The DOI matches its Crossref record; 47 of the 47 references it cites were found in a registry or an index.
Differential membrane binding of the human immunodeficiency virus type 1 matrix protein
Open accessAbstract
The human immunodeficiency virus type 1 matrix protein (p17MA) plays a central role at both the early and late stages of the virus life cycle. During viral assembly, the p17MA domain of Pr55gag promotes membrane association, which is essential for the formation of viral particles. When viral infection occurs, the mature p17MA dissociates from the plasma membrane and participates in the nuclear targeting process. Thus, p17MA contains a reversible membrane binding signal to govern its differential subcellular localization and biological functions. We previously identified a membrane binding signal within the amino-terminal 31 amino acids of the matrix domain of human immunodeficiency virus type 1 Gag, consisting of myristate and a highly basic region (W. Zhou, L. J. Parent, J. W. Wills, and M. D. Resh, J. Virol. 68:2556-2569, 1994). Here we show that exposure of this membrane binding signal is regulated in different Gag protein contexts. Within full-length Pr55gag, the membrane targeting signal is exposed and can direct Pr55gag as well as heterologous proteins to the plasma membrane. However, in the context of p17MA alone, this signal is hidden and unable to confer plasma membrane binding. To investigate the molecular mechanism for regulation of membrane binding, a series of deletions within p17MA was generated by sequentially removing alpha-helical regions defined by the nuclear magnetic resonance structure. Removal of the last alpha helix (amino acids 97 to 109) of p17MA was associated with enhancement of binding to biological membranes in vitro and in vivo. Liposome binding experiments indicated that the C-terminal region of p17MA exerts a negative effect on the N-terminal MA membrane targeting domain by sequestering the myristate signal. We propose that mature p17MA adopts a conformation different from that of the p17MA domain within Pr55gag and present evidence to support this hypothesis. It is likely that such a conformational change results in an N-terminal myristyl switch which governs differential membrane binding.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
A short amino acid sequence able to specify nuclear location
Kalderon, D., Roberts, B., Richardson, W. D., & Smith, A. E. (1984) · Cell · doi:10.1016/0092-8674(84)90457-4 · Cited by 2,511
Heim, R., Cubitt, A. B., & Tsien, R. Y. (1995) · Nature · doi:10.1038/373663b0 · Cited by 1,821
A simple method for the preparation of homogeneous phospholipid vesicles
Barenholz, Y., Gibbes, D. C., Litman, B. J., Goll, J., Thompson, T. E., & Carlson, F. D. (1977) · Biochemistry · doi:10.1021/bi00631a035 · Cited by 864
Heinzinger, N. K., Bukinsky, M. I., Haggerty, S. A., Ragland, A. M., Kewalramani, V, Lee, M. A., Gendelman, H. E., Ratner, L., Stevenson, M., & Emerman, M. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.15.7311 · Cited by 854
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
Bukrinsky, M., Haggerty, S., Dempsey, M. P., Sharova, N., Adzhubei, A. A., Spitz, L., Lewis, P. F., Goldfarb, D. S., Emerman, M., & Stevenson, M. (1993) · Nature · doi:10.1038/365666a0 · Cited by 801
Lewis, P. F., & Emerman, M. (1994) · Journal of Virology · doi:10.1128/jvi.68.1.510-516.1994 · Cited by 797
THE BIOLOGY AND ENZYMOLOGY OF EUKARYOTIC PROTEIN ACYLATION
Towler, D. A., Gordon, J. I., Adams, S. P., & Glaser, L. (1988) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.57.070188.000441 · Cited by 793
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
Effect of mutations affecting the p6 gag protein on human immunodeficiency virus particle release
Göttlinger, H. G., Dorfman, T., Sodroski, J. G., & Haseltine, W. A. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.8.3195 · Cited by 647
Cited by
Sorted by citations
Items 201–227 of 227
Regulation of Gag trafficking during retrovirus assembly and budding
Jin, J. (2007) · D-Scholarship@Pitt (University of Pittsburgh)
Brandano, L. A. (2011) · The Journal of the American Medical Association (JAMA) Network (American Medical Association) · doi:10.13028/5zmj-9x81
Studies on HIV-1 core assembly
Abdurahman, S. (2007) · Figshare
Characterisation of llama antibody fragments able to act as HIV-1 entry inhibitors
Quigley, A. F. (2009) · OpenGrey (Institut de l'Information Scientifique et Technique)
Llewellyn, G. N. (2012) · Deep Blue (University of Michigan)
The effect of alpha-HGA on HIV-1 replication
Youssefi, M. (2009) · Figshare
Pépin, G. (2004) · Corpus Université Laval (Université Laval)
Morikawa, Y. (2008) · The Journal of AIDS Research · doi:10.11391/aidsr1999.10.33
The Roles of Lipid and RNA in Regulating Retroviral Gag Membrane Binding and Targeting.
Inlora, J. (2015) · Deep Blue (University of Michigan)
Biochemical and Genetic Investigation of Immature Murine Leukemia Virus Assembly
Tinaztepe, S. (2017) · doi:10.7916/d82v2tng
“conformational change that sequesters this fatty acid chain within MA, allowing MA to dissociate from the membrane to perform its functions during viral entry [103-105].”
BackgroundZhang, Z., Zhang, F., Bai, S., Qiao, J., Shen, H., Huang, F., Gao, S., Li, S., Gu, Y., & Xia, N. (2018) · Biotechnology and Applied Biochemistry · doi:10.1002/bab.1662
Martin, G. E. (2007) · Corpus Université Laval (Université Laval)
Heilmann, I. (2013) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.717988250.793472526
Socas, L. B. P., & Ambroggio, E. E. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.08.25.505363
Giroud, C. (2012) · theses.fr (ABES) · doi:10.70675/dcb13f1azfc90z47d6zb978z456e9b4d70d5
da Silva, E. S. (2013) · theses.fr (ABES) · doi:10.70675/571be44cz38c0z432fzb87az66fd4686a457
Mécanistique de l'incorporation de la protéine Tat du VIH-1 dans les particules virales
Schatz, M. (2018) · theses.fr (ABES) · doi:10.70675/2dd44b60z26baz42e9zb74azde8c15215c4a
Mechanisms of HIV-1 assembly, release and maturation
Kleinpeter, A. B., & Freed, E. O. (2026) · Nature Reviews Microbiology · doi:10.1038/s41579-026-01327-6 · Cited by 2
“…mechanism for Gag membrane binding is suggested by the finding that the myristate is sequestered in a hydrophobic groove in isolated MA, but is exposed in the context of full-length Gag, and deletions in MA can increase Gag membrane binding by reversing this myristate sequestration 28 .”
Biophysical Investigation into the Mechanisms Regulating HIV-1 Envelope Glycoprotein Incorporation
Clark, A. R. (2025) · Digital Commons - DU (University of Denver) · doi:10.56902/etdcrp.2025.179
BindingDB (2020) · UC San Diego · doi:10.7270/q25x2cv0
Kim, A. L. (2012) · eScholarship@UMassChan · doi:10.13028/8pg6-xe17
“Inhibition of MA-mediated membrane binding of Gag through disruption of the myristate modification and mutation of the HBR has been shown to also inhibit virus production (122, 182, 183).”
BackgroundChukkapalli, V. (2011) · Deep Blue (University of Michigan)
Metadata
- Authors
- Zhou, W., & Resh, M. D.
- Affiliations
- Memorial Sloan Kettering Cancer Center (US)
- ORCID
- Resh, M D
- Venue
- Journal of Virology
- Publisher
- American Society for Microbiology
- Published
- 1996-12
- Volume
- 70
- Issue
- 12
- Pages
- 8540-8548
- ISSN
- 0022-538X (ISSN-L)
- 1098-5514
- PMC
- PMC190946
- OpenAlex
- W2102965972
- Cited by
- 226
- References
- 47
- Citations by year
- 2026: 1 · 2025: 2 · 2023: 3 · 2022: 6 · 2021: 4 · 2020: 5 · 2019: 3 · 2018: 9 · 2017: 3 · 2016: 4 · 2015: 6 · 2014: 10 · 2013: 10 · 2012: 13
- FWCI
- 3.01
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Virology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Cancer Institute (CA 72309, R01CA072309)
- Topics
- Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Life Sciences › Immunology and Microbiology › Immunology › T-cell and Retrovirus Studies
- Keywords
- HIV-1, Pr55gag, membrane binding, myristate, myristoylation, plasma membrane targeting, viral assembly, nuclear targeting, protein conformational change, liposome binding, subcellular localization
- MeSH terms
- Animals, Epitopes, Cell Membrane, Humans, Myristic Acids, Protein Precursors, Viral Proteins, Signal Transduction, HIV Antigens, HIV-1, Gene Products, gag, Sequence Deletion, COS Cells, Myristic Acid, gag Gene Products, Human Immunodeficiency Virus
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