CHARACTERIZATION AND IDENTIFICATION OF A PORCINE SMALL-INTESTINE MUCUS RECEPTOR FOR THE K88AB FIMBRIAL ADHESIN

被引:48
作者
METCALFE, JW
KROGFELT, KA
KRIVAN, HC
COHEN, PS
LAUX, DC
机构
[1] UNIV RHODE ISL, DEPT MICROBIOL, KINGSTON, RI 02881 USA
[2] TECH UNIV DENMARK, DEPT MICROBIOL, DK-2800 LYNGBY, DENMARK
[3] BIOCARB INC, DEPT MICROBIOL, GAITHERSBURG, MD 20879 USA
关键词
D O I
10.1128/IAI.59.1.91-96.1991
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
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 procine small intestine mucus is a 40- to 42-kDa glycoprotein.
引用
收藏
页码:91 / 96
页数:6
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