Literature DB >> 3481270

Immunological and chemical analysis of P6, the carboxyl-terminal fragment of HIV P15.

F D Veronese1, R Rahman, T D Copeland, S Oroszlan, R C Gallo, M G Sarngadharan.   

Abstract

The first open reading frame of the HIV genome has been identified as the gag gene. The proteins encoded by this gene are p17 as the amino-terminal protein, p24 as the middle peptide, and p15 as the carboxyl-terminal end. A monoclonal antibody recognizing an antigenic determinant on a fragment of p15 has been developed and designated M35/2F8. This monoclonal has been instrumental in radiosequencing the carboxyl-terminal product of p15, p6, and in determining the cleavage site between this protein and the amino-terminal product, p7. By immunoaffinity chromatography it was also possible to purify p6 from HIV lysates and all p6 containing polyproteins from HIV-infected cells. These results gave more insight into the composition and processing of the HIV gag gene.

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Year:  1987        PMID: 3481270     DOI: 10.1089/aid.1987.3.253

Source DB:  PubMed          Journal:  AIDS Res Hum Retroviruses        ISSN: 0889-2229            Impact factor:   2.205


  41 in total

1.  Determinants of the human immunodeficiency virus type 1 p15NC-RNA interaction that affect enhanced cleavage by the viral protease.

Authors:  N Sheng; S C Pettit; R J Tritch; D H Ozturk; M M Rayner; R Swanstrom; S Erickson-Viitanen
Journal:  J Virol       Date:  1997-08       Impact factor: 5.103

2.  Effect of mutations affecting the p6 gag protein on human immunodeficiency virus particle release.

Authors:  H G Göttlinger; T Dorfman; J G Sodroski; W A Haseltine
Journal:  Proc Natl Acad Sci U S A       Date:  1991-04-15       Impact factor: 11.205

3.  Mutations of RNA and protein sequences involved in human immunodeficiency virus type 1 packaging result in production of noninfectious virus.

Authors:  A Aldovini; R A Young
Journal:  J Virol       Date:  1990-05       Impact factor: 5.103

4.  Binding of human immunodeficiency virus type 1 (HIV-1) RNA to recombinant HIV-1 gag polyprotein.

Authors:  J Luban; S P Goff
Journal:  J Virol       Date:  1991-06       Impact factor: 5.103

5.  Human immunodeficiency virus type 1 Gag proteins are processed in two cellular compartments.

Authors:  A H Kaplan; R Swanstrom
Journal:  Proc Natl Acad Sci U S A       Date:  1991-05-15       Impact factor: 11.205

6.  Viral RNA annealing activities of human immunodeficiency virus type 1 nucleocapsid protein require only peptide domains outside the zinc fingers.

Authors:  H De Rocquigny; C Gabus; A Vincent; M C Fournié-Zaluski; B Roques; J L Darlix
Journal:  Proc Natl Acad Sci U S A       Date:  1992-07-15       Impact factor: 11.205

7.  Human immunodeficiency virus type 1 Pr55gag and Pr160gag-pol expressed from a simian virus 40 late replacement vector are efficiently processed and assembled into viruslike particles.

Authors:  A J Smith; M I Cho; M L Hammarskjöld; D Rekosh
Journal:  J Virol       Date:  1990-06       Impact factor: 5.103

8.  Replacement of the P1 amino acid of human immunodeficiency virus type 1 Gag processing sites can inhibit or enhance the rate of cleavage by the viral protease.

Authors:  Steve C Pettit; Gavin J Henderson; Celia A Schiffer; Ronald Swanstrom
Journal:  J Virol       Date:  2002-10       Impact factor: 5.103

9.  The p2 domain of human immunodeficiency virus type 1 Gag regulates sequential proteolytic processing and is required to produce fully infectious virions.

Authors:  S C Pettit; M D Moody; R S Wehbie; A H Kaplan; P V Nantermet; C A Klein; R Swanstrom
Journal:  J Virol       Date:  1994-12       Impact factor: 5.103

10.  Characterization of human immunodeficiency virus type 1 Pr55gag membrane association in a cell-free system: requirement for a C-terminal domain.

Authors:  E J Platt; O K Haffar
Journal:  Proc Natl Acad Sci U S A       Date:  1994-05-10       Impact factor: 11.205

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