Cited by 288HIV Research and TreatmentT-cell and Retrovirus StudiesHIV/AIDS drug development and treatment

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Role of the matrix protein in the virion association of the human immunodeficiency virus type 1 envelope glycoprotein

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Dorfman, T, Mammano, F, Haseltine, W A, Göttlinger, H G·1994·Journal of Virology

DOI 10.1128/jvi.68.3.1689-1696.1994PMC PMC236628

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Abstract

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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Role of capsid precursor processing and myristoylation in morphogenesis and infectivity of human immunodeficiency virus type 1
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-citation
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
Fäcke, 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).”
Background
A single amino acid substitution within the matrix protein of a type D retrovirus converts its morphogenesis to that of a type C retrovirus
Rhee, S. S., & Hunter, E. (1990) · Cell · doi:10.1016/0092-8674(90)90289-q · Cited by 160

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Background
A plasma membrane localization signal in the HIV-1 envelope cytoplasmic domain prevents localization at sites of vesicular stomatitis virus budding and incorporation into VSV virions.
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MethodSelf-citation
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Background
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Result
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“The HIV-1 MA is thought to be involved in virus entry (27), transport of the viral preintegration complex to the nucleus (1), envelope (Env) glycoprotein incorporation into virus particles (4, 5, 28), and virus particle assembly (3, 7, 28).”
Background
Virus Particle Release from Glycosphingolipid-Enriched Microdomains Is Essential for Dendritic Cell-Mediated Capture and Transfer of HIV-1 and Henipavirus
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Background
Multiple Functions for the Basic Amino Acids of the Human T-Cell Leukemia Virus Type 1 Matrix Protein in Viral Transmission
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“In HIV-1, mutations in the MA disturb glycoprotein incorporation (10, 50), probably because the MA has to accommodate the long cytoplasmic tail of the glycoproteins.”
Background
Second-Site Compensatory Mutations of HIV-1 Capsid Mutations
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Background
Analysis of HIV-1 Matrix-Envelope Cytoplasmic Tail Interactions
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“36 This theory is supported by the fact that Gag has a much greater affinity for membranes than MA. 34,37 The myr-exposed state is also promoted by the interaction of MA with PI(4,5)P2.”
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Background
Identification of the Glycoprotein 41™ Cytoplasmic Tail Domains of Human Immunodeficiency Virus Type 1 That Interact with Pr55Gag Particles
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“codon and a frameshift mutation in the gag gene (29).”
BackgroundSelf-citation
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Background
Dual Pathways of Human Immunodeficiency Virus Type 1 Envelope Glycoprotein Trafficking Modulate the Selective Exclusion of Uncleaved Oligomers from Virions
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“Mutations within the matrix region of Gag affect Env incorporation into virions (17, 22).”
BackgroundSelf-citation
Amino acid mutations of the infectious clone from Chinese EIAV attenuated vaccine resulted in reversion of virulence.
Shen, T., Liang, H., Tong, X., Fan, X., He, X., Ma, Y., Xiang, W.-H., Shen, R.-X., Zhang, X.-Y., & Shao, Y. (2006) · Vaccine · doi:10.1016/j.vaccine.2005.08.084 · Cited by 35
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“Of note was that the amino acid substitution was located in a very conserved region (gag p17, helix 1) previously described to be important for viral replication in Jurkat cells (35).”
Background
Interaction between the Cytoplasmic Domain of ICAM-1 and Pr55Gag Leads to Acquisition of Host ICAM-1 by Human Immunodeficiency Virus Type 1
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Background
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“Deletions and multiple amino acid substitutions throughout MA impair Env incorporation (9, 68), and single amino acid substitutions near the amino terminus of MA can abrogate Env incorporation (16, 19, 45).”
Background
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“HXBH10-gag(2) is a variant of HXBH10 that is unable to express p55 because of a premature termination codon in place of codon 8 of the gag gene and an additional frameshift mutation in the CA coding region (12).”
BackgroundMethod
Roles of the interactions between Env and Gag proteins in the HIV‐1 replication cycle
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Method
Identification of Retroviral Late Domains as Determinants of Particle Size
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Background
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“Some have claimed that the interaction between Env and core protein (Gag) is necessary for Env incorporation (Yu et al., 1992; Dorfman et al., 1994), whereas others have reported that some heterologous proteins can be efficiently incor- * Author for correspondence.”
Background
Biological, molecular, and structural analysis of a cytopathic variant from a molecularly cloned simian immunodeficiency virus
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Background
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“Mutational analysis of HIV-1 pl7 has indicated an essential role of this protein in targeting the correct cellular site for viral morphogenesis.18-20 Owens and Rose57 have shown that incorporation of HIV-1 Env glycoprotein into HIVenv-VSVgag chimeras is dependent on the cytoplasmic tail of VSV Env…”
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“RWEKIRL from p17(15–21) is similar to N WE V YKL from the rabbit skeletal muscle phosphofructokinase calmodulin-binding site 22 (boldface denotes similar residue) and to RW K K NF I from the rabbit skeletal MLCK calmodulin-binding site.”
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“However, the reciprocal incorporation of HIV-1 Env glycoprotein into other retroviral capsids has not succeeded (6, 43).”
Background
Regulation of HIV-1 gag Protein Subcellular Targeting by Protein Kinase C
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“Cellular and viral lysates were prepared and analyzed for Env expression and particle incorporation, respectively, using immunoblotting with an anti-HIV-1 Env MAb as previously described (13).”
BackgroundMethodInfluential
Analysis of human immunodeficiency virus matrix domain replacements.
Scholz, I. G., Still, A., Dhenub, T. C., Coday, K., Webb, M., & Barklis, E. (2008) · Virology · doi:10.1016/j.virol.2007.10.010 · Cited by 29
“One possible itinerary involves PrGag association with intracellular membranes such as multivesicular bodies (MVBs), followed by vesicular delivery to the plasma membrane (PM) (Bryant and Ratner, 1990; Davis et al., 2006; Dorfman et al., 1994; Freed and Martin, 1995, 1996).”
Domains in the simian immunodeficiency virus gp41 cytoplasmic tail required for envelope incorporation into particles.
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Mutations in Envelope gp120 Can Impact Proteolytic Processing of the gp160 Precursor and Thereby Affect Neutralization Sensitivity of Human Immunodeficiency Virus Type 1 Pseudoviruses
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“Several lines of evidence suggest that the Env spikes interact with the structural matrix (MA) protein via the cytoplasmic tail of gp41 (15, 17, 26, 57, 84).”
Background
Nef Enhances Human Immunodeficiency Virus Type 1 Infectivity in the Absence of Matrix
Dorfman, T., Popova, E. N., Pizzato, M., & Göttlinger, H. G. (2002) · Journal of Virology · doi:10.1128/jvi.76.13.6857-6862.2002 · Cited by 25
“viral particles (13, 55), but Env incorporation can be com-”
BackgroundSelf-citation
cDNA Encoding a Single-Chain Antibody to HIV p17 with Cytoplasmic or Nuclear Retention Signals Inhibits HIV-1 Replication
Tewari, D., Goldstein, S. L., Notkins, A. L., & Zhou, P. (1998) · The Journal of Immunology · doi:10.4049/jimmunol.161.5.2642 · Cited by 28
Envelope glycoproteins are not required for insertion of host ICAM-1 into human immunodeficiency virus type 1 and ICAM-1-bearing viruses are still infectious despite a suboptimal level of trimeric envelope proteins.
Beauséjour, Y., & Tremblay, M. (2004) · Virology · doi:10.1016/j.virol.2004.03.029 · Cited by 27
“…mutations in the HIV-1 matrix protein often result in a blocking of the incorporation of HIV-1 Env (gp120 and gp41) into assembling HIV-1 particles (Dorfman et al., 1994; Freed and Martin, 1995, 1996; Lee et al., 1997; Yu et al., 1992, 1993), a virus expression vector bearing a single-site…”
Background
Positive and Negative Modulation of Virus Infectivity and Envelope Glycoprotein Incorporation into Virions by Amino Acid Substitutions at the N Terminus of the Simian Immunodeficiency Virus Matrix Protein
Manrique, J. M., Celma, C. C. P., Hunter, E., Affranchino, J. L., & González, S. A. (2003) · Journal of Virology · doi:10.1128/jvi.77.20.10881-10888.2003 · Cited by 27
“within the N-terminal 100 amino acids (7, 36), and certain”
Background
Transfer of endoplasmic reticulum and Golgi retention signals to human immunodeficiency virus type 1 gp160 inhibits intracellular transport and proteolytic processing of viral glycoprotein but does not influence the cellular site of virus particle budding.
Pfeiffer, T., Zentgraf, H., Freyaldenhoven, B., & Bosch, V. (1997) · Journal of General Virology · doi:10.1099/0022-1317-78-7-1745 · Cited by 27
“The viral matrix (MA) domain of the precursor Pr55gag plays a central role both in particle formation and glycoprotein incorporation, and MA mutants have been generated which result in normal release of particles lacking Env, although Env had been present in the transfected cell (Yu et al., 1992 ; Dorfman et al., 1994…”
Background
In vitro binding of simian immunodeficiency virus matrix protein to the cytoplasmic domain of the envelope glycoprotein
Manrique, J. M., Affranchino, J. L., & González, S. A. (2008) · Virology · doi:10.1016/j.virol.2008.01.015 · Cited by 28
Human immunodeficiency virus matrix tyrosine phosphorylation: characterization of the kinase and its substrate requirements
Camaur, D., Gallay, P. A., Swingler, S., & Trono, D. (1997) · Journal of Virology · doi:10.1128/jvi.71.9.6834-6841.1997 · Cited by 25
“Small missense or deletion mutations in the MA region encoding the first 100 residues result in the production of virions that lack both surface glycoprotein gp120 and transmembrane glycoprotein gp41 (11, 51).”
Background
Blockage of N-myristoylation of HIV-1 gag induces the production of impotent progeny virus.
Furuishi, K., Matsuoka, H., Takama, M., Takahashi, I., Misumi, S., & Shoji, S. (1997) · Biochemical and Biophysical Research Communications - BBRC · doi:10.1006/bbrc.1997.7178 · Cited by 26
HIV-1 p17 Matrix Protein Interacts with Heparan Sulfate Side Chain of CD44v3, Syndecan-2, and Syndecan-4 Proteoglycans Expressed on Human Activated CD4+ T Cells Affecting Tumor Necrosis Factor α and Interleukin 2 Production
Francesco, M. A. D., Baronio, M., & Poiesi, C. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.191270 · Cited by 21
In vitro assembly of the feline immunodeficiency virus Gag polyprotein
Affranchino, J. L., & González, S. A. (2010) · Virus Research · doi:10.1016/j.virusres.2010.03.012 · Cited by 23
Identification and characterization of HIV-1 CD8+ T cell escape variants with impaired fitness.
Sanchez-Merino, V., Farrow, M. A., Brewster, F. E., Somasundaran, M., & Luzuriaga, K. (2008) · Journal of Infectious Diseases · doi:10.1086/524845 · Cited by 25
“for viral replication in culture [30].”
Background
Enhancement of immunogenicity of an HIV Env DNA vaccine by mutation of the Tyr-based endocytosis motif in the cytoplasmic domain.
Bu, Z., Ye, L., Vzorov, A., Taylor, D., Compans, R., & Yang, C.-L. (2004) · Virology · doi:10.1016/j.virol.2004.06.041 · Cited by 25
Retention of the Human Immunodeficiency Virus Type 1 Envelope Glycoprotein in the Endoplasmic Reticulum Does Not Redirect Virus Assembly from the Plasma Membrane
Salzwedel, K., West, J. T., Mulligan, M., & Hunter, E. (1998) · Journal of Virology · doi:10.1128/jvi.72.9.7523-7531.1998 · Cited by 25
“Deletions within the HIV-1 MA protein prevent the incorporation of glycoprotein into virions (8, 39).”
Background
TM domain swapping of murine leukemia virus and human T-cell leukemia virus envelopes confers different infectious abilities despite similar incorporation into virions
Denesvre, C., Carrington, C., Corbin, A., Takeuchi, Y., Cosset, F., Schulz, T. F., Sitbon, M., & Sonigo, P. (1996) · Journal of Virology · doi:10.1128/jvi.70.7.4380-4386.1996 · Cited by 25
Part of the C-terminal tail of the envelope gp41 transmembrane glycoprotein of human immunodeficiency virus type 1 is exposed on the surface of infected cells and is involved in virus-mediated cell fusion.
Cheung, L., McLain, L., Hollier, M. J., Reading, S. A., & Dimmock, N. (2005) · Journal of General Virology · doi:10.1099/vir.0.80439-0 · Cited by 25
Solution Structure of Calmodulin Bound to the Binding Domain of the HIV-1 Matrix Protein
Vlach, J., Samal, A. B., & Saad, J. S. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.543694 · Cited by 28
“Several residues in helix 1 of MA (Leu(13), Trp(16), Glu(17), and Lys(18)) are important for gp160 incorporation (89 –91), which led to the suggestion that the MA domain of Gag interacts directly with the gp160 protein via helix 1 (89, 92).”
Background
NMR, Biophysical, and Biochemical Studies Reveal the Minimal Calmodulin Binding Domain of the HIV-1 Matrix Protein
Samal, A. B., Ghanam, R. H., Fernandez, T. F., Monroe, E. B., & Saad, J. S. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.273623 · Cited by 27
Inhibition of human immunodeficiency virus type 1 particle formation by alterations of defined amino acids within the C terminus of the capsid protein.
Kattenbeck, B., von Poblotzki, A., Rohrhofer, A., Wolf, H. J., & Modrow, S. (1997) · Journal of General Virology · doi:10.1099/0022-1317-78-10-2489 · Cited by 19
“…(Freed et al., 1994 ; Morikawa et al., 1995) ; incorporation of the viral glycoprotein complexes via gp41 (Yu et al., 1992a ; Wang et al., 1993 ; Dorfman et al., 1994a) ; and directing the viral preintegration complex to the nucleus during the early steps of infection (Bukrinskaya et al., 1992…”
Background
Functional Role of the Cytoplasmic Tail Domain of the Major Envelope Fusion Protein of Group II Baculoviruses
Long, G., Pan, X.-Y., Westenberg, M., & Vlak, J. (2006) · Journal of Virology · doi:10.1128/jvi.01178-06 · Cited by 23
“The CTDs of virus glycoproteins are clearly involved in virus assembly, since they bind to the matrix protein of the nucleocapsid and collate the viral envelope and nucleocapsid (9, 12, 45).”
Background
Mutation of critical serine residues in HIV-1 matrix result in an envelope incorporation defect which can be rescued by truncation of the gp41 cytoplasmic tail
Bhatia, A. K., Kaushik, R., Campbell, N., Pontow, S. E., & Ratner, L. (2008) · Virology · doi:10.1016/j.virol.2008.10.047 · Cited by 21
“Co-expression of Env with Pr55Gag focuses budding exclusively at the basolateral surface of polarized epithelial cells (Dorfman et al., 1994; Owens et al., 1991).”
Background
MuLV-based vectors pseudotyped with truncated HIV glycoproteins mediate specific gene transfer in CD4+ peripheral blood lymphocytes
Lodge, R., Subbramanian, R. A., Forget, J., Lemay, G., & Cohen, É. A. (1998) · Gene Therapy · doi:10.1038/sj.gt.3300646 · Cited by 22
Molecular Biology of Lentivirus-Mediated Gene Transfer
Stevenson, M. (2002) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-56114-6_1 · Cited by 17
Viral and host factors regulating HIV-1 envelope protein trafficking and particle incorporation
Anokhin, B., & Spearman, P. (2022) · Viruses · doi:10.3390/v14081729 · Cited by 21
Atomic view of the HIV-1 matrix lattice; implications on virus assembly and envelope incorporation
Samal, A. B., Green, T. J., & Saad, J. S. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2200794119 · Cited by 21
Retroviral Env Glycoprotein Trafficking and Incorporation into Virions
Murakami, T. (2012) · Molecular Biology International · doi:10.1155/2012/682850 · Cited by 30
“The MA domain of Gag has been shown to be important for Env incorporation into virions [91, 92, 101, 102].”
Background
A CCR5-Tropic Simian-HIV Molecular Clone Capable of Inducing AIDS in Rhesus Macaques
Hsu, M.-L., Ho, S., Balfe, P., Gettie, A., Harouse, J., Blanchard, J., & Cheng-Mayer, C. (2005) · Journal of Acquired Immune Deficiency Syndromes · doi:10.1097/01.qai.0000184857.39318.4f · Cited by 21
Analysis of dominant-negative effects of mutant Env proteins of human immunodeficiency virus type 1.
Iwatani, Y., Kawano, K., Ueno, T., Tanaka, M., Ishimoto, A., Ito, M., & Sakai, H. (2001) · Virology · doi:10.1006/viro.2001.0944 · Cited by 21
Potential nuclease-based strategies for HIV gene therapy.
Singwi, S., & Joshi, S. (2000) · Frontiers in Bioscience · doi:10.2741/singwi · Cited by 21
“The association of Gag and Gag/Pol precursors with the Env protein is mediated by protein/protein interactions between the MA domain and gp41 protein (80).”
Background
Structural and biophysical characterizations of HIV-1 matrix trimer binding to lipid nanodiscs shed light on virus assembly
Murphy, R. E., Samal, A. B., Vlach, J., Más, V., Prevelige, P. E., & Saad, J. S. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.010997 · Cited by 25
“Genetic, in vivo, and biochemical studies suggested that incorporation of the Env protein into virus particles is mediated by interactions between the MA domain of Gag and the cytoplasmic tail of the transmembrane subunit of Env (gp41CT) (50-54).”
Background
Modification of virus infectivity by cytoplasmic tail of HIV-1 TM protein.
Iwatani, Y., Ueno, T., Nishimura, A., Zhang, X.-Y., Hattori, T., Ishimoto, A., Ito, M., & Sakai, H. (2001) · Virus Research · doi:10.1016/s0168-1702(00)00249-5 · Cited by 20
Expression of HIV-1 antigens in plants as potential subunit vaccines
Meyers, A., Chakauya, E., Shephard, E. G., Tanzer, F. L., Maclean, J., Lynch, A., Williamson, A., & Rybicki, E. (2008) · BMC Biotechnology · doi:10.1186/1472-6750-8-53 · Cited by 19
“The native p17 facilitates the intramembrane associations necessary for viral assembly and release [34,35] as well as being involved in the transport of the viral pre-integration complex into the nucleus [36].”
Background
Functional relationship between the matrix proteins of feline and simian immunodeficiency viruses
Manrique, M. L., González, S. A., & Affranchino, J. L. (2004) · Virology · doi:10.1016/j.virol.2004.07.029 · Cited by 18
“, 1996) and envelope glycoprotein incorporation into virions (Dorfman et al., 1994; Freed and Martin, 1996; Manrique et al., 2003; Murakami and Freed, 2000; Yu et al., 1992).”
Background
Efficient Production of HIV-1 Virus-Like Particles from a Mammalian Expression Vector Requires the N-Terminal Capsid Domain
Jalaguier, P., Turcotte, K., Danylo, A., Cantin, R., & Tremblay, M. J. (2011) · PLoS ONE · doi:10.1371/journal.pone.0028314 · Cited by 15
“envelope glycoproteins (ENV) [24,25].”
Role of envelope processing and gp41 membrane spanning domain in the formation of human immunodeficiency virus type 1 (HIV-1) fusion-competent envelope glycoprotein complex.
Welman, M., Lemay, G., & Cohen, É. (2007) · Virus Research · doi:10.1016/j.virusres.2006.10.009 · Cited by 18
Effect of Point Mutations in the N Terminus of the Lentivirus Lytic Peptide-1 Sequence of Human Immunodeficiency Virus Type 1 Transmembrane Protein gp41 on Env Stability*
Lee, S.-F., Ko, C., Wang, C.-T., & Chen, S. S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201479200 · Cited by 17
Solution Structure, Self-Assembly, and Membrane Interactions of the Matrix Protein from Newcastle Disease Virus at Neutral and Acidic pH
Shtykova, E., Petoukhov, M., Dadinova, L., Fedorova, N. V., Tashkin, V. Y., Timofeeva, T. A., Ksenofontov, A., Loshkarev, N. A., Baratova, L. A., Jeffries, C. M., et al. (2018) · Journal of Virology · doi:10.1128/jvi.01450-18 · Cited by 16
Multiple Gag Domains Contribute to Selective Recruitment of Murine Leukemia Virus (MLV) Env to MLV Virions
Gregory, D. A., Lyddon, T. D., & Johnson, M. C. (2012) · Journal of Virology · doi:10.1128/jvi.02604-12 · Cited by 15
“1524 jvi.asm.org Journal of Virology on July 22, 2018 by guest http://jvi.asm .org/ D ow nloaded from visna virus can convey the ability to incorporate HIV Env (12).”
BackgroundInfluential
A comparative analysis of viral matrix proteins using disorder predictors
Goh, G. K., Dunker, A. K., & Uversky, V. N. (2008) · Virology Journal · doi:10.1186/1743-422x-5-126 · Cited by 63
“Earlier it has been already observed that the envelope proteins are very sensitive to the behavior of the matrix proteins [3].”
Background
Equine Infectious Anemia Virus Gag p9 Function in Early Steps of Virus Infection and Provirus Production
Jin, S., Chen, C.-P., & Montelaro, R. (2005) · Journal of Virology · doi:10.1128/jvi.79.14.8793-8801.2005 · Cited by 16
“In this regard, studies with other retroviruses, including HIV-1, have implicated a number of virion proteins as important components of the viral DNA PIC, including the viral integrase (4, 6, 57), matrix (18, 20, 26, 28, 33, 61), capsid (10, 23, 64), and Vpr (5, 31, 42, 56).”
Background
The Triple Threat of HIV-1 Protease Inhibitors
Potempa, M., Lee, S.-K., Wolfenden, R. V., & Swanstrom, R. I. (2015) · Current topics in microbiology and immunology · doi:10.1007/82_2015_438 · Cited by 15
“And furthermore, deletions (Yu et al. 1992; Dorfman et al. 1994; Mammano et al. 1995; Murakami and Freed 2000) or single amino acid substitutions in MA (Freed and Martin 1995; Mammano et al. 1995; Brandano and Stevenson 2012) are sufficient for excluding Env from budding virions.”
Background
Evolution of feline immunodeficiency virus Gag proteins
Burkala, E. J., & Poss, M. L. (2007) · Virus Genes · doi:10.1007/s11262-006-0058-8 · Cited by 13
Structural elements in the Gag polyprotein of feline immunodeficiency virus involved in Gag self-association and assembly
Cerfoglio, J. C. A., González, S. A., & Affranchino, J. L. (2014) · Journal of General Virology · doi:10.1099/vir.0.065151-0 · Cited by 14

Authors: Dorfman, T., Mammano, F., Haseltine, W. A., & Göttlinger, H. G.
Affiliations: Dana-Farber Cancer Institute (US)
ORCID: Mammano, F
Haseltine, W A
Göttlinger, H G
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
DOI: 10.1128/jvi.68.3.1689-1696.1994
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
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
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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Role of the matrix protein in the virion association of the human immunodeficiency virus type 1 envelope glycoprotein

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