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Cited by 233T-cell and Retrovirus StudiesHIV Research and TreatmentInfectious Diseases and Mycology

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Murine leukemia virus maturation: Protease region required for conversion from “immature” to “Mature” core form and for virus infectivity

Katoh, Iyoko, Yoshinaka, Yoshiyuki, Rein, Alan, Shibuya, Masabumi, Odaka, Tekeshi, Oroszlan, Stephen·1985·Virology
DOI 10.1016/0042-6822(85)90161-8
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Abstract

Murine leukemia virus (MuLV) genome encodes a protease (Y. Yoshinaka, I. Katoh, T.D. Copeland, and S. Oroszlan (1985), Proc. Natl. Acad. Sci. USA 82, 1618-1622), which has been shown to cause maturation, specified as morphological conversion from "immature" to "mature" form of virus cores. To examine whether "immature" particles have infectivity or not, we constructed mutant DNAs with deletions in the protease region. The NIH/3T3 cells transfected with mutant DNAs produced "immature" particles, having immature morphology and containing Pr65gag, a polyprotein precursor of core proteins. The specific infectivity of the extracellularly released and purified particles was shown to be greatly reduced based on reverse transcriptase activity and protein content as compared with the "mature" particles obtained from wild-type DNA-transfected cells. The mutant genomes encoded functionally normal surface glycoprotein, gp70. These results strongly suggest that maturation of MuLV from "immature" to "mature" form of virus particles is indispensable to virus infectivity. The importance of processing of gag and pol, as well as transmembrane protein precursors by the viral protease is discussed.

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  • Mutations in the PR coding domain or inhibition of PR activity result in virions containing unprocessed Gag, rendering them noninfectious.

    “mutations in the PR coding domain or inhibition of PR activity result in virions containing unprocessed Gag, rendering them noninfectious”

    From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Katoh et al. 1985

  • Such structural differences have been observed in viruses that assemble at the plasma membrane, such as MLV and HIV-1, as well as those that preassemble in the cytoplasm before budding, such as MPMV and MMTV.

    “Such structural differences have been observed in viruses that assemble at the plasma membrane, such MLV and HIV-1, as well as those that preassemble in the cytoplasm before budding, such as MPMV and MMTV”

    From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Katoh et al. 1985

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Research works printed but not linked: 31

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Metadata

Authors
Katoh, I., Yoshinaka, Y., Rein, A., Shibuya, M., Odaka, T., & Oroszlan, S.
Affiliations
  • Frederick National Laboratory for Cancer Research (US)
  • Institute of Medical Science, The University of Tokyo (JP)
Corresponding author
Yoshinaka, Yoshiyuki
ORCID
Venue
Virology
Publisher
Elsevier BV
Published
1985-09
Volume
145
Issue
2
Pages
280-292
ISSN
0042-6822 (ISSN-L)
DOI
10.1016/0042-6822(85)90161-8
OpenAlex
W1996834128
Cited by
233
References
0
Citations by year
2026: 2 · 2025: 1 · 2024: 2 · 2023: 1 · 2022: 1 · 2021: 1 · 2016: 1 · 2014: 3 · 2012: 4
FWCI
3.94
Type
journal article
Language
en
Open access
closed
Licence
Locations
  • Virology (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • U.S. Department of Health and Human Services (NOl-CO-23909)
  • National Cancer Institute
Topics
  • Life Sciences › Immunology and Microbiology › Immunology › T-cell and Retrovirus Studies
  • Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
  • Health Sciences › Medicine › Infectious Diseases › Infectious Diseases and Mycology
Keywords
murine leukemia virus, virus maturation, viral protease, immature virus particles, infectivity, Gag processing, protease mutants, reverse transcriptase activity
MeSH terms
Amino Acid Sequence, Animals, Cells, Cultured, DNA Restriction Enzymes, Mice, Inbred Strains, Microscopy, Electron, Moloney murine leukemia virus, Mutation, Peptide Hydrolases, RNA-Directed DNA Polymerase, Transfection, Viral Proteins, Mice

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