Interaction of P-fimbriated Escherichia coli with human meconium.
The ability of Escherichia coli with different receptor specificities to interact with meconium was studied. E. coli strains expressing P-fimbriae, specific for Gal alpha 1-4Gal beta-containing receptors, were agglutinated by meconium at high titres. This reaction was inhibited by globotetraosylceramide. The attachment of P-fimbriated E. coli to human colonic epithelial cells of the HT-29 cell line was inhibited by meconium. Some type 1 fimbriated strains were agglutinated by meconium, but the agglutination was rarely blocked by methyl alpha-D-mannoside. The attachment by type 1 fimbriated strains to HT-29 cells was reduced by meconium only in some cases. These results suggest that meconium interacts with the P-fimbriae of E. coli, in a way that may influence bacterial colonization of the neonatal intestine.
Adlerberth
I
I
Department of Clinical Immunology, University of Göteborg, Sweden.
Svanborg
C
C
Hanson
L A
LA
Carlsson
B
B
Mellander
L
L
Jalil
F
F
Larsson
P
P
Wold
A E
AE
D018830:Adhesins, Escherichia coli; D000372:Agglutination Tests; D001422:Bacterial Adhesion; D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism; D002240:Carbohydrate Sequence; D002460:Cell Line; D004926:Escherichia coli / Q000502:physiology* / Q000648:ultrastructure; D010861:Fimbriae, Bacterial / Q000502:physiology; D006801:Humans; D007231:Infant, Newborn; D008470:Meconium / Q000382:microbiology*; D008969:Molecular Sequence Data
D018830:Adhesins, Escherichia coli; D001425:Bacterial Outer Membrane Proteins