Thin aggregative fimbriae from diarrheagenic Escherichia coli.
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.
Collinson
S K
SK
Department of Biochemistry and Microbiology, University of Victoria, British Columbia.
Emödy
L
L
Trust
T J
TJ
Kay
W W
WW
D000595:Amino Acid Sequence; D003967:Diarrhea / Q000382:microbiology*; D004926:Escherichia coli / Q000235:genetics / Q000302:isolation & purification / Q000648:ultrastructure*; D006801:Humans; D008562:Membrane Glycoproteins / Q000032:analysis* / Q000235:genetics; D008565:Membrane Proteins / Q000032:analysis; D008840:Microfilament Proteins; D016253:Microscopy, Immunoelectron; D008969:Molecular Sequence Data; D012477:Salmonella enteritidis / Q000235:genetics / Q000648:ultrastructure; D012689:Sequence Homology, Nucleic Acid
D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D008840:Microfilament Proteins; C026742:plastin