Escherichia coli O86 O-Antigen Biosynthetic Gene Cluster and Stepwise Enzymatic Synthesis of Human Blood Group B Antigen Tetrasaccharide

详细信息    查看全文

• 作者：Wen Yi ; Jun Shao ; Lizhi Zhu ; Mei Li ; Mamata Singh ; Yuquan Lu ; Steven Lin ; Hanfen Li ; Kang Ryu ; Jie Shen ; Hongjie Guo ; Qingjia Yao ; C. Allen Bush ; and Peng G. Wang
• 刊名：Journal of the American Chemical Society
• 出版年：2005
• 出版时间：February 23, 2005
• 年：2005
• 卷：127
• 期：7
• 页码：2040 - 2041
• 全文大小：50K
• 年卷期：v.127,no.7(February 23, 2005)
• ISSN：1520-5126

文摘

Previous study showed that some Gram-negative bacteria possess human blood group activity. Among them, Escherichia coli O86 has high blood group B activity and weak blood group A activity. This is due to the cell surface O-antigen structure, which resembles that of human blood group B antigen. In this study, we sequenced the entire E. coli O86 antigen gene cluster and identified all the genes responsible for O-antigen biosynthesis by sequence comparative analysis. The blood group B-like antigen in E. coli O86 O-polysaccharide was synthesized by sequentially employing three glycosyltransferases identified in the gene cluster. More importantly, we identified a new bacterial glycosyltransferase (WbnI) equivalent to human blood group transferase B (GTB). The enzyme substrate specificity and stepwise enzymatic synthesis of blood group B-like antigen revealed that the biosynthetic pathway of B antigen is essentially the same in E. coli O86 as in humans. This new finding provides a model to study the specificity and structure relationship of blood group transferases and supports the hypothesis of anti-blood group antibody production by bacterial stimulation.