Honma Y, Yamamoto K, Iwanaga M
Department of Bacteriology, Faculty of Medicine, University of the Ryukyus, Okinawa, Japan.
FEMS Microbiol Lett. 1995 Nov 1;133(1-2):151-4. doi: 10.1111/j.1574-6968.1995.tb07876.x.
Vibrio cholerae non-O1 strain N037 produced a hemolysin (NO37-Hly) which was antigenically similar to E1 Tor hemolysin (E1 Tor-Hly) but different in molecular size, hemolytic activity, and glucose binding capacity. In the gene encoding NO37-Hly, a 4-bp insertion into the structural gene for E1 Tor-Hly (hlyA) was found. The insertion in a shift of codon frames generating a new stop codon in the downstream region. NO37-Hly was a truncated product of E1 Tor-Hly sharing 90% of the N terminal region. This suggested that the 10% C-terminal region of E1 Tor-Hly is needed for the maximal hemolytic activity and glucose binding capacity.
霍乱弧菌非O1血清型菌株N037产生一种溶血素(NO37-Hly),其抗原性与埃尔托溶血素(E1 Tor-Hly)相似,但分子大小、溶血活性和葡萄糖结合能力不同。在编码NO37-Hly的基因中,发现有一个4碱基对插入到埃尔托溶血素(hlyA)的结构基因中。该插入导致密码子框架移位,在下游区域产生一个新的终止密码子。NO37-Hly是埃尔托溶血素的截短产物,共享90%的N端区域。这表明埃尔托溶血素10%的C端区域对于最大溶血活性和葡萄糖结合能力是必需的。