The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Role of the matrix protein in the virion association of the human immunodeficiency virus type 1 envelope glycoprotein
Open accessAbstract
The matrix (MA) protein of human immunodeficiency virus type 1 (HIV-1) forms an inner coat directly underneath the lipid envelope of the virion. The outer surface of the lipid envelope surrounding the capsid is coated by the viral Env glycoproteins. We report here that the HIV-1 capsid-Env glycoprotein association is very sensitive to minor alterations in the MA protein. The results indicate that most of the MA domain of the Gag precursor, except for its carboxy terminus, is essential for this association. Viral particles produced by proviruses with small missense or deletion mutations in the region coding for the amino-terminal 100 amino acids of the MA protein lacked both the surface glycoprotein gp120 and the transmembrane glycoprotein gp41, indicating a defect at the level of Env glycoprotein incorporation. Alterations at the carboxy terminus of the MA domain had no significant effect on the levels of particle-associated Env glycoprotein or on virus replication. The presence of HIV-1 MA protein sequences was sufficient for the stable association of HIV-1 Env glycoprotein with hybrid particles that contain the capsid (CA) and nucleocapsid (NC) proteins of visna virus. The association of HIV-1 Env glycoprotein with the hybrid particles was dependent upon the presence of the HIV-1 MA protein domain, as HIV-1 Env glycoprotein was not efficiently recruited into virus particles when coexpressed with authentic visna virus Gag proteins.
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In the citing paper
“The self-association of HIV-1 MA, and especially its trimerization, has also been shown to be crucial for the incorporation of envelope glycoprotein into the nascently forming virus particles”
From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Dorfman et al. 1994
In the citing paper
“Proper localization of Env at the plasma membrane is critical for its selective incorporation into budding virions, a process mediated by interactions between gp41 cytoplasmic tail and the MA domain of the Gag protein”
From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Dorfman et al. 1994
Citations
Cites
Göttlinger, H. G., Sodroski, J. G., & Haseltine, W. A. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.15.5781 · Cited by 841
Self-citationFäcke, M., Janetzko, A., Shoeman, R. L., & Kräusslich, H. G. (1993) · Journal of Virology · doi:10.1128/jvi.67.8.4972-4980.1993 · Cited by 198 · cited 2×
“virus particle release from the cell membrane (7).”
BackgroundRhee, S. S., & Hunter, E. (1990) · Cell · doi:10.1016/0092-8674(90)90289-q · Cited by 160
Cited by
Sorted by citations
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
“However, virions with N-terminal CA mutations often display marked infectivity defects and aberrant core morphology by EM (Jowett et al., 1992; von Poblotzki et al., 1993; Wang and Barklis, 1993; Dorfman et al., 1994a; Reicin et al., 1995, 1996).”
BackgroundInfluentialFunctional association of cyclophilin A with HIV-1 virions
Thali, M., Bukovsky, A., Kondo, E., Rosenwlrth, B., Walsh, C. T., Sodroski, J., & Göttlinger, H. G. (1994) · Nature · doi:10.1038/372363a0 · Cited by 629
Self-citationStructural 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
“…Wang & Barklis, 1993; Wang et al., 1993; Wills et al., 1991; Yuan et al., 1993; Zhou et al., 1994) and interacts with the cytoplasmic tail of TM (Dorfman et al., 1994b; Freed & Martin, 1996; Freed et al., 1994; Freed & Martin, 1995; Mammano et al., 1995; Wang & Barklis, 1993; Wang et al., 1993;…”
BackgroundHIV-1 Envelope Glycoprotein Biosynthesis, Trafficking, and Incorporation
Checkley, M. A., Luttge, B. G., & Freed, E. O. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.04.042 · Cited by 534
Huang, M., Orenstein, J. M., Martin, M. A., & Freed, E. O. (1995) · Journal of Virology · doi:10.1128/jvi.69.11.6810-6818.1995 · Cited by 486
“Mutations in the CA of murine leukemia virus (17, 35, 57), Mason-Pfizer monkey virus (59), and HIV-1 (5, 11, 40, 62) also disrupt virion formation.”
Background
Metadata
- Authors
- Dorfman, T., Mammano, F., Haseltine, W. A., & Göttlinger, H. G.
- Affiliations
- Dana-Farber Cancer Institute (US)
- Venue
- Journal of Virology
- Publisher
- American Society for Microbiology
- Published
- 1994-03
- Volume
- 68
- Issue
- 3
- Pages
- 1689-1696
- ISSN
- 0022-538X (ISSN-L)
- 1098-5514
- PMC
- PMC236628
- OpenAlex
- W1557860493
- Cited by
- 288
- References
- 0
- Citations by year
- 2025: 2 · 2024: 4 · 2023: 1 · 2022: 7 · 2021: 1 · 2020: 4 · 2019: 5 · 2018: 3 · 2017: 3 · 2016: 4 · 2015: 4 · 2014: 8 · 2013: 13 · 2012: 9
- FWCI
- 8.13
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Virology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Cancer Institute (CA06516, P30CA006516)
- National Institute of Allergy and Infectious Diseases (AI29873, AI28691, P30AI028691)
- 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 matrix protein, HIV-1 envelope glycoprotein, Gag precursor, gp120, gp41, visna virus, viral assembly, C-terminal domain, missense mutations, deletion mutations
- MeSH terms
- Cells, Cultured, DNA Mutational Analysis, Humans, Morphogenesis, Protein Binding, RNA, Viral, Structure-Activity Relationship, Viral Matrix Proteins, Virion, HIV-1, Gene Products, env
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