The C-Terminal Half of the Human Immunodeficiency Virus Type 1 Gag Precursor Is Sufficient for Efficient Particle Assembly
Open accessAbstract
Human immunodeficiency virus type 1 particle assembly is directed by the Gag polyprotein Pr55 gag , the precursor for the matrix (MA), capsid (CA), and nucleocapsid proteins of the mature virion. We now show that CA sequences N terminal to the major homology region (MHR), which form a distinct domain, are dispensable for particle formation. However, slightly larger deletions which extend into the MHR severely impair particle production. Remarkably, a deletion which removed essentially all MA and CA sequences between the N-terminal myristyl anchor and the MHR reduced the yield of extracellular particles only moderately. Particle formation even exceeded wild-type levels when additional MA sequences, either from the N or the C terminus of the domain, were retained. We conclude that no distinct region between the myristyl anchor and the MHR is required for efficient particle assembly or release.
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The minimal construct for assembly of virus-like particles in vitro does not include the CA-NTD.
“Thirdly, the minimal construct for assembly of virus-like particles in vitro does not include the CA-NTD”
From Retrovirus maturation-an extraordinary structural transformation (2016) · cites this paper as [38]
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References 35 · Cited by 126
- Authors
- Borsetti, A., Öhagen, Å., & Göttlinger, H. G.
- Venue
- Journal of Virology
- Publisher
- American Society for Microbiology
- Published
- 1998-11-01
- Volume
- 72
- Issue
- 11
- Pages
- 9313-9317
- ISSN
- 0022-538X (ISSN-L)
- 1098-5514
- PMC
- PMC110353
- OpenAlex
- W2098158896
- Cited by
- 126
- References
- 35
- Citations by year
- 2026: 2 · 2025: 1 · 2024: 2 · 2023: 2 · 2022: 2 · 2021: 2 · 2020: 3 · 2019: 2 · 2018: 2 · 2017: 2 · 2016: 4 · 2015: 2 · 2014: 6 · 2013: 6 · 2012: 1
- FWCI
- 1.70
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Virology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Allergy and Infectious Diseases (AI29873, AI28691, P30AI028691, R37AI029873, R01AI029873)
- Topics
- Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
- Life Sciences › Immunology and Microbiology › Immunology › T-cell and Retrovirus Studies
- Health Sciences › Medicine › Infectious Diseases › HIV/AIDS drug development and treatment
- Keywords
- HIV-1, Gag protein, Pr55gag, viral assembly, capsid protein, matrix protein, myristoylation, deletion mutants, virion release, retroviral assembly
- MeSH terms
- HeLa Cells, Humans, Microscopy, Electron, Peptide Fragments, Protein Precursors, Transfection, Virus Replication, HIV-1, Gene Products, gag, Sequence Deletion
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