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

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


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adhesins, Bacterial*
  • Animals
  • Antibodies, Bacterial
  • Antibodies, Monoclonal
  • Bacterial Outer Membrane Proteins / immunology
  • Bacterial Outer Membrane Proteins / isolation & purification*
  • Carrier Proteins*
  • Cell Compartmentation
  • Cross Reactions
  • Escherichia coli / chemistry*
  • Escherichia coli / immunology
  • Escherichia coli Proteins*
  • Species Specificity
  • Swine


  • Adhesins, Bacterial
  • Antibodies, Bacterial
  • Antibodies, Monoclonal
  • Bacterial Outer Membrane Proteins
  • Carrier Proteins
  • Escherichia coli Proteins
  • eaeA protein, E coli