Peptide mimotopes selected with HIV-1-blocking monoclonal antibodies against CCR5 represent motifs specific for HIV-1 entry.

Peptide mimotopes selected with HIV-1-blocking monoclonal antibodies against CCR5 represent motifs specific for HIV-1 entry. Research Abstract Details 

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Peptide mimotopes selected with HIV-1-blocking monoclonal antibodies against CCR5 represent motifs specific for HIV-1 entry. Abstract Text:

Christoph ,Anette Pustowka,James Irving,Christoph Kessel,Katharina Klich, Wegner,Merrill J Rowley,Ian R Mackay,Wolfhart Kreuz,Christian Griesinger,Ursula Dietrich,Christoph ,Anette Pustowka,James Irving,Christoph Kessel,Katharina Klich, Wegner,Merrill J Rowley,Ian R Mackay,Wolfhart Kreuz,Christian Griesinger,Ursula Dietrich,

CCR5 is a chemokine receptor that mediates entry of human immunodeficiency virus-1 (HIV-1). Two monoclonal antibodies (mAbs) that block HIV-1 entry, 3A9 and 5C7, were used to select peptide mimotopes of sequences on CCR5 from phage displayed peptide libraries. The selected mimotofpes comprised motifs at the N-terminus and on the first and third extracellular loops (ECL1 and ECL3) of CCR5. Amino acids in these motifs were exchanged for alanines by site-directed mutagenesis (sdm) in the cDNA for human CCR5. Ensuing effects on antibody binding to CCR5, cellular entry of HIV-1 and chemokine-induced signalling were analysed by transfection of mutant cDNAs into HEK293.CD4 cells. For both mAbs, fluorescence-activated cell sorting analysis was used to define overlapping conformational epitopes on CCR5 at the N-terminus, on ECL1 and ECL3. Mutation of the N-terminal motif 10YD11 prevented HIV-1 entry into transfected cells as judged by single round infection assays with R5 and R5X4 HIV-1 isolates, as did mutation of the motif 96FG97 in ECL1, whereas mutation of the motif 274RLD276 in ECL3 had only a minor effect. None of the motifs in CCR5 relevant to HIV-1 entry disrupted chemokine-induced signalling. Thus, peptide mimotopes of conformational contact sites of CCR5 with the paratope of mAbs 3A9 and 5C7 represent sites on CCR5 that are essential for HIV-1 entry. Structural knowledge of these mimotopes could help elucidate the nature of the interaction between CCR5 and HIV-1, and thus the derivation of specific inhibitors of entry of HIV-1 into susceptible cells without interference with chemokine signalling.

Peptide mimotopes selected with HIV-1-blocking monoclonal antibodies against CCR5 represent motifs specific for HIV-1 entry. Publishing Authors By Initials

C ,A Pustowka,J Irving,C Kessel,K Klich,V Wegner,MJ Rowley,IR Mackay,W Kreuz,C Griesinger,U Dietrich,C ,A Pustowka,J Irving,C Kessel,K Klich,V Wegner,MJ Rowley,IR Mackay,W Kreuz,C Griesinger,U Dietrich,

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Peptide mimotopes selected with HIV-1-blocking monoclonal antibodies against CCR5 represent motifs specific for HIV-1 entry. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Immunology and cell biology

VOLUME: 85

Page Numbers: 511-7

Journal Abbreviation: Immunol. Cell Biol.

ISSN: 0818-9641

DAY: 3

MONTH: 07

YEAR: 2007

Peptide mimotopes selected with HIV-1-blocking monoclonal antibodies against CCR5 represent motifs specific for HIV-1 entry. Information

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LANGUAGE: eng

NlmUniqueID: 8706300

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Grant and Affiliation Information for Peptide mimotopes selected with HIV-1-blocking monoclonal antibodies against CCR5 represent motifs specific for HIV-1 entry.

AFFILIATION: Georg-Speyer-Haus, Institute for Biomedical Research, Frankfurt am Main, Germany.

Country: Australia

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MEDLINETA: Immunol Cell Biol

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