Cleavage of recombinant and cell derived human immunodeficiency virus 1 (HIV‐1) Nef protein by HIV‐1 protease

Gaedigk-Nitschko, Kerstin; Schön, Annemarie; Wachinger, G.; Erfle, Volker; Kohleisen, Birgit

doi:10.1016/0014-5793(94)01370-g

Cited by 29 publications

(22 citation statements)

References 27 publications

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“…Although Nef clearly acts in the virus producer cell to modify the virion, no Nef-dependent structural or biochemical alterations of HIV-1 virions have been reported. Instead, Nef itself is packaged into virions (6,24,30,32), associated with the viral core (19), and cleaved by the viral protease (6,7,14,15,21,23). These studies suggest that Nef plays a role in an early postentry process of HIV infection and are consistent with the hypothesis that Nef regulates the disassembly of the viral core.…”

supporting

confidence: 60%

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Disassembly of Human Immunodeficiency Virus Type 1 Cores In Vitro Reveals Association of Nef with the Subviral Ribonucleoprotein Complex

Forshey

Aiken

2003

J Virol

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The human immunodeficiency virus type 1 (HIV-1) virulence factor Nef enhances viral infectivity in singlecycle infection assays and accelerates HIV-1 replication in vitro. It has been reported that the effects of Nef are mediated early after viral entry and before the completion of reverse transcription, as viral DNA synthesis is strongly attenuated during infection by Nef-defective virions. Our previous work has demonstrated that Nef is associated with mature HIV-1 cores, implicating Nef in the regulation of HIV-1 core stability. Here we report a comparative analysis of HIV-1 cores isolated from wild-type and Nef-defective particles. We observed no effect of Nef on HIV-1 core structure or stability; however, Nef cosedimented with a subviral ribonucleoprotein complex following dissociation of CA. These results indicate that Nef interacts tightly with an internal component of the HIV-1 core. They further suggest that virion-associated Nef may facilitate an early step in HIV-1 infection following dissociation of the viral capsid in the target cell.

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supporting

confidence: 60%

“…Previous reports have demonstrated that Nef is cleaved within the virion by the viral protease. Cleavage occurs between residues 57 and 58, releasing a 20-kDa "core" domain from the 7-kDa amino- terminal "linker" domain (6,7,14,15,21,23,24). Both intact and 20-kDa cleaved forms remained in pelletable form consistently throughout the incubation time course.…”

mentioning

confidence: 99%

Disassembly of Human Immunodeficiency Virus Type 1 Cores In Vitro Reveals Association of Nef with the Subviral Ribonucleoprotein Complex

Forshey

Aiken

2003

J Virol

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“…This relatively small amount of virion-associated Nef is likely insufficient to produce enough peptide ligand for presentation by MHC-I molecules. Additionally, Nef is proteolytically cleaved by the viral protease in the maturing virus particle (10,13), which might interfere with antigen processing. However, it has been demonstrated that HLA alleles that bind N-terminal dibasic peptides, such as HLA-B27, can present peptides from antigen present in amounts insufficient for presentation by other MHC-I molecules (15).…”

Section: Discussionmentioning

confidence: 99%

Pol-Specific CD8 ⁺ T Cells Recognize Simian Immunodeficiency Virus-Infected Cells Prior to Nef-Mediated Major Histocompatibility Complex Class I Downregulation

Sacha

Chung²,

Reed³

et al. 2007

J Virol

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“…This strong sequence context dependence also raises difficulties for predicting cleavage sites. For example, an early prediction method developed by Poorman et al (7) failed to predict the cleavage site in Nef protein (34). New prediction methods that take into account the context-dependent nature FIG.…”

Section: Discussionmentioning

confidence: 99%

Studies on the Symmetry and Sequence Context Dependence of the HIV-1 Proteinase Specificity

Tőzsér¹,

Bagossi²,

Weber³

et al. 1997

Journal of Biological Chemistry

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Two major types of cleavage sites with different sequence preferences have been proposed for the human immunodeficiency virus type 1 (HIV-1) proteinase. To understand the nature of these sequence preferences better, single and multiple amino acid substitutions were introduced into a type 1 cleavage site peptide, thus changing it to a naturally occurring type 2 cleavage site sequence. Our results indicated that the previous classification of the retroviral cleavage sites may not be generally valid and that the preference for a residue at a particular position in the substrate depends strongly on the neighboring residues, including both those at the same side and at the opposite side of the peptide backbone of the substrate. Based on these results, pseudosymmetric (palindromic) substrates were designed. The retroviral proteinases are symmetrical dimers of two identical subunits; however, the residues of naturally occurring cleavage sites do not show symmetrical arrangements, and no obvious symmetrical substrate preference has been observed for the specificity of HIV proteinase. To examine the role of the asymmetry created by the peptide bonds on the specificity of the respective primed and nonprimed halves of the binding site, amino acid substitutions were introduced into a palindromic sequence. In general, the results suggested that the asymmetry does not result in substantial differences in specificity of the S 3 and S 3 subsites, whereas its effect is more pronounced for the S 2 and S 2 subsites. Although it was possible to design several good palindromic substrates, asymmetrical arrangements may be preferred by the HIV proteinase.

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Cleavage of recombinant and cell derived human immunodeficiency virus 1 (HIV‐1) Nef protein by HIV‐1 protease

Cited by 29 publications

References 27 publications

Disassembly of Human Immunodeficiency Virus Type 1 Cores In Vitro Reveals Association of Nef with the Subviral Ribonucleoprotein Complex

Disassembly of Human Immunodeficiency Virus Type 1 Cores In Vitro Reveals Association of Nef with the Subviral Ribonucleoprotein Complex

Pol-Specific CD8 ⁺ T Cells Recognize Simian Immunodeficiency Virus-Infected Cells Prior to Nef-Mediated Major Histocompatibility Complex Class I Downregulation

Studies on the Symmetry and Sequence Context Dependence of the HIV-1 Proteinase Specificity

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Cleavage of recombinant and cell derived human immunodeficiency virus 1 (HIV‐1) Nef protein by HIV‐1 protease

Cited by 29 publications

References 27 publications

Disassembly of Human Immunodeficiency Virus Type 1 Cores In Vitro Reveals Association of Nef with the Subviral Ribonucleoprotein Complex

Disassembly of Human Immunodeficiency Virus Type 1 Cores In Vitro Reveals Association of Nef with the Subviral Ribonucleoprotein Complex

Pol-Specific CD8 + T Cells Recognize Simian Immunodeficiency Virus-Infected Cells Prior to Nef-Mediated Major Histocompatibility Complex Class I Downregulation

Studies on the Symmetry and Sequence Context Dependence of the HIV-1 Proteinase Specificity

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Pol-Specific CD8 ⁺ T Cells Recognize Simian Immunodeficiency Virus-Infected Cells Prior to Nef-Mediated Major Histocompatibility Complex Class I Downregulation