Critical amino acid changes in VP2 variable domain are associated with typical and atypical antigenicity in very virulent infectious bursal disease viruses.

Abstract:

:Classical serotype 1 infectious bursal disease viruses (IBDV), but not very virulent (vv) isolates, react with neutralizing monoclonal antibody (NMab) 3 in virus neutralization tests or antigen-capture ELISA. Two other NMabs, 6 and 8, bind to both classical and most vv strains, but not to the atypical 94,432 and 91,168 vv strains, respectively. The basis for such reactivities was investigated by sequencing the genome region encoding the VP2 major immunogenic domain. In classical, variant, vaccine or vv IBDV strains, negative reactions with NMab3 were associated with changes in the Proline-Glycine pair at amino-acid (aa) positions 222-223 (hydrophilic peak A), and negative reactions with NMabs 6 and 8 with aa changes from positions 318 to 324 (hydrophilic peak B). The 91,168 and 94,432 viruses are the first vvIBDVs to present aa changes in peak B.

journal_name

Arch Virol

journal_title

Archives of virology

authors

Eterradossi N,Arnauld C,Toquin D,Rivallan G

doi

10.1007/s007050050404

subject

Has Abstract

pub_date

1998-01-01 00:00:00

pages

1627-36

issue

8

eissn

0304-8608

issn

1432-8798

journal_volume

143

pub_type

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