HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Leonov, S. V. Articles by Norrby, E. Search for Related Content PubMed PubMed Citation Articles by Leonov, S. V. Articles by Norrby, E. Agricola Articles by Leonov, S. V. Articles by Norrby, E.

Linear antigenic and immunogenic regions of the respiratory syncytial virus P protein

¹ Microbiology and Tumorbiology Centre, Karolinska Institute, Doktorsringen 13-15, Solma, 17177 Stockholm, Sweden
and² Department of Virology, University of Turku, Kiinamyllynkatu 13, 20520 Turku, Finland

Three linear antigenic regions on the P protein from human respiratory syncytial virus (RSV) subgroup A (strain A2) were represented by peptides that reacted with monoclonal antibodies and with sera from humans with recent or previous RSV infection. The determinants were localized within three hydrophilic regions of the P protein: Pro₉₁ to Asp₁₁₀, Ser₁₆₁ to Lys₁₈₀ and Glu₂₂₁ to Phe₂₄₁. The role of individual amino acids in the epitopes defined by monoclonal antibodies was determined. Two monoclonal antibodies reacting with the same antigenic site were found to detect epitopes that had different amino acid dependencies. Rabbit hyperimmune sera raised against selected peptides specifically precipitated different forms of the P protein from RSV-infected ³⁵S-labelled cell extracts in a radioimmune precipitation assay. These findings have implications for forthcoming structural-functional studies of RSV capsid component interactions and also for serological diagnosis of RSV infection.

Received 7 October 1993; accepted 16 December 1993.