Four strains of diarrheagenic Escherichia coli originally isolated from distinct geographic regions were found to produce unusual thin aggregative fimbriae requiring depolymerization in formic acid prior to analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Immunoelectron microscopy of native fimbriae and Western blot (immunoblot) analysis of the corresponding 18-kDa fimbrins showed that these E. coli fimbriae were serologically cross-reactive with SEF 17 (Salmonella enteritidis fimbriae with a fimbrin molecular mass of 17 kDa). The E. coli and S. enteritidis fimbrins had similar total amino acid compositions and highly conserved N-terminal amino acid sequences. These results indicate that E. coli and S. enteritidis produce biochemically related, aggregative fimbriae which constitute a new type of intergenerically distributed fimbriae for which we propose the descriptive name GVVPQ fimbriae on the basis of the conserved N-terminal amino acid sequence.Successful bacterial pathogens present to their susceptible host complex cell surfaces which contain components enabling the bacteria to initially associate with and subsequently adhere to specific host tissues (2, 21). The attachment of enteropathogens to gastrointestinal epithelial cells is presumed to be essential if these bacteria are to avoid host clearance mechanisms and compete with normal flora for appropriate niches (2, 15). However, the specific attachment mechanism(s) of many enteropathogens in vivo has not been clearly established (2,14).