从虾壳表面提取的霍乱弧菌蛋白质冷冻保护剂的纯化与表征

Purification and characterization of a protein cryoprotective for Vibrio cholerae extracted from the prawn shell surface.

作者信息

Faming D, Shimodori S, Moriya T, Iwanaga S, Amako K

机构信息

Department of Bacteriology, Faculty of Medicine, Kyushu University, Fukuoka, Japan.

出版信息

Microbiol Immunol. 1993;37(11):861-8. doi: 10.1111/j.1348-0421.1993.tb01717.x.

DOI:10.1111/j.1348-0421.1993.tb01717.x

PMID:8295565

Abstract

A substance cryoprotective for Vibrio cholerae on the prawn shell surface was purified by ammonium sulfate precipitation and gel filtration. It was a protein of 81 kDa and called cryoprotective protein (CPP). The cryoprotective activity of this protein for V. cholerae was sensitive to heat at 100 C and trypsin treatment. In the presence of Mg ion the protein can bind to the bacterial cell surface. V. cholerae can adhere to the shell surface of the prawn. The number of adhered bacteria was reduced by treating the shell with anti-CPP serum, heat or by trypsin. The presence of Mg ion promoted the adherence. These results suggest that the CPP could serve as an adherence site for V. cholerae on the shell surface.

摘要

通过硫酸铵沉淀和凝胶过滤法，对虾壳表面上对霍乱弧菌具有 cryoprotective 作用的一种物质进行了纯化。它是一种 81 kDa 的蛋白质，被称为 cryoprotective protein（CPP）。这种蛋白质对霍乱弧菌的 cryoprotective 活性对 100℃的热和胰蛋白酶处理敏感。在镁离子存在的情况下，该蛋白质可以结合到细菌细胞表面。霍乱弧菌能够附着在虾的壳表面。用抗 CPP 血清、加热或胰蛋白酶处理虾壳后，附着的细菌数量减少。镁离子的存在促进了附着。这些结果表明，CPP 可以作为霍乱弧菌在壳表面的一个附着位点。