Literature DB >> 8460500

Identification of a region in the Pr55gag-polyprotein essential for HIV-1 particle formation.

A von Poblotzki1, R Wagner, M Niedrig, G Wanner, H Wolf, S Modrow.   

Abstract

The pr55gag polyprotein of HIV-1 plays a critical role in the formation of immature virus particles in the cell and during the budding process. We investigated the influence of amino acid substitutions in the p24CA- region of the gag polyprotein on the viral assembly process. Deletion of the amino acids 341-352 in the carboxy terminal part of the p24CA resulted in a loss of the capacity of the gag polyprotein to form virus-like particles when expressed in eucaryotic cells by recombinant vaccinia virus. In further experiments it turned out that the amino acids 341-346 and 350-352 are important for the ability of the pr55gag to form virus-like particles. Because these stretches are conserved among HIV-1, HIV-2, SIV, and FIV, we conclude that these amino acids form a domain highly important for the assembly of these lentiviruses.

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Year:  1993        PMID: 8460500     DOI: 10.1006/viro.1993.1210

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


  41 in total

1.  The dimer interfaces of protease and extra-protease domains influence the activation of protease and the specificity of GagPol cleavage.

Authors:  Steven C Pettit; Sergei Gulnik; Lori Everitt; Andrew H Kaplan
Journal:  J Virol       Date:  2003-01       Impact factor: 5.103

2.  Entropic switch regulates myristate exposure in the HIV-1 matrix protein.

Authors:  Chun Tang; Erin Loeliger; Paz Luncsford; Isaac Kinde; Dorothy Beckett; Michael F Summers
Journal:  Proc Natl Acad Sci U S A       Date:  2003-12-29       Impact factor: 11.205

3.  A new functional role of HIV-1 integrase during uncoating of the viral core.

Authors:  Marisa S Briones; Samson A Chow
Journal:  Immunol Res       Date:  2010-12       Impact factor: 2.829

4.  Effects of Gag mutation and processing on retroviral dimeric RNA maturation.

Authors:  William Fu; Que Dang; Kunio Nagashima; Eric O Freed; Vinay K Pathak; Wei-Shau Hu
Journal:  J Virol       Date:  2006-02       Impact factor: 5.103

5.  A putative alpha-helical structure which overlaps the capsid-p2 boundary in the human immunodeficiency virus type 1 Gag precursor is crucial for viral particle assembly.

Authors:  M A Accola; S Höglund; H G Göttlinger
Journal:  J Virol       Date:  1998-03       Impact factor: 5.103

6.  Sequential steps in human immunodeficiency virus particle maturation revealed by alterations of individual Gag polyprotein cleavage sites.

Authors:  K Wiegers; G Rutter; H Kottler; U Tessmer; H Hohenberg; H G Kräusslich
Journal:  J Virol       Date:  1998-04       Impact factor: 5.103

7.  The Vif and Gag proteins of human immunodeficiency virus type 1 colocalize in infected human T cells.

Authors:  J H Simon; R A Fouchier; T E Southerling; C B Guerra; C K Grant; M H Malim
Journal:  J Virol       Date:  1997-07       Impact factor: 5.103

8.  Inactivation of the human immunodeficiency virus type 1 inhibitory elements allows Rev-independent expression of Gag and Gag/protease and particle formation.

Authors:  R Schneider; M Campbell; G Nasioulas; B K Felber; G N Pavlakis
Journal:  J Virol       Date:  1997-07       Impact factor: 5.103

9.  p6Gag is required for particle production from full-length human immunodeficiency virus type 1 molecular clones expressing protease.

Authors:  M Huang; J M Orenstein; M A Martin; E O Freed
Journal:  J Virol       Date:  1995-11       Impact factor: 5.103

10.  The p6gag domain of human immunodeficiency virus type 1 is sufficient for the incorporation of Vpr into heterologous viral particles.

Authors:  E Kondo; F Mammano; E A Cohen; H G Göttlinger
Journal:  J Virol       Date:  1995-05       Impact factor: 5.103

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