Open AccessThe outer membrane protein of enteropathogenic Escherichia coli , described as the ‘localised adherence factor’, is OmpF and probably not involved in adhesion to HEp‐2 cells
Author(s) -
Chart Henrik,
Rowe Bernard
Publication year - 1989
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1989.tb03639.x
Subject(s) - porin , bacterial outer membrane , peptidoglycan , escherichia coli , microbiology and biotechnology , hela , bacterial adhesin , biology , enteropathogenic escherichia coli , enterobacteriaceae , salmonella , bacteria , adhesion , membrane protein , chemistry , membrane , biochemistry , in vitro , gene , genetics , organic chemistry
Strains of enteropathogenic Escherichia coli (EPEC) were examined for a factor, described as an outer membrane protein (OMP) of 32 kilodaltons (kDa) and reported to be involved in the adhesion of EPEC to HeLa cells. A comparable OMP of 35 kDa was detected in strains of EPEC, although expression of this protein was not related to the ability of strains to adhere to HEp‐2 cells. The 35 kDa OMP was found to be heat‐modifiable and peptidoglycan associated, and considered to be the porin protein OmpF.