Affiliation:
1. Department of Gastroenterology, Walter Reed Army Institute of Research, Washington, D.C. 20307-5100, USA.
Abstract
Intimin, an outer membrane protein encoded by eaeA that mediates close attachment of enteropathogenic bacteria to apical surfaces of epithelial cells, is required for formation of the attaching-effacing lesions and for full pathogenesis of the bacteria. Analysis of the eaeA sequence indicates that there is a high degree of homology at the N termini but less at the C termini of intimins. Antisera specific for the C-terminal third of RDEC-1 intimin, used to screen outer membrane proteins from 50 rabbit enteropathogenic Escherichia coli (EPEC), human EPEC, and human enterohemorrhagic E. coli (EHEC) strains, identified cross-reactive intimins from 24 isolates. Sequence analysis of the eaeA genes from human EPEC O111 and EHEC O26 isolates indicates that their intimins have C termini nearly identical to that of RDEC-1 intimin. Our results suggest that there are at least three families of related intimins and that the presence of intimin similar to that of RDEC-1 is not restricted by serogroup or host specificity.
Publisher
American Society for Microbiology
Subject
Infectious Diseases,Immunology,Microbiology,Parasitology
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