MersV1, Main, Exploration, bibRecord, 003F47

Mapping protein-protein contact sites using cellulose-bound peptide scans

Identifieur interne : 003F47 ( Main/Exploration ); précédent : 003F46; suivant : 003F48

Mapping protein-protein contact sites using cellulose-bound peptide scans

Auteurs : Ulrich Reineke [Allemagne] ; Robert Sabat [Allemagne] ; Achim Kramer [Allemagne] ; Rolf D. Stigler [Allemagne] ; Martina Seifert [Allemagne] ; Thomas Michel [Allemagne] ; Hans D. Volk [Allemagne] ; Jens Schneider-Mergener [Allemagne]

Source :

Molecular Diversity [ 1381-1991 ] ; 1996-05-01.

RBID : ISTEX:A72795DC9A4833C604C5BFF9AACE77B5311BAF5D

English descriptors

Abstract

Summary: We have characterized the interaction of two monoclonal antibodies with their respective antigens using cellulose-bound sets of overlapping peptides (peptide scans). Both antibodies CB/RS/5 and CB/MT/1 recognize discontinuous epitopes present in human interleukin-10 (IL-10) and tumor necrosis factor alpha (TNF-α). In addition, the interaction between TNF-a and its 55-kDa receptor (TNF-R) was investigated by the same approach. Both antibodies, as well as TNF-α, interacted with two or more regions of the peptide scans. Antibody-binding competition studies between the native antigens and peptides, covering single parts of the binding regions, enabled us to distinguish between binding to the paratope or other regions of the antibody. The combination of these experimental approaches allowed the identification of short antigen-derived sequences that are separated on the primary sequence but close in space on the surface of IL-10 and TNF-α, thus representing putative discontinuous epitopes. In the case of the TNF-R-derived peptide scans, two of the identified regions interact with the structurally similar TNF-β in the TNF-β-TNF-R complex. These data indicate that this approach should be generally applicable for mapping nonlinear protein-protein contact sites.

Url:

https://api.istex.fr/ark:/67375/1BB-2RCVJP1Z-B/fulltext.pdf

DOI: 10.1007/BF01544952

Affiliations:

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Le document en format XML

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<author><name sortKey="Kramer, Achim" sort="Kramer, Achim" uniqKey="Kramer A" first="Achim" last="Kramer">Achim Kramer</name>
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<author><name sortKey="Stigler, Rolf D" sort="Stigler, Rolf D" uniqKey="Stigler R" first="Rolf D." last="Stigler">Rolf D. Stigler</name>
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<author><name sortKey="Michel, Thomas" sort="Michel, Thomas" uniqKey="Michel T" first="Thomas" last="Michel">Thomas Michel</name>
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<front><div type="abstract" xml:lang="en">Summary: We have characterized the interaction of two monoclonal antibodies with their respective antigens using cellulose-bound sets of overlapping peptides (peptide scans). Both antibodies CB/RS/5 and CB/MT/1 recognize discontinuous epitopes present in human interleukin-10 (IL-10) and tumor necrosis factor alpha (TNF-α). In addition, the interaction between TNF-a and its 55-kDa receptor (TNF-R) was investigated by the same approach. Both antibodies, as well as TNF-α, interacted with two or more regions of the peptide scans. Antibody-binding competition studies between the native antigens and peptides, covering single parts of the binding regions, enabled us to distinguish between binding to the paratope or other regions of the antibody. The combination of these experimental approaches allowed the identification of short antigen-derived sequences that are separated on the primary sequence but close in space on the surface of IL-10 and TNF-α, thus representing putative discontinuous epitopes. In the case of the TNF-R-derived peptide scans, two of the identified regions interact with the structurally similar TNF-β in the TNF-β-TNF-R complex. These data indicate that this approach should be generally applicable for mapping nonlinear protein-protein contact sites.</div>
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Mapping protein-protein contact sites using cellulose-bound peptide scans

Mapping protein-protein contact sites using cellulose-bound peptide scans

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English descriptors

Abstract

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