Three-dimensional Structure of the Human Immunodeficiency Virus Type 1 Matrix Protein

Massiah, Michael A.; Starich, Mary R.; Paschall, Chiana M.; Summers, Michael F.; Christensen, Allyson M.; Sundquist, Wesley I.

doi:10.1006/jmbi.1994.1719

Cited by 260 publications

(309 citation statements)

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“…Myristate on the N terminus of recoverin is sequestered in a structure composed of five ␣-helices, which is similar to the ␣-helical structure of HIV-1 MA and that of M-PMV MA (9,17,38). Amino acid substitutions in recoverin that result in a less hydrophobic myristate-binding pocket have been shown to promote the calcium-induced conformation in which the myristate is extruded from the protein (3).…”

Section: Discussionmentioning

confidence: 99%

An Early Stage of Mason-Pfizer Monkey Virus Budding Is Regulated by the Hydrophobicity of the Gag Matrix Domain Core

Stansell

Tytler

Walter

et al. 2004

J Virol

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Intracellular capsid transport and release of Mason-Pfizer monkey virus are dependent on myristylation of the Gag matrix domain (MA). A myristylated MA mutant, in which Thr41 and Thr78 are replaced with isoleucines, assembles capsids that are transported to the plasma membrane but are blocked in an early budding step. Since the nuclear magnetic resonance structure of MA showed that these Thr residues point into the hydrophobic core of the protein, it was hypothesized that the T41I/T78I mutant was defective in release of myristic acid from the more hydrophobic core. In order to further investigate whether an increase in the hydrophobicity of the MA core modulates capsid-membrane interactions and viral budding, three tyrosine residues (11, 28, and 67), oriented toward the MA core, were replaced individually or in a pair-wise combination with the more hydrophobic phenylalanine residue(s). As a control, Tyr82, oriented toward the outer surface of MA, was also replaced with phenylalanine. These Tyr-to-Phe substitutions did not alter capsid assembly compared to wild type in a capsid assembly assay. Pulse-chase, immunofluorescence, and electron microscopy studies demonstrated that single substitutions of Tyr11, Tyr28, and Tyr67 recapitulated the T41I/T78I mutant phenotype of decreased budding kinetics and accumulation of capsids at the plasma membrane. MA double mutants with a combination of these Tyr substitutions exhibited a phenotype that was even more defective in budding. In contrast, MA mutants with Tyr82 replaced by Phe resulted in a transportdefective phenotype. These results strongly support the hypothesis that myristic acid is sequestered inside MA prior to capsid-membrane interactions.

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Section: Discussionmentioning

confidence: 99%

An Early Stage of Mason-Pfizer Monkey Virus Budding Is Regulated by the Hydrophobicity of the Gag Matrix Domain Core

Stansell

Tytler

Walter

et al. 2004

J Virol

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“…The ligands reported here could be used to characterize the molecular interactions between matrix and RNA, since at this time the nature of those interactions is not known. In the structures of the HIV-1 (41)(42)(43) and SIV matrix (44) proteins there is a patch of basic amino acids near the amino terminus that is located on one face of the protein. This region serves as the nuclear localization signal of matrix (8).…”

Section: Discussionmentioning

confidence: 99%

In vitro selection of RNAs that bind to the human immunodeficiency virus type-1 gag polyprotein

Lochrie

Waugh²,

Pratt³

et al. 1997

Nucleic Acids Research

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“…The recently determined structure of the p17 domain has been placed in the Gag structural cartoon (c) in the orientation suggested in the publications Matthews et al, Massiah et aL (1994).…”

Section: Discussionmentioning

confidence: 99%

Gag-Gag interactions in the C-terminal domain of human immunodeficiency virus type 1 p24 capsid antigen are essential for Gag particle assembly

Zhang¹,

Hockley

Nermut

et al. 1996

Journal of General Virology

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Seven internal deletions within the p24 domain of the human immunodeficiency virus type 1 Gag precursor have been assessed for their effect on Gag particle formation following their expression using recombinant baculoviruses. In addition, each deleted molecule was assessed for its ability to bind soluble p24 antigen in vitro. The mutants fell into three different phenotypic groups: (i) three mutants that had no effect on either p24 binding or Gag particle assembly, (ii) three mutants that abolished both features and (iii) one mutant that bound p24 in vitro but failed to assemble particles. Mutations that abolished both in vitro p24 binding and particle assembly mapped to the C terminus of p24 confirming this region as critical for virion assembly. We suggest the division of virion assembly into at least two distinct phases and suggest a model in which the critical sequences mapped to date are combined with available structural information.

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Three-dimensional Structure of the Human Immunodeficiency Virus Type 1 Matrix Protein

Cited by 260 publications

References 0 publications

An Early Stage of Mason-Pfizer Monkey Virus Budding Is Regulated by the Hydrophobicity of the Gag Matrix Domain Core

An Early Stage of Mason-Pfizer Monkey Virus Budding Is Regulated by the Hydrophobicity of the Gag Matrix Domain Core

In vitro selection of RNAs that bind to the human immunodeficiency virus type-1 gag polyprotein

Gag-Gag interactions in the C-terminal domain of human immunodeficiency virus type 1 p24 capsid antigen are essential for Gag particle assembly

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