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 Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

Monoclonal antibodies (MAbs) to the haemagglutinin-neuraminidase (HN), fusion (F) and matrix (M) proteins of Newcastle disease virus were prepared and characterized. At least three non-overlapping or partially overlapping antigenic sites were delineated on the HN, three on the F and three on the M proteins by competitive binding assays. Antigenic sites on the HN and F proteins roughly represented functional domains defined by serological tests. Two antigenic sites on the F protein were involved in virus neutralizing and haemolysis-inhibiting activity. These antigenic determinants were readily affected by treatment with certain surfactants and acetone. Proteolytic cleavage of the HN and F proteins was associated with conformational change, revealed by altered reactivity with MAbs and by altered topological arrangements of some epitopes. None of the anti-M MAbs inhibited any biological activities of the virus.

journal of general virology

Monoclonal Antibodies to Three Structural Proteins of Newcastle Disease Virus: Biological Characterization with Particular Reference to the Conformational Change of Envelope Glycoproteins Associated with Proteolytic Cleavage