Cr. Zhu et al., DETECTION AND LOCALIZATION OF THE EAEA PROTEIN OF ATTACHING AND EFFACING ESCHERICHIA-COLI O45 FROM PIGS USING A MONOCLONAL-ANTIBODY, Microbial pathogenesis, 21(3), 1996, pp. 205-213
The eaeA-positive, attaching and effacing (A/E) O45 E. coli isolates f
rom pigs express an EaeA protein with an estimated molecular weight of
97 kDa. In the present study, a monoclonal antibody was raised agains
t the EaeA protein of an A/E O45 isolate. Cross reaction of the monocl
onal antibody with the EaeA protein of A/E strain of the rabbit (RDEC-
1), but not with those of A/E strains of the human (E2348/69) and dog
(89-4221), was observed. Reactions of the monoclonal antibody to A/E i
solates in the O45 serogroup on the ELISA varied among isolates and ap
peared to be correlated with in vivo A/E capacity of these isolates. T
he EaeA protein of A/E O45 E. coil has an apparent isoelectric point o
f 8.4 and is exposed on the bacterial surface. The monoclonal antibody
provides a useful tool for characterization of the EaeA protein of E.
coli isolates from pigs. (C) 1996 Academic Press Limited