Literature DB >> 8661406

HIV-1 Gag protein associates with F-actin present in microfilaments.

O Rey1, J Canon, P Krogstad.   

Abstract

Several studies have provided evidence that the cellular cytoskeleton may be involved in the assembly and budding of retroviruses. In fractionation studies of HIV-1-infected CEM cells, the majority of the unprocessed Gag polyprotein cofractionated with the cellular cytoskeleton. In vivo and in vitro analyses of this interaction indicated that the unprocessed Gag polyprotein is capable of association with polymerized actin (F-actin). Binding of Gag to F-actin may be involved in the assembly or budding of HIV-1.

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Year:  1996        PMID: 8661406     DOI: 10.1006/viro.1996.0343

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


  48 in total

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Review 4.  Retroviral proteins that interact with the host cell cytoskeleton.

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Authors:  T Wilk; B Gowen; S D Fuller
Journal:  J Virol       Date:  1999-03       Impact factor: 5.103

8.  Identification of retroviral late domains as determinants of particle size.

Authors:  L Garnier; L J Parent; B Rovinski; S X Cao; J W Wills
Journal:  J Virol       Date:  1999-03       Impact factor: 5.103

9.  Cryoelectron microscopic examination of human immunodeficiency virus type 1 virions with mutations in the cyclophilin A binding loop.

Authors:  L B Kong; D An; B Ackerson; J Canon; O Rey; I S Chen; P Krogstad; P L Stewart
Journal:  J Virol       Date:  1998-05       Impact factor: 5.103

10.  The HIV envelope but not VSV glycoprotein is capable of mediating HIV latent infection of resting CD4 T cells.

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