当前位置： SCI文献检索 > EPIDEMIOLOGY AND INFECTION期刊下所有文献 > Characterization of monoclonal antibodies against a type SAT 2 foot-and-mouth disease virus.

Characterization of monoclonal antibodies against a type SAT 2 foot-and-mouth disease virus.

Abstract：

:This paper is the first to describe characterization of monoclonal antibodies (MAbs) against a South African Territories 2 (SAT 2) foot-and-mouth disease virus (isolate Rho 1/48). Twelve MAbs which neutralized homologous virus were characterized in indirect and sandwich ELISA using purified Rho 1/48 virus particles, subunits, trypsin-treated, and chemically denatured virus. All the MAbs inhibited haemagglutination by parental virus. Binding of the MAbs to 73 SAT 2 field isolates was measured in a sandwich ELISA and defined four distinct antigenic regions. Preliminary characterization of escape mutants selected with some of the MAbs using virus neutralization tests, ELISA, and amino acid sequencing is included. MAbs 2, 25, 40, 48 and 64, reacted with a linear epitope on the VP1 loop region. An amino acid change at position 149 (valine to glutamic acid) was detected in mutants selected by MAb 2 and 40 and this eliminated binding and neutralization by all the other MAb. This epitope was conformation-dependent and was conserved in all 73 isolates of SAT 2 examined. Escape mutants isolated with MAb 41 and 44, had changes at positions 156 (glycine to aspartic acid), or 158 (serine to leucine) respectively. These MAbs bound with Rho 1/48 only out of 73 field strain viruses studies and the reactions of MAbs from the other groups was unaltered. MAb 27, 28 and 37 reacted with a conformation-dependent epitope on VP1 which was not conserved in field isolates. All mutants selected by these MAbs had a single amino acid substitution at position 149 (valine to alanine). The same change was always found in field isolates which did not bind MAbs from this group. MAb 11 reacted with a linear epitope associated with amino acids 147 or 148 on VP1 and showed similar binding characteristics to a conformation dependent MAb 7, no amino acid residue changes were found within VP1 for monoclonal antibody 7 mutants.

journal_name

Epidemiol Infect

journal_title

Epidemiology and infection

authors

Crowther JR,Rowe CA,Butcher R

doi

10.1017/s0950268800057083

subject

Has Abstract

pub_date

1993-10-01 00:00:00

pages

391-406

issue

eissn

0950-2688

issn

1469-4409

journal_volume

111

pub_type

杂志文章

在线工具

Characterization of monoclonal antibodies against a type SAT 2 foot-and-mouth disease virus.