Tarsi R, Pruzzo C
Institute of Microbiology, University of Ancona, 60131 Ancona, Italy.
Appl Environ Microbiol. 1999 Mar;65(3):1348-51. doi: 10.1128/AEM.65.3.1348-1351.1999.
The role of surface proteins in Vibrio cholerae attachment to chitin particles in vitro was studied. Treatment of V. cholerae O1 ATCC 14034 and ATCC 14035 with pronase E reduced the attachment of bacteria to chitin particles by 57 to 77%. A statistically significant reduction was also observed when the attachment to chitin was evaluated in the presence of homologous Sarkosyl-insoluble membrane proteins (MPs) (67 to 84%), N-acetylglucosamine (GlcNAc) (62%), the sugar that makes up chitin, and wheat germ agglutinin (40 to 56%), a lectin that binds GlcNAc. The soluble oligomers N,N'-diacetylchitobiose or N,N', N"-triacetylchitotriose caused an inhibition of 14 to 23%. Sarkosyl-insoluble MPs able to bind chitin particles were isolated and visualized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis; two of these peptides (molecular sizes, 36 and 53 kDa) specifically bind GlcNAc.
研究了表面蛋白在霍乱弧菌体外附着于几丁质颗粒中的作用。用链霉蛋白酶E处理霍乱弧菌O1 ATCC 14034和ATCC 14035，可使细菌对几丁质颗粒的附着减少57%至77%。当在同源月桂酰肌氨酸钠不溶性膜蛋白（MPs）（67%至84%）、N-乙酰葡糖胺（GlcNAc）（62%）（构成几丁质的糖类）和麦胚凝集素（40%至56%）（一种结合GlcNAc的凝集素）存在的情况下评估对几丁质的附着时，也观察到了统计学上的显著降低。可溶性低聚物N,N'-二乙酰壳二糖或N,N',N"-三乙酰壳三糖引起了14%至23%的抑制。通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳分离并可视化了能够结合几丁质颗粒的月桂酰肌氨酸钠不溶性MPs；其中两种肽（分子大小分别为36 kDa和53 kDa）特异性结合GlcNAc。
