The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Binding of Human Immunodeficiency Virus Type 1 Gag to Membrane: Role of the Matrix Amino Terminus
Open accessAbstract
Binding of the human immunodeficiency virus type 1 (HIV-1) Gag protein precursor, Pr55 Gag , to membrane is an indispensable step in virus assembly. Previously, we reported that a matrix (MA) residue 6 substitution (6VR) imposed a virus assembly defect similar to that observed with myristylation-defective mutants, suggesting that the 6VR change impaired membrane binding. Intriguingly, the 6VR mutation had no effect on Gag myristylation. The defective phenotype imposed by 6VR was reversed by changes at other positions in MA, including residue 97. In this study, we use several biochemical methods to demonstrate that the residue 6 mutation, as well as additional substitutions in MA amino acids 7 and 8, reduce membrane binding without affecting N-terminal myristylation. This effect is observed in the context of Pr55 Gag , a truncated Gag containing only MA and CA, and in MA itself. The membrane binding defect imposed by the 6VR mutation is reversed by second-site changes in MA residues 20 and 97, both of which, when present alone, increase membrane binding to levels greater than those for the wild type. Both reduced and enhanced membrane binding imposed by the MA substitutions depend upon the presence of the N-terminal myristate. The results support the myristyl switch model recently proposed for the regulation of Gag membrane binding, according to which membrane binding is determined by the degree of exposure or sequestration of the N-terminal myristate moiety. Alternatively, insertion of the myristate into the lipid bilayer might be a prerequisite event for the function of other distinct MA-encoded membrane binding domains.
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Cites
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
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
Self-citationHill, C. P., Worthylake, D., Bancroft, D. P., Christensen, A. M., & Sundquist, W. I. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.7.3099 · Cited by 473
Willey, R. L., Bonifacino, J. S., Potts, B. J., Martin, M. A., & Klausner, R. D. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.24.9580 · Cited by 428
Dorfman, T., Mammano, F., Haseltine, W. A., & Göttlinger, H. G. (1994) · Journal of Virology · doi:10.1128/jvi.68.3.1689-1696.1994 · Cited by 288 · cited 1×
“Deletions (9, 48, 52) and single amino acid substitutions (13, 15, 33) in MA can block HIV-1 envelope glycoprotein incorporation into virus particles, and HIV-1 MA has been implicated in early events postinfection (for a review, see reference 11).”
BackgroundThree-dimensional structure of the human immunodeficiency virus type 1 matrix protein
Massiah, M. A., Starich, M. R., Paschall, C., Summers, M. F., Christensen, A. M., & Sundquist, W. I. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1719 · Cited by 271 · cited 2×
“It has been proposed that basic residues within this domain and elsewhere in MA form a positively charged surface which interacts with negatively charged phospholipids on the inner face of the lipid bilayer (21, 29, 54, 55).”
BackgroundParent, L. J., Bennett, R. P., Craven, R. C., Nelle, T. D., Krishna, N. K., Bowzard, J. B., Wilson, C. B., Puffer, B. A., Montelaro, R. C., & Wills, J. W. (1995) · Journal of Virology · doi:10.1128/jvi.69.9.5455-5460.1995 · Cited by 258 · cited 2×
“These domains, which drive Gag membrane binding, Gag-Gag interactions, and late budding functions, have been referred to as M, I, and L, respectively (35).”
BackgroundDifferential membrane binding of the human immunodeficiency virus type 1 matrix protein
Zhou, W., & Resh, M. D. (1996) · Journal of Virology · doi:10.1128/jvi.70.12.8540-8548.1996 · Cited by 226 · cited 5×
“p17 (MA) thus displays a significantly reduced affinity for membrane compared with Pr55 (42, 55).”
BackgroundInfluentialFäcke, 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 1×
“The observation that large deletions (10, 17) and single amino acid changes (16) in MA cause a redirection of assembly to cytoplasmic compartments indicates that MA plays a role not only in promoting membrane binding in general but also in the targeting of Gag to the plasma membrane in particular.”
Background
Cited by
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
Plasma Membrane Is the Site of Productive HIV-1 Particle Assembly
Jouvenet, N., Neil, S. J. D., Bess, C., Johnson, M. C., Virgen, C. A., Simon, S. M., & Bieniasz, P. D. (2006) · PLoS Biology · doi:10.1371/journal.pbio.0040435 · Cited by 357
Chukkapalli, V., Hogue, I. B., Boyko, V., Hu, W.-S., & Ono, A. (2008) · Journal of Virology · doi:10.1128/jvi.01614-07 · Cited by 268
Self-citationAnalysis of human immunodeficiency virus type 1 matrix binding to membranes and nucleic acids
Alfadhli, A., Still, A., & Barklis, E. (2009) · Journal of Virology · doi:10.1128/jvi.01197-09 · Cited by 145
Molecular determinants that regulate plasma membrane association of HIV-1 Gag
Chukkapalli, V., & Ono, A. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.04.015 · Cited by 129
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Metadata
- Authors
- Ono, A., & Freed, E. O.
- Venue
- Journal of Virology
- Publisher
- American Society for Microbiology
- Published
- 1999-05
- Volume
- 73
- Issue
- 5
- Pages
- 4136-4144
- ISSN
- 0022-538X (ISSN-L)
- 1098-5514
- OpenAlex
- W2115644744
- Cited by
- 241
- References
- 9
- FWCI
- 2.57
- Type
- journal article
- Language
- en
- Open access
- green
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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