Cited by 336HIV Research and TreatmentT-cell and Retrovirus StudiesHIV/AIDS drug development and treatment

The DOI matches its Crossref record; 65 of the 65 references it cites were found in a registry or an index.

Sequential Steps in Human Immunodeficiency Virus Particle Maturation Revealed by Alterations of Individual Gag Polyprotein Cleavage Sites

Open access

Wiegers, Klaus, Rutter, Gabriel, Kottler, Hubert, Tessmer, Uwe, Hohenberg, Heinz, Kräusslich, Hans-Georg·1998·Journal of Virology

DOI 10.1128/jvi.72.4.2846-2854.1998PMC PMC109729

Open this paper in CoChat — free account

Abstract

Retroviruses are produced as immature particles containing structural polyproteins, which are subsequently cleaved by the viral proteinase (PR). Extracellular maturation leads to condensation of the spherical core to a capsid shell formed by the capsid (CA) protein, which encases the genomic RNA complexed with nucleocapsid (NC) proteins. CA and NC are separated by a short spacer peptide (spacer peptide 1 [SP1]) on the human immunodeficiency virus type 1 (HIV-1) Gag polyprotein and released by sequential PR-mediated cleavages. To assess the role of individual cleavages in maturation, we constructed point mutations abolishing cleavage at these sites, either alone or in combination. When all three sites between CA and NC were mutated, immature particles containing stable CA-NC were observed, with no apparent effect on other cleavages. Delayed maturation with irregular morphology of the ribonucleoprotein core was observed when cleavage of SP1 from NC was prevented. Blocking the release of SP1 from CA, on the other hand, yielded normal condensation of the ribonucleoprotein core but prevented capsid condensation. A thin, electron-dense layer near the viral membrane was observed in this case, and mutant capsids were significantly less stable against detergent treatment than wild-type HIV-1. We suggest that HIV maturation is a sequential process controlled by the rate of cleavage at individual sites. Initial rapid cleavage at the C terminus of SP1 releases the RNA-binding NC protein and leads to condensation of the ribonucleoprotein core. Subsequently, CA is separated from the membrane by cleavage between the matrix protein and CA, and late release of SP1 from CA is required for capsid condensation.

Integrity signals

Registry

Crossref · 10.1128/jvi.72.4.2846-2854.1998

Cites

65 of 65 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

A low-viscosity epoxy resin embedding medium for electron microscopy.
Spurr, A. (1969) · Journal of Ultrastructure Research · doi:10.1016/s0022-5320(69)90033-1 · Cited by 13,268
Rapid and efficient site-specific mutagenesis without phenotypic selection.
Kunkel, T. A. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.2.488 · Cited by 7,309
High-Efficiency Transformation of Mammalian Cells by Plasmid DNA
Chen, C., & Okayama, H. (1987) · Molecular and Cellular Biology · doi:10.1128/mcb.7.8.2745 · Cited by 5,327
On the size of the active site in proteases. I. Papain
Schechter, I., & Berger, A. (1967) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(67)80055-x · Cited by 5,256
Production of acquired immunodeficiency syndrome-associated retrovirus in human and nonhuman cells transfected with an infectious molecular clone
Adachi, A., Gendelman, H. E., Koenig, S., Folks, T. M., Willey, R. L., Rabson, A. B., & Martín, M. Á. (1986) · Journal of Virology · doi:10.1128/jvi.59.2.284-291.1986 · Cited by 2,805
Simplified method for silver staining of proteins in polyacrylamide gels and the mechanism of silver staining
Heukeshoven, J., & Dernick, R. (1985) · Electrophoresis · doi:10.1002/elps.1150060302 · Cited by 1,339
Active human immunodeficiency virus protease is required for viral infectivity
Kohl, N. E., Emini, E. A., Schleif, W. A., Davis, L. J., Heimbach, J. C., Dixon, R. A., Scolnick, E. M., & Sigal, I. S. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.13.4686 · Cited by 1,307
Infection of HTLV-III/LAV in HTLV-I-Carrying Cells MT-2 and MT-4 and Application in a Plaque Assay
Harada, S., Koyanagi, Y., & Yamamoto, N. (1985) · Science · doi:10.1126/science.2992081 · Cited by 857
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
Assembly and release of HIV-1 precursor Pr55gag virus-like particles from recombinant baculovirus-infected insect cells
Gheysen, D., Jacobs, E. J., de Foresta, F., Thiriart, C., Francotte, M., Thines, D., & Wilde, M. D. (1989) · Cell · doi:10.1016/0092-8674(89)90873-8 · Cited by 743

Show all 65 references

Research works printed but not linked: 2

10.1128/mcb.7.8.2745-2752.1987 · DOI
10.1111/j.1432-1033.1995.tb20249.x · DOI

Sorted by citations

Structure‐Based Design of Inhibitors of Protein–Protein Interactions: Mimicking Peptide Binding Epitopes
Pelay‐Gimeno, M., Glas, A., Koch, O., & Grossmann, T. N. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201412070 · Cited by 740
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
Structural 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
PA-457: A potent HIV inhibitor that disrupts core condensation by targeting a late step in Gag processing
Li, F., Goila-Gaur, R., Salzwedel, K., Kilgore, N., Reddick, M., Matallana, C., Castillo, A., Zoumplis, D., Martin, D. E., Orenstein, J. M., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2234683100 · Cited by 427
Functional Surfaces of the Human Immunodeficiency Virus Type 1 Capsid Protein
von Schwedler, U. K., Stray, K. M., Garrus, J. E., & Sundquist, W. I. (2003) · Journal of Virology · doi:10.1128/jvi.77.9.5439-5450.2003 · Cited by 421
An atomic model of HIV-1 capsid-SP1 reveals structures regulating assembly and maturation
Schur, F. K. M., Obr, M., Hagen, W. J. H., Wan, W., Jakobi, A. J., Kirkpatrick, J. M., Sachse, C., Kräusslich, H., & Briggs, J. A. G. (2016) · Science · doi:10.1126/science.aaf9620 · Cited by 423
Fifteen years of HIV Protease Inhibitors: raising the barrier to resistance
Wensing, A. M. J., van Maarseveen, N. M., & Nijhuis, M. (2009) · Antiviral Research · doi:10.1016/j.antiviral.2009.10.003 · Cited by 336
Proteolytic refolding of the HIV‐1 capsid protein amino‐terminus facilitates viral core assembly
von Schwedler, U. K., Stemmler, T. L., Klishko, V. Y., Li, S., Albertine, K. H., Davis, D. R., & Sundquist, W. I. (1998) · The EMBO Journal · doi:10.1093/emboj/17.6.1555 · Cited by 337
Functional Profiling of Recombinant NS3 Proteases from All Four Serotypes of Dengue Virus Using Tetrapeptide and Octapeptide Substrate Libraries
Li, J., Lim, S. P., Beer, D., Patel, V. M., Wen, D., Tumanut, C., Tully, D. C., Williams, J. A. S., Jiřiček, J., Priestle, J. P., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500588200 · Cited by 251
A conformational switch controlling HIV‐1 morphogenesis
Gross, I., Hohenberg, H., Wilk, T., Wiegers, K. J., Grättinger, M., Müller, B., Fuller, S., & Kräusslich, H. (2000) · The EMBO Journal · doi:10.1093/emboj/19.1.103 · Cited by 241
Self-citation
A peptide inhibitor of HIV-1 assembly in vitro
Sticht, J., Humbert, M., Findlow, S. C., Bodem, J., Müller, B., Dietrich, U., Werner, J. M., & Kräusslich, H. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb964 · Cited by 224
Coupling of Human Immunodeficiency Virus Type 1 Fusion to Virion Maturation: a Novel Role of the gp41 Cytoplasmic Tail
Wyma, D. J., Jiang, J., Shi, J., Zhou, J., Lineberger, J. E., Miller, M. D., & Aiken, C. (2004) · Journal of Virology · doi:10.1128/jvi.78.7.3429-3435.2004 · Cited by 225
The Molecular Architecture of HIV
Briggs, J. A. G., & Kräusslich, H. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.04.021 · Cited by 228
Biochemical and Structural Analysis of Isolated Mature Cores of Human Immunodeficiency Virus Type 1
Welker, R., Hohenberg, H., Tessmer, U., Huckhagel, C., & Kräusslich, H. (2000) · Journal of Virology · doi:10.1128/jvi.74.3.1168-1177.2000 · Cited by 207
Self-citation
HIV-1 nuclear import in macrophages is regulated by CPSF6-capsid interactions at the nuclear pore complex
Bejarano, D. A., Peng, K., Laketa, V., Börner, K., Jost, K. L., Lucic, B., Glass, B., Lusic, M., Müller, B., & Kräusslich, H.-G. (2019) · eLife · doi:10.7554/elife.41800 · Cited by 197
Revisiting HIV-1 uncoating
Arhel, N. (2010) · Retrovirology · doi:10.1186/1742-4690-7-96 · Cited by 200
Head‐to‐tail dimers and interdomain flexibility revealed by the crystal structure of HIV‐1 capsid protein (p24) complexed with a monoclonal antibody Fab
Berthet-Colominas, C., Monaco, S., Novelli, A., Sibaı̈, G., Mallet, F., & Cusack, S. (1999) · The EMBO Journal · doi:10.1093/emboj/18.5.1124 · Cited by 191
Betulinic acid derivatives as HIV-1 antivirals
Aiken, C., & Chen, C. (2004) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2004.11.001 · Cited by 189
Human immunodeficiency virus type 1 assembly, release, and maturation
Adamson, C. S., & Freed, E. O. (2007) · Advances in Pharmacology · doi:10.1016/s1054-3589(07)55010-6 · Cited by 179
N-Terminal Extension of Human Immunodeficiency Virus Capsid Protein Converts the In Vitro Assembly Phenotype from Tubular to Spherical Particles
Gross, I., Hohenberg, H., Huckhagel, C., & Kräusslich, H. (1998) · Journal of Virology · doi:10.1128/jvi.72.6.4798-4810.1998 · Cited by 173
Self-citation
Small-Molecule Inhibition of Human Immunodeficiency Virus Type 1 Replication by Specific Targeting of the Final Step of Virion Maturation
Zhou, J., Yuan, X., Dismuke, D. J., Forshey, B. M., Lundquist, C. A., Lee, K., Aiken, C., & Chen, C. (2003) · Journal of Virology · doi:10.1128/jvi.78.2.922-929.2004 · Cited by 177
The HIV-1 capsid protein C-terminal domain in complex with a virus assembly inhibitor
Ternois, F., Sticht, J., Duquerroy, S., Kräusslich, H., & Rey, F. A. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb967 · Cited by 176
A Novel Substrate-Based HIV-1 Protease Inhibitor Drug Resistance Mechanism
Nijhuis, M., van Maarseveen, N. M., Lastère, S., Schipper, P. J., Coakley, E. P. G., Glass, B., Rovenska, M., de Jong, D. C. M., Chappey, C., Goedegebuure, I. W., et al. (2007) · PLoS Medicine · doi:10.1371/journal.pmed.0040036 · Cited by 168
A multifunctional serine protease primes the malaria parasite for red blood cell invasion
Koussis, K., Martinez, C., Yeoh, S., Child, M. A., Hackett, F., Knuepfer, E., Juliano, L., Woehlbier, U., Bujard, H., & Blackman, M. J. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.22 · Cited by 167
Assembly and Architecture of HIV
Ganser‐Pornillos, B. K., Yeager, M. J., & Pornillos, O. (2011) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-0980-9_20 · Cited by 178
Nucleocapsid protein function in early infection processes
Thomas, J. A., & Gorelick, R. J. (2008) · Virus Research · doi:10.1016/j.virusres.2007.12.006 · Cited by 162
Opposing Effects of Human Immunodeficiency Virus Type 1 Matrix Mutations Support a Myristyl Switch Model of Gag Membrane Targeting
Paillart, J., & Göttlinger, H. G. (1999) · Journal of Virology · doi:10.1128/jvi.73.4.2604-2612.1999 · Cited by 151
Retroviral proteases and their roles in virion maturation
Konvalinka, J., Kräusslich, H.-G., & Müller, B. (2015) · Virology · doi:10.1016/j.virol.2015.03.021 · Cited by 148
Self-citation
Initial Cleavage of the Human Immunodeficiency Virus Type 1 GagPol Precursor by Its Activated Protease Occurs by an Intramolecular Mechanism
Pettit, S. C., Everitt, L., Choudhury, S., Dunn, B. M., & Kaplan, A. H. (2004) · Journal of Virology · doi:10.1128/jvi.78.16.8477-8485.2004 · Cited by 145
Novel approaches to inhibiting HIV-1 replication
Adamson, C. S., & Freed, E. O. (2009) · Antiviral Research · doi:10.1016/j.antiviral.2009.09.009 · Cited by 149
Human Immunodeficiency Virus gag and protease: partners in resistance
Fun, A., Wensing, A. M. J., Verheyen, J., & Nijhuis, M. (2012) · Retrovirology · doi:10.1186/1742-4690-9-63 · Cited by 139
Processing sites in the human immunodeficiency virus type 1 (HIV-1) Gag-Pro-Pol precursor are cleaved by the viral protease at different rates
Pettit, S. C., Lindquist, J. N., Kaplan, A. H., & Swanstrom, R. I. (2005) · Retrovirology · doi:10.1186/1742-4690-2-66 · Cited by 135
Cryo Electron Tomography of Native HIV-1 Budding Sites
Carlson, L.-A., de Marco, A., Oberwinkler, H., Habermann, A., Briggs, J. A. G., Kräusslich, H.-G., & Grünewald, K. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1001173 · Cited by 133
Self-citation
The Choreography of HIV-1 Proteolytic Processing and Virion Assembly
Lee, S.-K., Potempa, M., & Swanstrom, R. I. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r112.399444 · Cited by 139
Crystal structure of an HIV assembly and maturation switch
Wagner, J. M., Zadrozny, K. K., Chrustowicz, J., Purdy, M. D., Yeager, M. J., Ganser‐Pornillos, B. K., & Pornillos, O. (2016) · eLife · doi:10.7554/elife.17063 · Cited by 136
On the Role of the SP1 Domain in HIV-1 Particle Assembly: a Molecular Switch?
Datta, S. A. K., Temeselew, L. G., Crist, R. M., Soheilian, F., Kamata, A., Mirro, J., Harvin, D., Nagashima, K., Cachau, R. E., & Rein, A. (2011) · Journal of Virology · doi:10.1128/jvi.00006-11 · Cited by 127
In Vitro Resistance to the Human Immunodeficiency Virus Type 1 Maturation Inhibitor PA-457 (Bevirimat)
Adamson, C. S., Ablan, S. D., Boeraș, I., Goila-Gaur, R., Soheilian, F., Nagashima, K., Li, F., Salzwedel, K., Sakalian, M., Wild, C. T., et al. (2006) · Journal of Virology · doi:10.1128/jvi.01369-06 · Cited by 124
The HIV-1 assembly machine
Göttlinger, H. G. (2001) · AIDS · doi:10.1097/00002030-200100005-00003 · Cited by 124
Association of Nef with the Human Immunodeficiency Virus Type 1 Core
Kotov, A., Zhou, J., Flicker, P. F., & Aiken, C. (1999) · Journal of Virology · doi:10.1128/jvi.73.10.8824-8830.1999 · Cited by 123
Delivering Cas9/sgRNA ribonucleoprotein (RNP) by lentiviral capsid-based bionanoparticles for efficient ‘hit-and-run’ genome editing
Lyu, P., Javidi-Parsijani, P., Atala, A., & Lu, B. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz605 · Cited by 123
Binding and Susceptibility to Postentry Restriction Factors in Monkey Cells Are Specified by Distinct Regions of the Human Immunodeficiency Virus Type 1 Capsid
Owens, C. M., Song, B., Perron, M. J., Yang, P. C., Stremlau, M. H., & Sodroski, J. (2004) · Journal of Virology · doi:10.1128/jvi.78.10.5423-5437.2004 · Cited by 118
HIV-1 Maturation Inhibitor Bevirimat Stabilizes the Immature Gag Lattice
Keller, P. W., Adamson, C. S., Heymann, J. B., Freed, E. O., & Steven, A. C. (2010) · Journal of Virology · doi:10.1128/jvi.01926-10 · Cited by 116
Structural Analysis of HIV-1 Maturation Using Cryo-Electron Tomography
de Marco, A., Müller, B., Glass, B., Riches, J. D., Kräusslich, H.-G., & Briggs, J. A. G. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1001215 · Cited by 114
Replacement of the P1 Amino Acid of Human Immunodeficiency Virus Type 1 Gag Processing Sites Can Inhibit or Enhance the Rate of Cleavage by the Viral Protease
Pettit, S. C., Henderson, G. J., Schiffer, C. A., & Swanstrom, R. I. (2002) · Journal of Virology · doi:10.1128/jvi.76.20.10226-10233.2002 · Cited by 112
Model for lentivirus capsid core assembly based on crystal dimers of EIAV p26
Jin, Z., Jin, L., Peterson, D. L., & Lawson, C. L. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2443 · Cited by 113
Structure and self-association of the Rous sarcoma virus capsid protein
Kingston, R. L., Fitzon-Ostendorp, T., Eisenmesser, E. Z., Schatz, G. W., Vogt, V. M., Post, C. B., & Rossmann, M. G. (2000) · Structure · doi:10.1016/s0969-2126(00)00148-9 · Cited by 112
Feline Immunodeficiency Virus (FIV) as A Model for Study of Lentivirus Infections: Parallels with HIV
Elder, J. H., Lin, Y., Fink, E. A., & Grant, C. K. (2010) · Current HIV Research · doi:10.2174/157016210790416389 · Cited by 109
Cryo-electron microscopy of tubular arrays of HIV-1 Gag resolves structures essential for immature virus assembly
Bharat, T. A. M., Castillo Menendez, L. R., Hagen, W. J. H., Lux, V., Igonet, S., Schorb, M., Schur, F. K. M., Kräusslich, H.-G., & Briggs, J. A. G. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1401455111 · Cited by 107
Maturation of the matrix and viral membrane of HIV-1
Qu, K., Ke, Z., Žíla, V., Anders‐Össwein, M., Glass, B., Muecksch, F., Müller, R., Schultz, C., Müller, B., Kräusslich, H., et al. (2021) · Science · doi:10.1126/science.abe6821 · Cited by 107
HIV-1 Gag Processing Intermediates Trans-dominantly Interfere with HIV-1 Infectivity
Müller, B., Anders‐Össwein, M., Akiyama, H., Welsch, S., Glass, B., Nikovics, K., Clavel, F., Tervo, H.-M., Keppler, O. T., & Kräusslich, H. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.027144 · Cited by 113
Characterization of a Putative α-Helix across the Capsid-SP1 Boundary That Is Critical for the Multimerization of Human Immunodeficiency Virus Type 1 Gag
Liang, C., Hu, J., Russell, R. S., Roldán, A., Kleiman, L., & Wainberg, M. A. (2002) · Journal of Virology · doi:10.1128/jvi.76.22.11729-11737.2002 · Cited by 103
Dimer Initiation Signal of Human Immunodeficiency Virus Type 1: Its Role in Partner Selection during RNA Copackaging and Its Effects on Recombination
Moore, M. D., Fu, W., Nikolaitchik, O. A., Chen, J., Ptak, R. G., & Hu, W.-S. (2007) · Journal of Virology · doi:10.1128/jvi.02589-06 · Cited by 101
HIV Protease: Historical Perspective and Current Research
Weber, I. T., Wang, Y., & Harrison, R. W. (2021) · Viruses · doi:10.3390/v13050839 · Cited by 101
Proline Residues in the HIV-1 NH2-Terminal Capsid Domain: Structure Determinants for Proper Core Assembly and Subsequent Steps of Early Replication
Fitzon, T., Leschonsky, B., Bieler, K., Paulus, C., Schröder, J., Wolf, H. J., & Wagner, R. (2000) · Virology · doi:10.1006/viro.1999.0178 · Cited by 100
HIV-1 Maturation: Lessons Learned from Inhibitors
Kleinpeter, A. B., & Freed, E. O. (2020) · Viruses · doi:10.3390/v12090940 · Cited by 106
Association of Human Immunodeficiency Virus Type 1 Gag with Membrane Does Not Require Highly Basic Sequences in the Nucleocapsid: Use of a Novel Gag Multimerization Assay
Ono, A., Waheed, A. A., Joshi, A., & Freed, E. O. (2005) · Journal of Virology · doi:10.1128/jvi.79.22.14131-14140.2005 · Cited by 91
Comparing the Accumulation of Active- and Nonactive-Site Mutations in the HIV-1 Protease
Clemente, J. C., Moose, R. E., Hemrajani, R., Whitford, L. R. S., Lakshmanan Govindasamy, A., Reutzel, R., McKENNA, R. V., Agbandje‐McKenna, M., Goodenow, M. M., & Dunn, B. M. (2004) · Biochemistry · doi:10.1021/bi049459m · Cited by 91
Strukturbasierte Entwicklung von Protein‐Protein‐Interaktionsinhibitoren: Stabilisierung und Nachahmung von Peptidliganden
Pelay‐Gimeno, M., Glas, A., Koch, O., & Grossmann, T. N. (2015) · Angewandte Chemie · doi:10.1002/ange.201412070 · Cited by 90
Ordered Processing of the Human Immunodeficiency Virus Type 1 GagPol Precursor Is Influenced by the Context of the Embedded Viral Protease
Pettit, S. C., Clemente, J. C., Jeung, J. A., Dunn, B. M., & Kaplan, A. H. (2005) · Journal of Virology · doi:10.1128/jvi.79.16.10601-10607.2005 · Cited by 87
Proteolytic Processing of the P2/Nucleocapsid Cleavage Site Is Critical for Human Immunodeficiency Virus Type 1 RNA Dimer Maturation
Shehu-Xhilaga, M., Kraeusslich, H.-G., Pettit, S. C., Swanstrom, R. I., Jy, L., Marshall, J. A., Crowe, S. M., & Mak, J. (2001) · Journal of Virology · doi:10.1128/jvi.75.19.9156-9164.2001 · Cited by 87
Inhibition of HIV-1 Maturation via Drug Association with the Viral Gag Protein in Immature HIV-1 Particles
Zhou, J., Huang, L., Hachey, D. L., Chen, C., & Aiken, C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508951200 · Cited by 88
Polymorphisms in Gag spacer peptide 1 confer varying levels of resistance to the HIV- 1maturation inhibitor bevirimat
Adamson, C. S., Sakalian, M., Salzwedel, K., & Freed, E. O. (2010) · Retrovirology · doi:10.1186/1742-4690-7-36 · Cited by 88
Timing of the Components of the HIV Life Cycle in Productively Infected CD4 + T Cells in a Population of HIV-Infected Individuals
Murray, J. M., Kelleher, A. D., & Cooper, D. A. (2011) · Journal of Virology · doi:10.1128/jvi.05095-11 · Cited by 88
Helical structure determined by NMR of the HIV‐1 (345–392)Gag sequence, surrounding p2: Implications for particle assembly and RNA packaging
Morellet, N., Druillennec, S., Lenoir, C., Bouaziz, S., & Roques, B. P. (2005) · Protein Science · doi:10.1110/ps.041087605 · Cited by 86
Disrupting HIV‐1 capsid formation causes cGAS sensing of viral DNA
Sumner, R. P., Harrison, L., Touizer, E., Peacock, T. P., Spencer, M. K., Zuliani‐Alvarez, L., & Towers, G. J. (2020) · The EMBO Journal · doi:10.15252/embj.2019103958 · Cited by 86
MicroED structures of HIV-1 Gag CTD-SP1 reveal binding interactions with the maturation inhibitor bevirimat
Purdy, M. D., Shi, D., Chrustowicz, J., Hattne, J., Gonen, T., & Yeager, M. J. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1806806115 · Cited by 89
A Strongly Transdominant Mutation in the Human Immunodeficiency Virus Type 1 gag Gene Defines an Achilles Heel in the Virus Life Cycle
Lee, S.-K., Harris, J., & Swanstrom, R. (2009) · Journal of Virology · doi:10.1128/jvi.00317-09 · Cited by 83
HIV Type 1 Gag as a Target for Antiviral Therapy
Waheed, A. A., & Freed, E. O. (2011) · AIDS Research and Human Retroviruses · doi:10.1089/aid.2011.0230 · Cited by 84
Tumultuous Relationship between the Human Immunodeficiency Virus Type 1 Viral Infectivity Factor (Vif) and the Human APOBEC-3G and APOBEC-3F Restriction Factors
Henriet, S., Mercenne, G., Bernacchi, S., Paillart, J., & Marquet, R. (2009) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00040-08 · Cited by 81
Structural Requirements for Recognition of the Human Immunodeficiency Virus Type 1 Core during Host Restriction in Owl Monkey Cells
Forshey, B. M., Shi, J., & Aiken, C. (2004) · Journal of Virology · doi:10.1128/jvi.79.2.869-875.2005 · Cited by 80
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
Role of Vif in Stability of the Human Immunodeficiency Virus Type 1 Core
Öhagen, Å., & Gabuzda, D. H. (2000) · Journal of Virology · doi:10.1128/jvi.74.23.11055-11066.2000 · Cited by 79
Residues in the HIV-1 capsid assembly inhibitor binding site are essential for maintaining the assembly-competent quaternary structure of the capsid protein
Bartonova, V., Igonet, S., Sticht, J., Glass, B., Habermann, A., Vaney, M.-C., Sehr, P., Lewis, J., Rey, F. A., & Kraüsslich, H.-G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804230200 · Cited by 76
Saturation of TRIM5α-mediated restriction of HIV-1 infection depends on the stability of the incoming viral capsid
Shi, J., & Aiken, C. (2006) · Virology · doi:10.1016/j.virol.2006.03.013 · Cited by 76
Maturation-Dependent Human Immunodeficiency Virus Type 1 Particle Fusion Requires a Carboxyl-Terminal Region of the gp41 Cytoplasmic Tail
Jiang, J., & Aiken, C. (2007) · Journal of Virology · doi:10.1128/jvi.00592-07 · Cited by 74
The Dimer Interfaces of Protease and Extra-Protease Domains Influence the Activation of Protease and the Specificity of GagPol Cleavage
Pettit, S. C., Gulnik, S., Everitt, L., & Kaplan, A. H. (2002) · Journal of Virology · doi:10.1128/jvi.77.1.366-374.2003 · Cited by 72
Vif is a RNA chaperone that could temporally regulate RNA dimerization and the early steps of HIV-1 reverse transcription
Henriet, S., Sinck, L., Bec, G., Gorelick, R. J., Marquet, R., & Paillart, J. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm542 · Cited by 73
High-resolution structures of HIV-1 Gag cleavage mutants determine structural switch for virus maturation
Mattei, S., Tan, A. W. K., Glass, B., Müller, B., Kräusslich, H., & Briggs, J. A. G. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1811237115 · Cited by 73
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
The sequence of the CA-SP1 junction accounts for the differential sensitivity of HIV-1 and SIV to the small molecule maturation inhibitor 3-O-{3',3'-dimethylsuccinyl}-betulinic acid
Zhou, J., Chen, C., & Aiken, C. (2004) · Retrovirology · doi:10.1186/1742-4690-1-15 · Cited by 73
Retrovirus maturation-an extraordinary structural transformation
Mattei, S., Schur, F. K., & Briggs, J. A. (2016) · Current Opinion in Virology · doi:10.1016/j.coviro.2016.02.008 · Cited by 72
“Cleavage upstream of CA and downstream of SP1 leads to disruption of the immature lattice, while cleavage between CA and SP1 is additionally required to assemble the mature lattice [64,66].”
Background
Virus maturation as a new HIV-1 therapeutic target
Adamson, C. S., Salzwedel, K., & Freed, E. O. (2009) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728220903039714 · Cited by 74
Use of Aptamers as Diagnostics Tools and Antiviral Agents for Human Viruses
González, V. M., Martín, M. E., Fernández, G., & García-Sacristán, A. (2016) · Pharmaceuticals · doi:10.3390/ph9040078 · Cited by 71
A Structurally Disordered Region at the C Terminus of Capsid Plays Essential Roles in Multimerization and Membrane Binding of the Gag Protein of Human Immunodeficiency Virus Type 1
Liang, C., Hu, J., Whitney, J. B., Kleiman, L., & Wainberg, M. A. (2003) · Journal of Virology · doi:10.1128/jvi.77.3.1772-1783.2003 · Cited by 72
Flexibility in the P2 domain of the HIV‐1 Gag polyprotein
Newman, J. L., Butcher, E. W., Patel, D. T., Mikhaylenko, Y., & Summers, M. F. (2004) · Protein Science · doi:10.1110/ps.04614804 · Cited by 71
The molecular basis of HIV capsid assembly—five years of progress
Adamson, C. S., & Jones, I. M. (2004) · Reviews in Medical Virology · doi:10.1002/rmv.418 · Cited by 69
High Level Expression of Human Immunodeficiency Virus Type-1 Vif Inhibits Viral Infectivity by Modulating Proteolytic Processing of the Gag Precursor at the p2/Nucleocapsid Processing Site
Akari, H., Fujita, M., Kao, S., Khan, M. A., Shehu-Xhilaga, M., Adachi, A., & Strebel, K. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312426200 · Cited by 68
Determinants of activity of the HIV-1 maturation inhibitor PA-457.
Li, F., Zoumplis, D., Matallana, C., Kilgore, N., Reddick, M., Yunus, A., Adamson, C. S., Salzwedel, K., Martin, D. E., Allaway, G., et al. (2006) · Virology · doi:10.1016/j.virol.2006.07.023 · Cited by 70
Mutational Analysis of the C-Terminal Gag Cleavage Sites in Human Immunodeficiency Virus Type 1
Coren, L. V., Thomas, J. A., Chertova, E. N., Sowder, R. C., Gagliardi, T. D., Gorelick, R. J., & Ott, D. E. (2007) · Journal of Virology · doi:10.1128/jvi.02496-06 · Cited by 67
Secondary Mutations M36I and A71V in the Human Immunodeficiency Virus Type 1 Protease Can Provide an Advantage for the Emergence of the Primary Mutation D30N
Clemente, J. C., Hemrajani, R., Blum, L. E., Goodenow, M. M., & Dunn, B. M. (2003) · Biochemistry · doi:10.1021/bi035701y · Cited by 68
A Two-Pronged Structural Analysis of Retroviral Maturation Indicates that Core Formation Proceeds by a Disassembly-Reassembly Pathway Rather than a Displacive Transition
Keller, P. W., Huang, R. K., England, M. R., Waki, K., Cheng, N., Heymann, J. B., Craven, R. C., Freed, E. O., & Steven, A. C. (2013) · Journal of Virology · doi:10.1128/jvi.01408-13 · Cited by 69
Electron Cryotomography Studies of Maturing HIV-1 Particles Reveal the Assembly Pathway of the Viral Core
Woodward, C. L., Cheng, S. N., & Jensen, G. J. (2014) · Journal of Virology · doi:10.1128/jvi.02997-14 · Cited by 70
Molecular Architecture of the Retroviral Capsid
Perilla, J. R., & Gronenborn, A. M. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2016.02.009 · Cited by 68
The capsid-spacer peptide 1 Gag processing intermediate is a dominant-negative inhibitor of HIV-1 maturation
Checkley, M. A., Luttge, B. G., Soheilian, F., Nagashima, K., & Freed, E. O. (2010) · Virology · doi:10.1016/j.virol.2010.01.028 · Cited by 65
The Conserved Carboxy Terminus of the Capsid Domain of Human Immunodeficiency Virus Type 1 Gag Protein Is Important for Virion Assembly and Release
Melamed, D., Mark‐Danieli, M., Kenan-Eichler, M., Kraus, O., Castiel, A., Laham-Karam, N., Pupko, T., Glaser, F., Ben‐Tal, N., & Bacharach, E. (2004) · Journal of Virology · doi:10.1128/jvi.78.18.9675-9688.2004 · Cited by 63
An Update in the Development of HIV Entry Inhibitors
Rusconi, S., Scozzafava, A., Mastrolorenzo, A., & Supuran, C. T. (2007) · Current Topics in Medicinal Chemistry · doi:10.2174/156802607781212239 · Cited by 64
A Mutation in the Human Immunodeficiency Virus Type 1 Gag Protein Destabilizes the Interaction of the Envelope Protein Subunits gp120 and gp41
Davis, M., Jiang, J., Zhou, J.-J., Freed, E., & Aiken, C. (2006) · Journal of Virology · doi:10.1128/jvi.80.5.2405-2417.2006 · Cited by 71
Mutations That Abrogate Human Immunodeficiency Virus Type 1 Reverse Transcriptase Dimerization Affect Maturation of the Reverse Transcriptase Heterodimer
Wapling, J., Moore, K. L., Sonza, S., Mak, J., & Tachedjian, G. (2005) · Journal of Virology · doi:10.1128/jvi.79.16.10247-10257.2005 · Cited by 60
Quenching protein dynamics interferes with HIV capsid maturation
Wang, M., Quinn, C. M., Perilla, J. R., Zhang, H., Schirra, R. T., Hou, G., Byeon, I. L., Suiter, C. L., Ablan, S. D., Urano, E., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-01856-y · Cited by 61
Gag-Pol Processing during HIV-1 Virion Maturation: A Systems Biology Approach
Könnyű, B., Sadiq, S. K., Turányi, T., Hírmondó, R., Müller, B., Kräusslich, H., Coveney, P. V., & Müller, V. (2013) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1003103 · Cited by 68

Authors: Wiegers, K., Rutter, G., Kottler, H., Tessmer, U., Hohenberg, H., & Kräusslich, H.-G.
Affiliations: Leibniz Institute of Virology (LIV) (DE)
Heinrich-Pette-Institut, D-20251 Hamburg,1 and
German Cancer Research Center (DE)
Venue: Journal of Virology
Publisher: American Society for Microbiology
Published: 1998-04
Volume: 72
Issue: 4
Pages: 2846-2854
ISSN: 0022-538X (ISSN-L)
1098-5514
DOI: 10.1128/jvi.72.4.2846-2854.1998
PMC: PMC109729
OpenAlex: W2169408873
Cited by: 336
References: 65
Citations by year: 2026: 5 · 2025: 3 · 2024: 4 · 2023: 3 · 2022: 15 · 2021: 12 · 2020: 12 · 2019: 9 · 2018: 7 · 2017: 11 · 2016: 12 · 2015: 21 · 2014: 11 · 2013: 15 · 2012: 10
FWCI: 3.29
Type: journal article
Language: en
Open access: green
europepmc.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)
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, virus maturation, Gag protein, proteolytic cleavage sites, capsid protein, nucleocapsid protein, capsid stability, point mutations, matrix protein
MeSH terms: Amino Acid Sequence, Animals, Binding Sites, Capsid, Cell Line, Cell Line, Transformed, Cloning, Molecular, Detergents, Humans, Molecular Sequence Data, Protein Processing, Post-Translational, Proteins, Virion, HIV-1, Gene Products, gag, HIV Protease, Point Mutation, Octoxynol, Virus Assembly, COS Cells

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Sequential Steps in Human Immunodeficiency Virus Particle Maturation Revealed by Alterations of Individual Gag Polyprotein Cleavage Sites

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks