English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Antigenic and structural variation in the major nucleocapsid protein, VPN41, from different strains of respiratory syncytial (RS) virus was observed using a combination of monoclonal antibodies and two-dimensional peptide mapping. Limited trypsin treatment of intact nucleocapsids produced two peptide fragments Mr 27K and Mr 14K. Two monoclonal antibodies, N1 and N2, reactive with primary sequence epitopes located on intact nucleocapsids also reacted with either the 27K fragment (N2) or the 14K fragment (N1). Competitive radioimmunoassay studies using N1 and N2 antibodies revealed two discrete antigenic groups among the seven human strains of RS virus examined. A bovine strain of RS virus, although antigenically similar to the human strain of RS virus, was placed in a separate group. Two-dimensional peptide mapping of 125I-labelled VPN41 purified by SDS-PAGE revealed extensive structural homology between all strains. However, several unique tryptic/chymotryptic peptides supported the grouping obtained with the monoclonal antibodies.

Antigenic and Structural Variation in the Major Nucleocapsid Protein of Respiratory Syncytial Virus