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Cited by 198HIV Research and TreatmentT-cell and Retrovirus StudiesCellular transport and secretion

A large deletion in the matrix domain of the human immunodeficiency virus gag gene redirects virus particle assembly from the plasma membrane to the endoplasmic reticulum

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Fäcke, M, Janetzko, A, Shoeman, R L, Kräusslich, H G·1993·Journal of Virology
DOI 10.1128/jvi.67.8.4972-4980.1993PMC PMC237885
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Abstract

Morphogenesis of retroviruses involves assembly of the structural Gag and Gag-Pol polyproteins with subsequent budding of the virus particle from the plasma membrane and proteolytic cleavage by the viral proteinase. The matrix (MA) domain, representing the N-terminal segment of Gag, plays a critical role in this process. We constructed an in-frame deletion in the MA coding region (lacking codons 16 to 99) of the human immunodeficiency virus (HIV) type 1 gag gene. Following transient transfection of the complete proviral DNA carrying the deletion, the mutant polyprotein was synthesized and proteolytically processed like the wild-type polyprotein. However, release of virus particles was reduced approximately 10-fold. The extracellular particles that were released did not contain viral glycoproteins and were noninfectious. Electron micrographs revealed budding of virus particles into the endoplasmic reticulum (ER) of transfected cells and large numbers of particles within the ER. These particles were all immature and morphologically indistinguishable from intracisternal A-type particles, a class of murine endogenous retrovirus elements. Budding structures at the plasma membrane were rarely seen and only a few extracellular particles were observed, but in contrast to those in the ER, these particles had the morphology of mature particles, similar to that of wild-type HIV, except for the lack of surface projections.

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  • Alterations in the MA domain of HIV-1 Gag, whether through amino acid substitutions or deletions, redirect virus assembly to the cytoplasm or intracellular membranes, such as the endoplasmic reticulum.

    “alterations in the MA domain of HIV-1 Gag, whether through amino acid substitutions or deletions, have been shown to redirect virus assembly to the cytoplasm or intracellular membranes, such as the endoplasmic reticulum”

    From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Fäcke et al. 1993

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Authors
Fäcke, M., Janetzko, A., Shoeman, R. L., & Kräusslich, H. G.
Affiliations
German Cancer Research Center (DE)
ORCID
Venue
Journal of Virology
Publisher
American Society for Microbiology
Published
1993-08
Volume
67
Issue
8
Pages
4972-4980
ISSN
  • 0022-538X (ISSN-L)
  • 1098-5514
DOI
10.1128/jvi.67.8.4972-4980.1993
PMC
PMC237885
OpenAlex
W2153090499
Cited by
198
References
46
Citations by year
2026: 1 · 2025: 1 · 2024: 2 · 2023: 1 · 2021: 1 · 2020: 2 · 2019: 1 · 2018: 3 · 2017: 1 · 2016: 5 · 2015: 2 · 2014: 4 · 2013: 2 · 2012: 5
FWCI
4.61
Type
journal article
Language
en
Open access
Licence
journals.asm.org/non-commercial-tdm-license (tdm)
Locations
  • Journal of Virology (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • Max Planck Institute for Plasma Physics (submittedVersion)
  • MPG.PuRe (Max Planck Society) (submittedVersion)
Topics
  • Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
  • Life Sciences › Immunology and Microbiology › Immunology › T-cell and Retrovirus Studies
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Keywords
HIV-1, gag gene, matrix domain, viral assembly, endogenous retroviruses, viral particle release, proteolytic processing, Gag-Pol polyprotein
MeSH terms
Animals, Cell Line, Cell Membrane, Chlorocebus aethiops, Endoplasmic Reticulum, Enzyme-Linked Immunosorbent Assay, Humans, Kidney, Kinetics, Models, Biological, Morphogenesis, RNA, Messenger, Time Factors, Protein Biosynthesis, Virus Replication, Blotting, Western, HIV-1, Gene Products, gag, Fusion Proteins, gag-pol, Genes, gag, Gene Expression, Genome, Viral, Sequence Deletion

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