ArticleJournal of virology1996
Cytoskeletal proteins inside human immunodeficiency virus type 1 virions.
Article in Journal of virology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers.
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Who cites it
101 citing papers in PubMed, 210 citations in OpenAlex.
- The Era of Gene Therapy: The Advancement of Lentiviral Vectors and Their Pseudotyping.Viruses · 2025Review
- The host cytoskeleton: a key regulator of early HIV-1 infection.The FEBS journal · 2024Review
- Analysis of individual HIV-1 budding event using fast AFM reveals a multiplexed role for VPS4.Biophysical journal · 2022Article
- Review
- Budding of a Retrovirus: Some Assemblies Required.Viruses · 2020Review
- How HIV-1 Gag Manipulates Its Host Cell Proteins: A Focus on Interactors of the Nucleocapsid Domain.Viruses · 2020Review
- Mass spectrometry analysis reveals differences in the host cell protein species found in pseudotyped lentiviral vectors.Biologicals : journal of the International Association of Biological Standardization · 2018Article
- All-Round Manipulation of the Actin Cytoskeleton by HIV.Viruses · 2018Review
- Role of Ezrin Phosphorylation in HIV-1 Replication.Frontiers in microbiology · 2018Article
- Subcellular Localization of HIV-1Journal of virology · 2017Article
- The Life-Cycle of the HIV-1 Gag-RNA Complex.Viruses · 2016Review
- M2BP inhibits HIV-1 virion production in a vimentin filaments-dependent manner.Scientific reports · 2016Article
- Biochemical and proteomic characterization of retrovirus Gag based microparticles carrying melanoma antigens.Scientific reports · 2016Article
- Coarse-grained simulation reveals key features of HIV-1 capsid self-assembly.Nature communications · 2016Article
- Small G Rac1 is involved in replication cycle of dengue serotype 2 virus in EAhy926 cells via the regulation of actin cytoskeleton.Science China. Life sciences · 2016Article
- Involvement of the Rac1-IRSp53-Wave2-Arp2/3 Signaling Pathway in HIV-1 Gag Particle Release in CD4 T Cells.Journal of virology · 2015Article
- Nucleocapsid Protein: A Desirable Target for Future Therapies Against HIV-1.Current topics in microbiology and immunology · 2015Review
- The nucleocapsid domain of Gag is dispensable for actin incorporation into HIV-1 and for association of viral budding sites with cortical F-actin.Journal of virology · 2014Article
- Ezrin is a component of the HIV-1 virological presynapse and contributes to the inhibition of cell-cell fusion.Journal of virology · 2014Article
- Investigating the role of F-actin in human immunodeficiency virus assembly by live-cell microscopy.Journal of virology · 2014Article
41 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have identified three types of cytoskeletal proteins inside human immunodeficiency virus type 1 (HIV-1) virions by analyzing subtilisin-digested particles. HIV-1 virions were digested with protease, and the treated particles were isolated by sucrose density centrifugation. This method removes both exterior viral proteins and proteins associated with microvesicles that contaminate virion preparations. Since the proteins inside the virion are protected from digestion by the viral lipid envelope, they can be isolated and analyzed after treatment. Experiments presented here demonstrated that this procedure removed more than 95% of the protein associated with microvesicles. Proteins in digested HIV-1(MN) particles from infected H9 and CEM(ss) cell lines were analyzed by high-pressure liquid chromatography, protein sequencing, and immunoblotting. The data revealed that three types of cytoskeletal proteins are present in virions at different concentrations relative to the molar level of Gag: actin (approximately 10 to 15%), ezrin and moesin (approximately 2%), and cofilin (approximately 2 to 10%). Our analysis of proteins within virus particles detected proteolytic fragments of alpha-smooth muscle actin and moesin that were cleaved at sites which might be recognized by HIV-1 protease. These cleavage products are not present in microvesicles from uninfected cells. Therefore, these processed proteins are most probably produced by HIV-1 protease digestion. The presence of these fragments, as well as the incorporation of a few specific cytoskeletal proteins into virions, suggests an active interaction between cytoskeletal and viral proteins.
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