Cited by 198HIV Research and TreatmentT-cell and Retrovirus StudiesCellular transport and secretion

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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

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Fäcke, M, Janetzko, A, Shoeman, R L, Kräusslich, H G·1993·Journal of Virology

DOI 10.1128/jvi.67.8.4972-4980.1993PMC PMC237885

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Abstract

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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Background
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Background
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Background
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Background
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Li, S., Bozzo, L., Wu, Z., Lu, W., & Romerio, F. (2010) · PubMed · Cited by 10
Mutation affecting the cytoplasmic domain of the Moloney murine leukemia virus envelope protein: rapid reversion during replication
Granowitz, C. B., Berkowitz, R. D., & Goff, S. P. (1996) · Virus Research · doi:10.1016/0168-1702(95)01278-8 · Cited by 10
Specificity of Plasma Membrane Targeting by the Rous Sarcoma Virus Gag Protein
Scheifele, L. Z., Rhoads, J. D., & Parent, L. J. (2002) · Journal of Virology · doi:10.1128/jvi.77.1.470-480.2003 · Cited by 10
“Numerous mutations and deletions affecting the polybasic stretch between amino acids 15 and 31 of the HIV M domain result in relocalization of the Gag precursor to intracellular membranes (10, 13, 19, 32, 48, 57).”
Background
Retrotransposition of Nonviral RNAs in an Avian Packaging Cell Line
Lum, R., & Linial, M. L. (1998) · Journal of Virology · doi:10.1128/jvi.72.5.4057-4064.1998 · Cited by 10
“Rather than resulting from autoretrofection events, we think that these retrogenes are episomes that may have resulted from viral budding into intracellular compartments (9, 19) or from retrogenes formed after extracellular reinfection that are blocked at integration.”
Background
Targeting Human Immunodeficiency Virus Type 1 Assembly, Maturation and Budding
Wapling, J., Srivastava, S., Shehu-Xhilaga, M., & Tachedjian, G. (2007) · Drug Target Insights · doi:10.1177/117739280700200020 · Cited by 11
“Membrane targeting of Gag is mediated by the N-terminal myristoyl group in concert with conserved basic amino acids at the N-terminus of the MA domain of Gag (Bryant and Ratner, 1990; Facke et al. 1993; Ono and Freed, 1999; Ono et al. 2000).”
Transport and processing of the Rous sarcoma virus Gag protein in the endoplasmic reticulum
Krishna, N. K., Weldon, R. A., & Wills, J. W. (1996) · Journal of Virology · doi:10.1128/jvi.70.3.1570-1579.1996 · Cited by 8
The gag proteins of human immunodeficiency virus type 1: mechanisms of virus assembly and possibilities for interference
Modrow, S., Kattenbeck, B., von Poblotzki, A., Niedrig, M., Wagner, R., & Wolf, H. J. (1994) · Medical Microbiology and Immunology · doi:10.1007/bf00194171 · Cited by 8
“When residues 16 to 99 were deleted, the release of HIV particles from cells was reduced up to tenfold, budding events occurred preferentially at the membrane of the ER and incorporation of gpl60 into the particulate structures was inhibited [24, 51].”
Rescue of internal scaffold-deleted Mason-Pfizer monkey virus particle production by plasma membrane targeting
Sakalian, M., & Rapp, N. D. (2005) · Virology · doi:10.1016/j.virol.2005.09.066 · Cited by 7
Tracking the Assembly Pathway of Human Immunodeficiency Virus Type 1 Gag Deletion Mutants by Immunogold Labeling
Wang, J.-J., Sandefur, S., Spearman, P., Ou, C.-C. T., Chiang, P., & Ratner, L. (2001) · Applied immunohistochemistry & molecular morphology (Print) · doi:10.1097/00129039-200112000-00014 · Cited by 6
Probing the interactions of the HIV-1 matrix protein-derived polybasic region with lipid bilayers: insights from AFM imaging and force spectroscopy
Aryal, C. M., & Pan, J. (2024) · European Biophysics Journal · doi:10.1007/s00249-023-01697-2 · Cited by 6
“The highly basic region, characterized by a dense clus - ter of positively charged amino acid residues, represents the second domain regulating MA’s membrane binding (Facke et al. 1993; Cannon et al. 1997; Ono et al. 2000; Hermida-Matsumoto and Resh 2000).”
The Envelope Cytoplasmic Tail of HIV-1 Subtype C Contributes to Poor Replication Capacity through Low Viral Infectivity and Cell-to-Cell Transmission
da Silva, E. S., Mulinge, M. M., Lemaire, M., Masquelier, C., Beraud, C., Rybicki, A., Servais, J.-Y., Iserentant, G., Schmit, J., Seguin‐Devaux, C., et al. (2016) · PLoS ONE · doi:10.1371/journal.pone.0161596 · Cited by 7
“Basic residues 17–21 mediating MA interaction with Env [137] [38, 40–42, 44, 70, 138] or AA involved in p55Gag trafficking via adaptor proteins (Y132 and V135 at the MA/CA junction) [49, 68, 139, 140] were also conserved.”
Background
Chimeric HIV-1 containing SIV matrix exhibit enhanced assembly in murine cells and replicate in a cell-type-dependent manner in human T cells
Chen, P., Hübner, W., Riviere, K., Liu, Y., & Chen, B. K. (2006) · Virology · doi:10.1016/j.virol.2006.02.022 · Cited by 6
“) f Because small sequence differences in HIV-1 MA can affect the efficiency of Env incorporation (Dorfman et al., 1994; Freed and Martin, 1995), we examined the ability of SHIV(MA) and SHIV(MA N1–96) viruses to incorporate native HIV-1 Env or ΔCT Env.”
Background
Spectroscopic study of an HIV‐1 capsid protein major homology region peptide analog
Clish, C. B., Peyton, D. H., & Barklis, E. (1996) · FEBS Letters · doi:10.1016/0014-5793(95)01419-5 · Cited by 6
HIV-1 Matrix Protein p17 Modulates in Vivo Preactivated Murine T-Cell Response and Enhances the Induction of Systemic and Mucosal Immunity Against Intranasally Co-administered Antigens
Fiorentini, S., Becker, P., Marini, E., Marconi, P., Avolio, M., Tosti, G., Link, C., Manservigi, R., Guzmán, C., & Caruso, A. (2006) · Viral immunology · doi:10.1089/vim.2006.19.177 · Cited by 7
Hydrophilicity dependent budding and secretion of chimeric HIV Gag-V3 virus-like particles
Luo, L., Li, Y., Ha, S. D., & Kang, C. Y. (2007) · Virus Genes · doi:10.1007/s11262-007-0108-x · Cited by 6
Inositol Phosphates and Retroviral Assembly: A Cellular Perspective
Ricana, C. L., & Dick, R. A. (2021) · Viruses · doi:10.3390/v13122516 · Cited by 5
“Knowing that IP6 promotes in vitro assembly of full-length HIV Gag, but was not needed for Gag∆MA (here ∆MA refers to an internal MA deletion of amino acids 16–99 first described in [40,41]; due to the persistence of this annotation in the literature we will use ∆MA to refer to ∆16–99 as well unless otherwise noted),…”
Method
Assembly and Release of Human Immunodeficiency Virus Type 1 Gag Proteins Containing Tandem Repeats of the Matrix Protein Coding Sequences in the Matrix Domain
Wang, C.-T., Chen, S. S.-L., & Chiang, C.-C. (2000) · Virology · doi:10.1006/viro.2000.0655 · Cited by 5
Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication
Jehad, M. A., Ali, L. M., Pillai, V. N., Prabhu, S. G., Mustafa, F., & Rizvi, T. A. (2026) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuaf066 · Cited by 5
“Along the same lines, 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 cyto-plasm or intracellular membranes, such as the endoplasmic reticulum (Fäcke et al. 1993 , Cannon et al. 1997 ).”
Reversible aggregation of HIV-1 Gag proteins mediated by nucleic acids
Chen, Z., & Cheng, W. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.12.054 · Cited by 5
“Previously, it was reported that this large truncation in the MA domain changed the site of virus budding from plasmamembrane to endoplasmic reticulum, but the morphology of resulting virions remains largely unchanged [14].”
Background
The central domain of the matrix protein of HIV-1: influence on protein structure and virus infectivity
Ellenrieder, A.-D., Kremer, W., Kattenbeck, B., Hantschel, O. D., Horn, G., Kalbitzer, H. R., & Modrow, S. (2004) · Biological Chemistry · doi:10.1515/bc.2004.026 · Cited by 4
“In addition, the capacity to form particulate structures was maintained after deletion of large parts of this protein but the assembly process was redirected to the endoplasmic reticulum (Fäcke et al., 1993).”
BackgroundResultInfluential
HIV-1 p17 matrix protein enhances type I interferon responses through the p17–OLA1–STING axis
Zhang, L., Li, S. C., Xu, X., Ma, C., Zhang, P., Ji, W., & Liu, X. (2023) · Journal of Cell Science · doi:10.1242/jcs.261500 · Cited by 3
Evidence that Vpu Modulates HIV-1 Gag-Envelope Interaction towards Envelope Incorporation and Infectivity in a Cell Type Dependent Manner
Gautam, A., & Bhattacharya, J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0061388 · Cited by 3
“Previous studies demonstrated that specific amino acid substitutions in the Gag MA region abrogate incorporation of HIV-1 Env glycoproteins into virus particles [24–26] and redirects particle assembly to intracellular sites [27,28].”
Background
Genomic and antigenic variation among rotavirus strains circulating in a large city of Argentina
Espul, C., Cuello, H., Martínez, N. E., de Centorbi, O. N. P., O’Ryan, M., Jackson, L., Campos, F., & Matson, D. O. (2000) · Journal of Medical Virology · doi:10.1002/1096-9071(200008)61:4 · Cited by 10
RNA ‐centric world of retroviruses: unravelling the molecular strategies of genomic RNA packaging
Jehad, M. A., Prabhu, S., Ali, L. M., Pillai, V. N., Mustafa, F., & Rizvi, T. A. (2026) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1002/brv.70188 · Cited by 2
Human Immunodeficiency Virus From Virus Structure to Pathogenesis
Gelderblom, H. R., & Böller, K. (2005) · Kluwer Academic Publishers eBooks · doi:10.1007/0-306-47650-9_11 · Cited by 2
HIV-1 Assembly and Cellular Trafficking Pathways: Current Understanding and Potential for Future Therapeutics
Spearman, P. W. (2007) · Future HIV Therapy · doi:10.2217/17469600.1.1.113 · Cited by 2
“Deletion of a large portion of the globular head of MA while retaining the N-terminal myristoylation motif of Gag leads to budding within the endoplasmic reticulum [8], while more subtle mutations in helix 1 or MA residues 84–88 redirect assembly from the plasma membrane to intracellular locations [9].”
Background
Intracellular trafficking of HIV-1 Gag via Syntaxin 6-positive compartments/vesicles: Involvement in tumor necrosis factor secretion
Tsurutani, N., Momose, F., Ogawa, K., Sano, K., & Morikawa, Y. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.105687 · Cited by 2
Proteolytic cleavage events in the maturation of HIV-1 reverse transcriptase
Abram, M. E. (2005) · D-Scholarship@Pitt (University of Pittsburgh) · Cited by 1
Virus Assembly as a Target for Antiretroviral Therapy
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Die Rolle von p6* für den HI-viralen Replikationszyklus
Leiherer, A. (2009) · University of Regensburg Publication Server (University of Regensburg) · doi:10.5283/epub.12102
Co-evolution of HIV-1 Protease and its Substrates: A Dissertation
Kolli, M. (2009) · The Journal of the American Medical Association (JAMA) Network (American Medical Association) · doi:10.13028/hnsw-f822
Herstellung und Evaluierung transdominant negativ wirksamer Varianten des HIV-1 gruppenspezifischen Antigens als Basiskomponente einer HIV-1-Gentherapie
Hammer, D. (2006) · University of Regensburg Publication Server (University of Regensburg) · doi:10.5283/epub.10447
Investigation of the C-Terminal Helix of HIV-1 Matrix: A Region Essential for Multiple Functions in the Viral Life Cycle: A Dissertation
Brandano, L. A. (2011) · The Journal of the American Medical Association (JAMA) Network (American Medical Association) · doi:10.13028/5zmj-9x81
Determinants of HIV-1 Gag Localization to Uropods in Polarized T Cells and the Role Uropods Play in Virus Spread.
Llewellyn, G. N. (2012) · Deep Blue (University of Michigan)
A molecular study of the immunopathogenesis of TB spondylitis in HIV -infected and -uninfected patients.
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Background
Expression, Purification and Characterization of Hiv-1 Capsid Precursor Protein p41
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Authors: Fäcke, M., Janetzko, A., Shoeman, R. L., & Kräusslich, H. G.
Affiliations: German Cancer Research Center (DE)
ORCID: Shoeman, R L
Kräusslich, H G
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
DOI: 10.1128/jvi.67.8.4972-4980.1993
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
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
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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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

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