Journal article
Novel peptides based on HIV-1 gp120 sequence with homology to chemokines inhibit HIV infection in cell culture
PloS one, v 6(1), pp e14474-e14474
11 Jan 2011
PMID: 21264298
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
The sequential interaction of the envelope glycoprotein of the human immunodeficiency virus type 1 (HIV-1) with CD4 and certain chemokine coreceptors initiates host cell entry of the virus. The appropriate chemokines have been shown to inhibit viral replication by blocking interaction of the gp120 envelope protein with the coreceptors. We considered the possibility that this interaction involves a motif of the gp120 that may be structurally homologous to the chemokines. In the amino acid sequences of most chemokines there is a Trp residue located at the beginning of the C-terminal α-helix, which is separated by six residues from the fourth Cys residue. The gp120 of all HIV-1 isolates have a similar motif, which includes the C-terminal part of a variable loop 3 (V3) and N-terminal part of a conserved region 3 (C3). Two synthetic peptides, derived from the relevant gp120 sequence inhibited HIV-1 replication in macrophages and T lymphocytes in sequence-dependent manner. The peptides also prevented binding of anti-CXCR4 antibodies to CXCR4, and inhibited the intracellular Ca(2+) influx in response to CXCL12/SDF-1α. Thus these peptides can be used to dissect gp120 interactions with chemokine receptors and could serve as leads for the design of new inhibitors of HIV-1.
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Details
- Title
- Novel peptides based on HIV-1 gp120 sequence with homology to chemokines inhibit HIV infection in cell culture
- Creators
- Oleg Chertov - Protein Chemistry Laboratory, Advanced Technology Program, SAIC-Frederick, Inc., National Cancer Institute at Frederick, Frederick, Maryland, United States of AmericaNing ZhangXin ChenJoost J OppenheimJacek LubkowskiConnor McGrathRaymond C Sowder, 2ndBruce J CriseAnatoli MalyguineMichele A KutzlerAmber D SteeleEarl E HendersonThomas J Rogers
- Publication Details
- PloS one, v 6(1), pp e14474-e14474
- Publisher
- Public LIbrary of Science (PLOS); United States
- Grant note
- DA-25532 / NIDA NIH HHS R01 DA006650 / NIDA NIH HHS F31 DA-05894 / NIDA NIH HHS P30 DA013429 / NIDA NIH HHS T32 DA007237 / NIDA NIH HHS P01DA-23860 / NIDA NIH HHS F31 DA005894 / NIDA NIH HHS N01-CO-12400 / NCI NIH HHS R01 DA025532 / NIDA NIH HHS P01 DA023860 / NIDA NIH HHS R01 DA014230 / NIDA NIH HHS S10 RR027910 / NCRR NIH HHS Intramural NIH HHS N01CO12400 / NCI NIH HHS DA-14230 / NIDA NIH HHS P30DA-13429 / NIDA NIH HHS DA-06650 / NIDA NIH HHS
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Infectious Diseases (and HIV Medicine)
- Web of Science ID
- WOS:000286514000001
- Scopus ID
- 2-s2.0-79251587133
- Other Identifier
- 991014877765504721
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- Collaboration types
- Industry collaboration
- Domestic collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology