ArticleAntimicrobial agents and chemotherapy2003
Two mechanisms for human immunodeficiency virus type 1 inhibition by N-terminal modifications of RANTES.
Article in Antimicrobial agents and chemotherapy, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 75 citations in OpenAlex.
- The Effect of N-Terminal Cyclization on the Function of the HIV Entry Inhibitor 5P12-RANTES.International journal of molecular sciences · 2017Article
- CCR5 susceptibility to ligand-mediated down-modulation differs between human T lymphocytes and myeloid cells.Journal of leukocyte biology · 2015Article
- Chemokine and chemokine receptor structure and interactions: implications for therapeutic strategies.Immunology and cell biology · 2015Review
- Combination of the CCL5-derived peptide R4.0 with different HIV-1 blockers reveals wide target compatibility and synergic cobinding to CCR5.Antimicrobial agents and chemotherapy · 2014Article
- Targeting spare CC chemokine receptor 5 (CCR5) as a principle to inhibit HIV-1 entry.The Journal of biological chemistry · 2014Article
- Multifaceted mechanisms of HIV inhibition and resistance to CCR5 inhibitors PSC-RANTES and Maraviroc.Antimicrobial agents and chemotherapy · 2013Article
- Closing the door to human immunodeficiency virus.Protein & cell · 2013Review
- HIV-1 resistance to maraviroc conferred by a CD4 binding site mutation in the envelope glycoprotein gp120.Journal of virology · 2013Article
- Sensitivity changes over the course of infection increases the likelihood of resistance against fusion but not CCR5 receptor blockers.AIDS research and human retroviruses · 2012Article
- Review
- Highly potent chimeric inhibitors targeting two steps of HIV cell entry.The Journal of biological chemistry · 2011Article
- Article
- Chemokine oligomerization and interactions with receptors and glycosaminoglycans: the role of structural dynamics in function.Experimental cell research · 2011Review
- New insights into the mechanisms whereby low molecular weight CCR5 ligands inhibit HIV-1 infection.The Journal of biological chemistry · 2011Article
- Functional stability of unliganded envelope glycoprotein spikes among isolates of human immunodeficiency virus type 1 (HIV-1).PloS one · 2011Article
- Resistance to the CCR5 inhibitor 5P12-RANTES requires a difficult evolution from CCR5 to CXCR4 coreceptor use.PloS one · 2011Article
- CC chemokine receptor 5 (CCR5) desensitization: cycling receptors accumulate in the trans-Golgi network.The Journal of biological chemistry · 2010Article
- Article
- Engineering of Lactobacillus jensenii to secrete RANTES and a CCR5 antagonist analogue as live HIV-1 blockers.Antimicrobial agents and chemotherapy · 2010Article
- "Resistance" to PSC-RANTES revisited: two mutations in human immunodeficiency virus type 1 HIV-1 SF162 or simian-human immunodeficiency virus SHIV SF162-p3 do not confer resistance.Journal of virology · 2010Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
C-C chemokine receptor 5 (CCR5) is the primary coreceptor for human immunodeficiency virus type 1 (HIV-1) infection. Native chemokines that bind to CCR5 inhibit HIV-1 infection, albeit weakly, but chemically modified chemokines inhibit infection more efficiently. We have investigated the inhibitory mechanism of three N-terminally modified RANTES variants (AOP-, NNY-, and PSC-RANTES) with the MT-2 human T-cell line stably expressing either native or mutated CCR5. The RANTES analogues showed the same rank order (PSC > NNY > AOP) in their capacity to induce prolonged CCR5 internalization, inhibit surface reexpression, and prevent HIV-1 infection on MT-2 cells expressing wild-type CCR5 or CCR5 with four C-terminal serine phosphorylation sites mutated to alanine. None of the RANTES analogues caused internalization of a C-terminal cytoplasmic domain deletion mutant of CCR5, and each derivative had equal potency in inhibiting HIV-1 infection of MT-2 cells expressing this mutant. We conclude that the C-terminal cytoplasmic residues of CCR5 are necessary for receptor sequestration by RANTES analogues but that the process and the relative activity of each derivative are not dependent upon phosphorylation of the C-terminal serine residues. Two mechanisms of antiviral activity are demonstrated: receptor blockade and receptor sequestration. Potency correlates with the ability to induce CCR5 sequestration but not with receptor binding, suggesting that sequestration may make the greater contribution to antiviral activity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.