The DOI matches its Crossref record; 46 of the 46 references it cites were found in a registry or an index.
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
Open accessAbstract
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, 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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Cites
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Fine structure of human immunodeficiency virus (HIV) and immunolocalization of structural proteins
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HIV-1 Gag proteins: diverse functions in the virus life cycle
Freed, E. O. (1998) · Virology · doi:10.1006/viro.1998.9398 · Cited by 717
“For example, deletion of a large region of MA retargeted virus assembly to the ER (Facke et al., 1993; Gallina et al., 1994) and replacement of the entire MA sequence with a heterologous membrane binding domain resulted in promiscuous assembly at both plasma and intracellular membranes (Reil et…”
BackgroundPhosphatidylinositol (4,5) bisphosphate regulates HIV-1 Gag targeting to the plasma membrane
Ono, A., Ablan, S. D., Lockett, S. J., Nagashima, K., & Freed, E. O. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405596101 · Cited by 553
Zhou, W., Parent, L. J., Wills, J. W., & Resh, M. D. (1994) · Journal of Virology · doi:10.1128/jvi.68.4.2556-2569.1994 · Cited by 529
“Several other studies have attempted to probe the sequence elements important for membrane targeting of HIV-1 Gag and subsequent virion production (10, 61, 62).”
BackgroundInfluentialStructural biology of HIV 1 1Edited by P. E. Wright
Turner, B. G., & Summers, M. F. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2354 · Cited by 470
Functional Surfaces of the Human Immunodeficiency Virus Type 1 Capsid Protein
von Schwedler, U. K., Stray, K. M., Garrus, J. E., & Sundquist, W. I. (2003) · Journal of Virology · doi:10.1128/jvi.77.9.5439-5450.2003 · Cited by 421
Metadata
- Authors
- Fäcke, M., Janetzko, A., Shoeman, R. L., & Kräusslich, H. G.
- Affiliations
- German Cancer Research Center (DE)
- 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
- 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
- bronze
- doi.org
- 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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