Sato Y, Yamamoto Y, Kizaki H
Department of Biochemistry, Tokyo Dental College, Chiba City, Japan.
Infect Immun. 1997 Feb;65(2):668-75. doi: 10.1128/iai.65.2.668-675.1997.
We have isolated dextran-aggregation-negative mutants of Streptococcus mutans following random mutagenesis with plasmid pVA891 clone banks. A chromosomal region responsible for this phenotype was characterized in one of the mutants. A 2.2-kb fragment from the region was cloned in Escherichia coli and sequenced. A gene specifying a putative protein of 583 amino acid residues with a calculated molecular weight of 63,478 was identified. The amino acid sequence deduced from the gene exhibited no similarity to the previously identified S. mutans 74-kDa glucan-binding protein or to glucan-binding domains of glucosyltransferases but exhibited similarity to surface protein antigen (Spa)-family proteins from streptococci. Extract from an E. coli clone of the gene exhibited glucan-binding activity. Therefore, the gene encoded a novel glucan-binding protein.
我们利用质粒pVA891克隆文库进行随机诱变,分离出了变形链球菌的葡聚糖聚集阴性突变体。在其中一个突变体中对负责该表型的染色体区域进行了表征。从该区域获得的一个2.2kb片段被克隆到大肠杆菌中并进行测序。鉴定出一个基因,该基因编码一个推定的蛋白质,由583个氨基酸残基组成,计算分子量为63478。从该基因推导的氨基酸序列与先前鉴定的变形链球菌74kDa葡聚糖结合蛋白或葡糖基转移酶的葡聚糖结合结构域没有相似性,但与链球菌的表面蛋白抗原(Spa)家族蛋白具有相似性。该基因的大肠杆菌克隆提取物表现出葡聚糖结合活性。因此,该基因编码一种新型葡聚糖结合蛋白。