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http://dx.doi.org/10.4014/jmb.0805.325

Recombinant S-Layer Proteins of Lactobacillus brevis Mediating Antibody Adhesion to Calf Intestine Alleviated Neonatal Diarrhea Syndrome  

Khang, Yong-Ho (School of Biotechnology, Yeungnam University)
Park, Hee-Young (School of Biotechnology, Yeungnam University)
Jeong, Yoo-Seok (School of Biotechnology, Yeungnam University)
Kim, Jung-Ae (College of Pharmacy, Yeungnam University)
Kim, Young-Hwan (Gyeongsangbuk-do Veterinary Service Laboratory)
Publication Information
Journal of Microbiology and Biotechnology / v.19, no.5, 2009 , pp. 511-519 More about this Journal
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 Fe-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 500-1 fermentor were likely to be stable in the range of pH 5 to 8 and $0^{\circ}C$ to $40^{\circ}C$. 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 S-layer 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.
Keywords
Antibody adhesion; enzyme immobilization; Hanwoo calf; Lactobacillus brevis; neonatal diarrhea; recombinant S-layer;
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