Date of Original Version
The ability of Escherichia coli K-12(K88ab) to adhere to immobilized porcine small intestine mucus was examined. E. coli K-12(K88ab) but not the isogenic E. coli K-12 strain was found to adhere readily to immobilized crude mucus but not to bovine serum albumin. The adhesion of E. coli K-12(K88ab) was inhibited in a specific fashion by anti-K88 antiserum. Adhesion was also inhibited by pretreatment of receptor-containing crude mucus preparations with sodium metaperiodate or proteolytic enzymes. Removal of glycolipids from crude mucus by chloroform methanol extraction did not affect the ability of E. coli K-12(K88ab) to bind to mucus preparations. Adsorption of crude mucus preparations with K88ab fimbriae but not type 1 fimbriae resulted in the removal of K88-specific receptors. Analysis of the pelleted fimbriae receptor complex by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, together with gel filtration chromatography of crude mucus preparations, suggest that the K88-specific receptor present in porcine small intestine mucus is a 40- to 42-kDa glycoprotein.
Metcalfe, J. W., Krogfelt, K. A., Krivan, H. C., Cohen, P. S., & Laux, D. C. (1991). Characterization and Identification of a Porcine Small Intestine Mucus Receptor for the K88ab Fimbrial Adhesin. Infec. Immun., 59(1), 91-96. Retrieved from https://iai.asm.org/content/59/1/91.
Available at: https://iai.asm.org/content/59/1/91