Epitope Mapping of the Major Inner Capsid Protein of Group A Rotavirus Using Peptide Synthesis
Autor: | J.B. Bour, C. Bourgeois, Evelyne Kohli, L. Maurice, Pierre Pothier |
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Rok vydání: | 1993 |
Předmět: |
Rotavirus
Antigenicity medicine.drug_class Molecular Sequence Data Enzyme-Linked Immunosorbent Assay Peptide Biology Monoclonal antibody Epitope Epitopes chemistry.chemical_compound Capsid Virology medicine Peptide synthesis Amino Acid Sequence Antigens Viral chemistry.chemical_classification Sequence Homology Amino Acid Antibodies Monoclonal Molecular biology Peptide Fragments Epitope mapping chemistry Pepscan Capsid Proteins Oligopeptides |
Zdroj: | Virology. 194:110-116 |
ISSN: | 0042-6822 |
Popis: | Three hundred and ninety-one consecutive heptapeptides derived from the VP6 protein of bovine rotavirus (397 AA) were synthesized using the "pepscan" method and were assayed on the synthesis pins with monoclonal antibodies to VP6. Heptapeptides reactive with MAbs were located in four main regions: regions AA 32-64, AA 155-167, AA 208-274, and a fourth region at the C-terminal, from AA 380 to AA 397. Among these regions, two sequences were also reactive with the MAbs when longer peptides were assayed. The sequence located between AA 58 and AA 62 (NWNFD), recognized by MAbs RV-1026, RV-50, and RV-443, was previously reported. A new site was defined in the region essential for trimerization, between AA 159 and AA 165 (PYSASFT), which was recognized by MAbs RV-133 and RV-138. This mapping may be useful to locate functional domains on the VP6 protein. |
Databáze: | OpenAIRE |
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