total

1.  Discovery of Dehydroamino Acid Residues in the Capsid and Matrix Structural Proteins of HIV-1.

Authors:  Rachel M Miller; Rachel A Knoener; Bayleigh E Benner; Brian L Frey; Mark Scalf; Michael R Shortreed; Nathan M Sherer; Lloyd M Smith
Journal:  J Proteome Res       Date:  2022-02-22       Impact factor: 4.466

  1 in total

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