Cited by 160T-cell and Retrovirus StudiesHIV Research and TreatmentCellular transport and secretion

A single amino acid substitution within the matrix protein of a type D retrovirus converts its morphogenesis to that of a type C retrovirus

Rhee, Sung S., Hunter, Eric·1990·Cell

Abstract

Two different morphogenic processes of retroviral capsid assembly have been observed: the capsid is either assembled at the plasma membrane during the budding process (type C), or preassembled within the cytoplasm (types B and D). We describe here a gag mutant of Mason-Pfizer monkey virus, a type D retrovirus, in which a tryptophan substituted for an arginine in the matrix protein results in efficient assembly of capsids at the plasma membrane through a morphogenic process similar to that of type C retroviruses. We conclude that a type D retrovirus Gag polyprotein contains an additional, dominant signal that prevents immediate transport of precursors from the site of biosynthesis to the plasma membrane. Instead, they are directed to and retained at a cytoplasmic site where a concentration sufficient for self-assembly into capsids occurs. Thus, capsid assembly processes for different retroviruses appear to differ only in the intracellular site to which capsid precursors are directed.

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Crossref · 10.1016/0092-8674(90)90289-q

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62 of 62 references verified0 citation errors · 0 not checkable

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  • In RSV, MA and envelope chemically cross-link, while mutations in MPMV MA lead to inefficient envelope incorporation and postbudding cleavage of the envelope.

    “For example, in RSV, MA and envelope chemically cross-link, while mutations in MPMV MA lead to inefficient envelope incorporation and postbudding cleavage of the envelope”
  • The MA domain of Gag in other retroviruses is involved in envelope incorporation.

    “The MA domain of Gag in other retroviruses has also been shown to be involved in envelope incorporation.”
  • Amino acid substitutions in the MA sequence of MPMV, MMTV, JSRV, and spumaviruses relocate their assembly from cytoplasm to plasma membrane, a major shift from type D to type C pattern.

    “The critical role of Gag in virion assembly has been clearly demonstrated by amino acid substitutions(s) in the MA sequence of MPMV, MMTV, JSRV, and spumaviruses, resulting in the relocation of their assembly from cytoplasm to the plasma membrane—a major shift from a type D to a type C pattern”

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Authors
Rhee, S. S., & Hunter, E.
Affiliations
University of Alabama at Birmingham (US)
Venue
Cell
Publisher
Elsevier BV
Published
1990-10
Volume
63
Issue
1
Pages
77-86
ISSN
0092-8674 (ISSN-L)
OpenAlex
W2130138608
Cited by
160
References
67
Citations by year
2026: 1 · 2025: 2 · 2024: 2 · 2022: 2 · 2021: 1 · 2020: 2 · 2019: 1 · 2018: 3 · 2017: 1 · 2016: 2 · 2015: 2 · 2013: 4
FWCI
4.30
Type
journal article
Language
en
Open access
closed
Locations
  • Cell (publishedVersion)
  • PubMed (publishedVersion)
Funders
National Cancer Institute (CA27834)
Topics
  • Life Sciences › Immunology and Microbiology › Immunology › T-cell and Retrovirus Studies
  • Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Keywords
capsid assembly, matrix protein, type D retroviruses, type C retroviruses, Mason-Pfizer monkey virus, Gag protein, amino acid substitutions, tryptophan substitution, intracellular trafficking
MeSH terms
Amino Acid Sequence, Animals, Capsid, Cell Line, Clone Cells, HeLa Cells, Molecular Sequence Data, Morphogenesis, Mutation, Retroviridae, Sequence Homology, Nucleic Acid, Transfection, Viral Matrix Proteins, Virion, Gene Products, gag, Betaretrovirus

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