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
Nucleocapsid Promotes Localization of HIV-1 Gag to Uropods That Participate in Virological Synapses between T Cells
Llewellyn, G. N., Hogue, I. B., Grover, J. R., & Ono, A. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1001167 · Cited by 88
“Because MA is essential for specific targeting of Gag to the plasma membrane [11,12,100,133,134,135,136,137,138,139], it is conceivable that MA also regulates specific localization of Gag to uropods.”
Background
Efficient in vivo and in vitro assembly of retroviral capsids from Gag precursor proteins expressed in bacteria
Klikova, M., Rhee, S. S., Hunter, E., & Ruml, T. (1995) · Journal of Virology · doi:10.1128/jvi.69.2.1093-1098.1995 · Cited by 85
“Mutagenesis has been used to define regions of the gag gene product that mediate the assembly process itself (6, 11, 15, 24, 29, 31, 34).”
Method
Evidence that Productive Human Immunodeficiency Virus Type 1 Assembly Can Occur in an Intracellular Compartment
Joshi, A., Ablan, S. D., Soheilian, F., Nagashima, K., & Freed, E. O. (2009) · Journal of Virology · doi:10.1128/jvi.00109-09 · Cited by 83
“Mutational analyses have indicated that the viral determinant of Gag targeting to the PM lies in the MA domain (15, 22, 34, 56, 66, 75, 76).”
Background
Efficient particle formation can occur if the matrix domain of human immunodeficiency virus type 1 Gag is substituted by a myristylation signal
Lee, P. P., & Linial, M. (1994) · Journal of Virology · doi:10.1128/jvi.68.10.6644-6654.1994 · Cited by 89
“In the case of HIV-1, it is clear that a great deal of the matrix domain may be dispensable for assembly (13, 59).”
Background
Quantification of phosphoinositides reveals strong enrichment of PIP2 in HIV-1 compared to producer cell membranes
Mücksch, F., Citir, M., Lüchtenborg, C., Glass, B., Traynor-Kaplan, A., Schultz, C., Brügger, B., & Kräusslich, H.-G. (2019) · Scientific Reports · doi:10.1038/s41598-019-53939-z · Cited by 73
Self-citation
Roles of Matrix, p2, and N-Terminal Myristoylation in Human Immunodeficiency Virus Type 1 Gag Assembly
Morikawa, Y., HOCKLEY, D. J., Nermut, M. V., & Jones, I. M. (2000) · Journal of Virology · doi:10.1128/jvi.74.1.16-23.2000 · Cited by 80
“Since several large and even entire deletions of the MA domain within the Gag precursor have been shown to have little effect on and even to enhance Gag VLP formation (12, 29, 43), in some situations the step could be bypassed because of other dominant assembly domains within Gag precursor.”
Background
Detection of a Trimeric Human Immunodeficiency Virus Type 1 Gag Intermediate Is Dependent on Sequences in the Matrix Protein, p17
Morikawa, Y., Zhang, W., HOCKLEY, D. J., Nermut, M. V., & Jones, I. M. (1998) · Journal of Virology · doi:10.1128/jvi.72.9.7659-7663.1998 · Cited by 75
“Some studies have suggested that MA is dispensable for a form of virus assembly (10, 21, 36), but a larger number of studies suggest a role for MA in normal virus assembly (5, 6, 12, 28, 35).”
Background
Analysis of Minimal Human Immunodeficiency Virus Type 1 gag Coding Sequences Capable of Virus-Like Particle Assembly and Release
Wang, C.-T., Lai, H.-Y., & Li, J.-J. (1998) · Journal of Virology · doi:10.1128/jvi.72.10.7950-7959.1998 · Cited by 70
“It is responsible for membrane association and targeting of the Gag precursors to the plasma membrane (2, 11, 46, 63).”
Background
The Nef protein of human immunodeficiency virus type 1 enhances serine phosphorylation of the viral matrix
Swingler, S., Gallay, P. A., Camaur, D., Song, J., Abo, A., & Trono, D. (1997) · Journal of Virology · doi:10.1128/jvi.71.6.4372-4377.1997 · Cited by 68
Identification of Two Sequences in the Cytoplasmic Tail of the Human Immunodeficiency Virus Type 1 Envelope Glycoprotein That Inhibit Cell Surface Expression
Bültmann, A., Muranyi, W., Seed, B., & Haas, J. (2001) · Journal of Virology · doi:10.1128/jvi.75.11.5263-5276.2001 · Cited by 68
“Due to a direct interaction between Env viral matrix proteins, the carboxy-terminal end of the gp41 cytoplasmic domain appears to inﬂuence the incorporation of glycoproteins into virions (13, 15, 16, 22, 25, 28, 39, 72, 73).”
Comparison of the NMR and X‐ray structures of the HIV‐1 matrix protein: Evidence for conformational changes during viral assembly
Massiah, M. A., Worthylake, D. K., Christensen, A. M., Sundquist, W. I., Hill, C. P., & Summers, M. F. (1996) · Protein Science · doi:10.1002/pro.5560051202 · Cited by 65
Intracellular Transport of Retroviral Capsid Components
Kräusslich, H., & Welker, R. (1996) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-80145-7_2 · Cited by 65
Self-citation
HIV Cell-to-Cell Transmission Requires the Production of Infectious Virus Particles and Does Not Proceed through Env-Mediated Fusion Pores
Monel, B., Beaumont, É., Vendrame, D., Schwartz, O., Brand, D., & Mammano, F. (2012) · Journal of Virology · doi:10.1128/jvi.06478-11 · Cited by 67
“Mutations affecting residues of the MA protein induce a range of perturbations in the virus assembly process, including a defect in particle release (24, 62), and the redirection of assembly to the endoplasmic reticulum or other intracellular compartments, in particular multivesicular bodies or late endosomes (21, 27,…”
Background
HIV-1 matrix protein p17 increases the production of proinflammatory cytokines and counteracts IL-4 activity by binding to a cellular receptor
Francesco, M. A. D., Baronio, M., Fiorentini, S., Signorini, C., Bonfanti, C., Poiesi, C., Popovič, M., Grassi, M., Garrafa, E., Bozzo, L., et al. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.142274699 · Cited by 64
A Human Nuclear Shuttling Protein That Interacts with Human Immunodeficiency Virus Type 1 Matrix Is Packaged into Virions
Gupta, K., Ott, D., Hope, T., Siliciano, R., & Boeke, J. (2000) · Journal of Virology · doi:10.1128/jvi.74.24.11811-11824.2000 · Cited by 68
“The Gag proteins recruit viral genomic RNA, as well as viral and host cell proteins, into the newly budding virion (17, 57, 68).”
Background
Structural analysis of human immunodeficiency virus type 1 Gag protein interactions, using cysteine-specific reagents
McDermott, J., Farrell, L. E., Ross, R., & Barklis, E. (1996) · Journal of Virology · doi:10.1128/jvi.70.8.5106-5114.1996 · Cited by 62
“Mutations of MA are characterized by a reduction in membrane binding (33, 39), impaired assembly (8, 33) or assembly on intracellular membranes (8, 16), reduced incorporation of viral envelope products (Env) into virus particles (8, 43), and/or impaired Env function (39, 42).”
Background
Retroviral Matrix Proteins: A Structural Perspective
Conte, M. R., & Matthews, S. (1998) · Virology · doi:10.1006/viro.1998.9206 · Cited by 61
Sequence requirements for encapsidation of deletion mutants and chimeras of human immunodeficiency virus type 1 Gag precursor into retrovirus-like particles
Carrière, C., Gay, B., Chazal, N., Morin, N., & Boulanger, P. A. (1995) · Journal of Virology · doi:10.1128/jvi.69.4.2366-2377.1995 · Cited by 62
Phosphoinositides Direct Equine Infectious Anemia Virus Gag Trafficking and Release
Fernandes, F., Chen, K., Ehrlich, L. S., Jin, J., Chen, M. H., Medina, G. N., Symons, M. H., Montelaro, R. C., Donaldson, J. G., Tjandra, N., et al. (2010) · Traffic · doi:10.1111/j.1600-0854.2010.01153.x · Cited by 61
“EIAV has been shown to localize in internal compartments; hence, the significance of its interaction with PI(4,5)P2 is unclear.”
BackgroundInfluential
Human Immunodeficiency Virus Type 1 Reverse Transcriptase and Early Events in Reverse Transcription
Arts, E. J., & Wainberg, M. A. (1996) · Advances in virus research · doi:10.1016/s0065-3527(08)60071-8 · Cited by 62
Three-dimensional structure of the HTLV-II matrix protein and comparative analysis of matrix proteins from the different classes of pathogenic human retroviruses
Christensen, A. M., Massiah, M. A., Turner, B. G., Sundquist, W. I., & Summers, M. F. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0700 · Cited by 59
Mutational Analysis of the Human Immunodeficiency Virus Type 1 Vpu Transmembrane Domain That Promotes the Enhanced Release of Virus-Like Particles from the Plasma Membrane of Mammalian Cells
Paul, M., Mazumder, S., Raja, N. U., & Jabbar, M. A. (1998) · Journal of Virology · doi:10.1128/jvi.72.2.1270-1279.1998 · Cited by 60
Atomic Resolution Structure of Moloney Murine Leukemia Virus Matrix Protein and Its Relationship to Other Retroviral Matrix Proteins
Riffel, N., Harlos, K., Iourin, O., Rao, Z., Kingsman, A. J., Stuart, D. I., & Fry, E. E. (2002) · Structure · doi:10.1016/s0969-2126(02)00896-1 · Cited by 60
Basic residues in the Mason-Pfizer monkey virus gag matrix domain regulate intracellular trafficking and capsid-membrane interactions
Stansell, E., Apkarian, R., Haubova, S., Diehl, W. E., Tytler, E. M., & Hunter, E. (2007) · Journal of Virology · doi:10.1128/jvi.00657-07 · Cited by 59
“MA mutants of HIV-1, which alter or abolish the globular head of MA and in which myristate may be constitutively exposed, could also be seen assembling at and budding into intracellular vesicles (10, 11, 30, 38).”
Background
Nucleocapsid and Matrix Protein Contributions to Selective Human Immunodeficiency Virus Type 1 Genomic RNA Packaging
Poon, D. T. K., Li, G.-D., & Aldovini, A. (1998) · Journal of Virology · doi:10.1128/jvi.72.3.1983-1993.1998 · Cited by 70
“Immature and mature particles were also present among the cells transfected with plasmids pHXDMA, confirming previous observations (15, 30, 31), and pHX/MT-NC (Fig.”
Result
The three‐dimensional solution structure of the matrix protein from the type D retrovirus, the Mason–Pfizer monkey virus, and implications for the morphology of retroviral assembly
Conte, M. R., Rumlová, M., Hunter, E., Ruml, T., & Matthews, S. (1997) · The EMBO Journal · doi:10.1093/emboj/16.19.5819 · Cited by 59
“This, together with other studies (Yu et al., 1992; Fäcke et al., 1993;Yuan et al., 1993; Freed et al., 1994), implies a key role for the MA in the morphogenesis of retroviruses.”
Result
Identification of a cytoplasmic targeting/retention signal in a retroviral Gag polyprotein
Choi, G., Park, S., Choi, B., Hong, S., Lee, J., Hunter, E., & Rhee, S. S. (1999) · Journal of Virology · doi:10.1128/jvi.73.7.5431-5437.1999 · Cited by 61
“Others have reported that human immunodeficiency virus and Moloney murine leukemia virus (MoMuLV) with amino acid substitutions or deletions in MA undergo capsid assembly within cytoplasmic vacuoles rather than at the plasma membrane (3, 10, 12, 38).”
Organization of HIV-1 Capsid Proteins on a Lipid Monolayer
Barklis, E., McDermott, J., Wilkens, S., Fuller, S., & Thompson, D. H. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.13.7177 · Cited by 57
Arbitrary-Region Raster Image Correlation Spectroscopy
Hendrix, J., Dekens, T., Schrimpf, W., & Lamb, D. C. (2016) · Biophysical Journal · doi:10.1016/j.bpj.2016.09.012 · Cited by 54
“Previously, it had been shown that, under some conditions, the incorrect assembly of Gag can occur in the ER (30).”
Background
Comparative morphology and structural classification of retroviruses.
Nermut, M., & Hockley, D. (1996) · Current Topics in Microbiology and Immunology · doi:10.1007/978-3-642-80145-7_1 · Cited by 60
Analysis of HIV-1 Gag Protein Interactions via Biotin Ligase Tagging
Ritchie, C., Cylinder, I., Platt, E. J., & Barklis, E. (2015) · Journal of Virology · doi:10.1128/jvi.03584-14 · Cited by 57
“observations (30, 51-52, 69) Gag proteins expressed from MA-BirA* and MA-BirA* gave 382”
Background
Virion Envelope Content, Infectivity, and Neutralization Sensitivity of Simian Immunodeficiency Virus
Yuste, E., Johnson, W., Pavlakis, G., & Desrosiers, R. (2005) · Journal of Virology · doi:10.1128/jvi.79.19.12455-12463.2005 · Cited by 57
Regulation of cargo transfer between ESCRT-0 and ESCRT-I complexes by flotillin-1 during endosomal sorting of ubiquitinated cargo
Meister, M., Bänfer, S., Gärtner, U., Koskimies, J., Amaddii, M., Jacob, R., & Tikkanen, R. (2017) · Oncogenesis · doi:10.1038/oncsis.2017.47 · Cited by 52
Human immunodeficiency virus type 1 capsid formation in reticulocyte lysates
Spearman, P. W., & Ratner, L. (1996) · Journal of Virology · doi:10.1128/jvi.70.11.8187-8194.1996 · Cited by 51
“These data are consistent with data from mammalian cell systems in which matrixdeleted HIV Gag proteins have been shown to form immature intracellular particles (8, 25).”
BackgroundResult
Human immunodeficiency virus type 1 MA deletion mutants expressed in baculovirus-infected cells: cis and trans effects on the Gag precursor assembly pathway
Chazal, N., Gay, B., Carrière, C., Tournier, J., & Boulanger, P. A. (1995) · Journal of Virology · doi:10.1128/jvi.69.1.365-375.1995 · Cited by 51
Mutations in the Ty3 major homology region affect multiple steps in Ty3 retrotransposition
Orlinsky, K. J., Gu, J., Hoyt, M., Sandmeyer, S. B., & Menees, T. M. (1996) · Journal of Virology · doi:10.1128/jvi.70.6.3440-3448.1996 · Cited by 50
The membrane-binding domain of the Rous sarcoma virus Gag protein
Verderame, M., Nelle, T., & Wills, J. W. (1996) · Journal of Virology · doi:10.1128/jvi.70.4.2664-2668.1996 · Cited by 61
HIV-1 replication cycle
Ferguson, M. R., Rojo, D. R., von Lindern, J. J., & O’Brien, W. A. (2002) · Clinics in Laboratory Medicine · doi:10.1016/s0272-2712(02)00015-x · Cited by 48
“During assembly of the virus in host cells, the N-terminal MA domain of Gag targets the protein to the plasma membrane and serves to incorporate the membrane-spanning envelope proteins into the newly forming virions [10,11].”
Background
HEED, the Product of the Human Homolog of the Murineeed Gene, Binds to the Matrix Protein of HIV-1
Peytavi, R., Hong, S. S., Gay, B., d’Angeac, A. D., Selig, L., Bénichou, S., Bénarous, R., & Boulanger, P. A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.3.1635 · Cited by 49
Endophilins interact with Moloney murine leukemia virus Gag and modulate virion production
Wang, M. Q., Kim, W., Gao, G., Torrey, T. A., Morse, H. C., Camilli, P. V. D., & Goff, S. P. (2003) · Journal of Biology · doi:10.1186/1475-4924-3-4 · Cited by 49
Membrane-induced alterations in HIV-1 gag and matrix protein-protein interactions
Scarlata, S., Ehrlich, L. S., & Carter, C. A. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1615 · Cited by 48
A molecular determinant of human immunodeficiency virus particle assembly located in matrix antigen p17
Morikawa, Y., Kishi, T., Zhang, W. H., Nermut, M. V., HOCKLEY, D. J., & Jones, I. M. (1995) · Journal of Virology · doi:10.1128/jvi.69.7.4519-4523.1995 · Cited by 47
“Mutational analysis of the matrix domain has shown it to contain signals for nuclear localization (2), transport to the plasma membrane (8, 9, 48), and the coincorporation of envelope antigen (47) in addition to signals for particle assembly (9).”
Background
Ubiquitination of Human Immunodeficiency Virus Type 1 Gag Is Highly Dependent on Gag Membrane Association
Jäger, S., Gottwein, E., & Kräusslich, H. (2007) · Journal of Virology · doi:10.1128/jvi.00044-07 · Cited by 47
“Deletion of the globular head of MA (pNL43 p17) and a point mutation within the HIV-1 MA domain (pNL43/87VE) had previously been shown to retarget Gag to intracellular membranes of the endoplasmic reticulum and the MVB, respectively (6, 7, 31).”
BackgroundMethodSelf-citation
Efficient assembly of an HIV-1/MLV Gag-chimeric virus in murine cells
Chen, B. K., Rousso, I. Y., Shim, S., & Kim, P. S. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.261563198 · Cited by 47
Efficient support of virus-like particle assembly by the HIV-1 packaging signal
Comas‐García, M., Kroupa, T., Datta, S. A., Harvin, D., Hu, W.-S., & Rein, A. R. (2018) · eLife · doi:10.7554/elife.38438 · Cited by 48
HIV-1 matrix protein p17: A candidate antigen for therapeutic vaccines against AIDS
Fiorentini, S., Giagulli, C., Caccuri, F., Magiera, A. K., & Caruso, A. (2010) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2010.08.005 · Cited by 45

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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