Immunological and Chemical Analysis of P6, the Carboxyl-Terminal Fragment of HIV P15

Veronese, Fulvia; Rahman, Rukhsana; Copeland, Terry D.; Oroszlan, Stephen; Gallo, Robert C.; Sarngadharan, M. G.

doi:10.1089/aid.1987.3.253

Cited by 99 publications

(23 citation statements)

References 8 publications

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“…analyses suggested that the C-terminal domain of Gag, which is processed in NCp7 and p6 (15), could interact with Vpr. Moreover, both the C and the N termini of Vpr were reported to be necessary for the incorporation of this protein in the virus particles (10,24,25).…”

Section: In Vitro Interactions Of Vpr With Ncp7 But Not P6 and Importmentioning

confidence: 99%

“…The involvement of NCp7 in Vpr encapsidation would raise the question of the coexistence of NCp7-Vpr complexes with those resulting from the binding of genomic RNA to the nucleocapsid domain of Gag, a process known to be critical for RNA packaging (15,18). Fluorescence and NMR studies have shown that the zinc finger domains of NC proteins participate in the RNA binding (40,41), a finding supported by the observed reduction in RNA packaging of HIV-1 mutants with defects in the structure of the zinc fingers (37)(38)(39).…”

Section: Fig 6 Ratio Of Virion-incorporated Vprmentioning

confidence: 99%

“…Vpr is present in virions, and its encapsidation has been reported to be dependent on the presence of NCp15, the C-terminal part of the polyprotein Gag (8 -14). In the virions, NCp15 is cleaved by the viral protease to form NCp7 and p6 (15). NCp7 is a small basic protein of 72 amino acids (see Fig.…”

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confidence: 99%

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The Zinc Fingers of HIV Nucleocapsid Protein NCp7 Direct Interactions with the Viral Regulatory Protein Vpr

Rocquigny

Petitjean

Tanchou

et al. 1997

Journal of Biological Chemistry

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The 96-amino acid protein Vpr functions as a regulator of cellular processes involved in human immunodeficiency virus, type 1 (HIV-1) life cycle, in particular by interrupting cells division in the G 2 phase. Incorporation of Vpr in the virion was reported to be mediated by the C-terminal domain of the Pr55Gag polyprotein precursor, which includes NCp7, a protein involved in the genomic RNA encapsidation and p6, a protein required for particle budding. To precisely define the Gag and Vpr sequences involved in this protein-protein interaction, NCp7, p6, and Vpr as well as a series of derived peptides were synthesized using Fmoc (N-(9-fluorenyl)-methoxycarbonyl) chemistry. Binding assays were carried out by Far Western experiments and by competition studies using (52-96)Vpr immobilized onto agarose beads. The results show that interaction between NCp7 and Vpr occurs in vitro by a recognition mechanism requiring the zinc fingers of NCp7 and the last 16 amino acids of Vpr. Moreover, NCp10, the equivalent of NCp7 in Moloney murine leukemia virus but not polysine inhibits Vpr-NCp7 complexation. Interestingly enough, Vpr was found to interact with Gag, NCp15, and NCp7 but not with mature p6 in vitro. In vivo mutations in NCp7 zinc fingers in an HIV-1 molecular clone led to viruses with important defects in Vpr encapsidation. Together, these results suggest that NCp7 cooperates with p6 to induce Vpr encapsidation in HIV-1 mature particles. The NCp7-Vpr complex could also be important for interaction of Vpr with cellular proteins involved in cell division.

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Section: In Vitro Interactions Of Vpr With Ncp7 But Not P6 and Importmentioning

confidence: 99%

Section: Fig 6 Ratio Of Virion-incorporated Vprmentioning

confidence: 99%

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The Zinc Fingers of HIV Nucleocapsid Protein NCp7 Direct Interactions with the Viral Regulatory Protein Vpr

Rocquigny

Petitjean

Tanchou

et al. 1997

Journal of Biological Chemistry

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“…Cleavage of HIV-1 Pr55m by the viral protease occurs during virion formation and yields the major core proteins-namely, matrix (MA), capsid (CA), and nucleocapsid (NC) proteins with molecular masses of 17 (p17), 24 (p24), and 7 (p7) kDa, respectively (7). Additionally, a 6-kDa proline-rich C-terminal protein, p6, is generated (8). While cleavage of HIV-1 Pr55m8 is necessary for the production of infectious virions, it is not required for budding to occur, as shown by viral protease inhibitor (9) and mutagenesis studies (10).…”

mentioning

confidence: 99%

“…A role for the C terminus of HIV-1 gag in virion assembly is suggested by mutagenesis studies in which C-terminal truncations of Pr55m prevent particle formation (8,(17)(18)(19). We theorized that these truncations may inhibit particle formation through abrogation of gag membrane association.…”

mentioning

confidence: 99%

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

Platt

Haffar

1994

Proc. Natl. Acad. Sci. U.S.A.

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Association of the human immunodeficiency virus type 1 (HIV-1) gag polyprotein precursor with cellular membranes is necessary for assembly of virions. We used in vitro synthesized HIV-1 gag to study its association with isolated cellular membranes. Rabbit reticulocyte lysates programmed with HIV-1 gag mRNA incorporated [35S]methionine and [3H]myristate into two predominant species of 55 kDa and 40 kDa. Radioimmunoprecipitation with HIV-1-specific antibodies suggested that the 55-kDa protein represented the polyprotein precursor (Pr55gag), while the 40-kDa protein was a mixture of N- or C-terminal truncations of the gag precursor. The Pr55gag protein bound to cellular membranes, while the 40-kDa mixed protein species did not. Membrane binding studies with C terminus-truncated and point mutants revealed that the seven-amino acid sequence located between the two Cys-His arrays in the nucleocapsid region was necessary for stable association to occur. Therefore, we propose that signals in addition to myristate are required for the membrane association of HIV-1 gag proteins and that these signals include a domain in the nucleocapsid protein.

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HIV-1 reverse transcriptase specifically interacts with the anticodon domain of its cognate primer tRNA.

et al. 1989

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The virion cores of the replication competent type 1 human immunodeficiency virus (HIV‐1), a retrovirus, contain and RNA genome associated with nucleocapsid (NC) and reverse transcriptase (RT p66/p51) molecules. In vitro reconstructions of these complexes with purified components show that NC is required for efficient annealing of the primer tRNALys,3. In the absence of NC, HIV‐1 RT is unable to retrotranscribe the viral RNA template from the tRNA primer. We demonstrate that the HIV‐1 RT p66/p51 specifically binds to its cognate primer tRNALys,3 even in the presence of a 100‐fold molar excess of other tRNAs. Cross‐linking analysis of this interaction locates the contact site to a region within the heavily modified anti‐codon domain of tRNALys,3.

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Immunological and Chemical Analysis of P6, the Carboxyl-Terminal Fragment of HIV P15

Cited by 99 publications

References 8 publications

The Zinc Fingers of HIV Nucleocapsid Protein NCp7 Direct Interactions with the Viral Regulatory Protein Vpr

The Zinc Fingers of HIV Nucleocapsid Protein NCp7 Direct Interactions with the Viral Regulatory Protein Vpr

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

HIV-1 reverse transcriptase specifically interacts with the anticodon domain of its cognate primer tRNA.

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