Recombinant S-layer proteins of Lactobacillus brevis mediating antibody adhesion to calf intestine alleviated neonatal diarrhea syndrome.

Abstract:

:A chimeric gene encoding enhanced green fluorescent protein (EGFP) and a S-layer protein from Lactobacillus brevis KCTC3102, and/or two copies of the Fc-binding Z-domain, a synthetic analog of the B-domain of protein A, was constructed and expressed in Escherichia coli BL21(DE3). The S-layer fusion proteins produced in a 500-l fermentor were likely to be stable in the range of pH 5 to 8 and 0 degree to 40 degrees . Their adhesive property enabled an easy and rapid immobilization of enzymes or antibodies on solid materials such as plastics, glass, sol-gel films, and intestinal epithelial cells. Owing to their affinity towards intestinal cells and immunoglobulin G, the Slayer fusion proteins enabled the adhesion of antibodies to human epithelial cells. In addition, feeding a mixture of the S-layer fusion proteins and antibodies against neonatal calf diarrhea (coronavirus, rotavirus, Escherichia coli, and Salmonella typhimurium) to Hanwoo calves resulted in 100% prevention of neonatal calf diarrhea syndrome (p<0.01),whereas feeding antibodies only resulted in 56% prevention.

journal_name

J Microbiol Biotechnol

authors

Khang YH,Park HY,Jeong YS,Kim JA,Kim YH

doi

10.4014/jmb.0805.325

subject

Has Abstract

pub_date

2009-05-01 00:00:00

pages

511-9

issue

5

eissn

1017-7825

issn

1738-8872

pii

8277

journal_volume

19

pub_type

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