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Detection and localization of the EaeA protein of attaching and effacing Escherichia coli O45 from pigs using a monoclonal antibody.

作者信息

Zhu C, Ménard S, Dubreuil J D, Fairbrother J M

机构信息

Groupe de Recherche sur les Maladies Infectieuses du Porc, Université de Montréal, Faculté de Médecine Vétérinaire, Québec, Canada.

出版信息

Microb Pathog. 1996 Sep;21(3):205-13. doi: 10.1006/mpat.1996.0055.

DOI:10.1006/mpat.1996.0055
PMID:8878017
Abstract

The eaeA-positive, attaching and effacing (A/E) O45 E. coli isolates from pigs express an EaeA protein with an estimated molecular weight of 97 kDa. In the present study, a monoclonal antibody was raised against the EaeA protein of an A/E O45 isolate. Cross reaction of the monoclonal 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 isolates in the O45 serogroup on the ELISA varied among isolates and appeared to be correlated with in vivo A/E capacity of these isolates. The EaeA protein of A/E O45 E. coli has an apparent isoelectric point of 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.

摘要

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