Nimmich W
Institut für Medizinische Mikrobiologie, Medizinische Fakultät, Universität Rostock, Germany.
FEMS Microbiol Lett. 1997 Aug 1;153(1):105-10. doi: 10.1111/j.1574-6968.1997.tb10470.x.
The serologically and structurally related Eschrichia coli capsular polysaccharides (K antigens) K13, K20, and K23 were found to be depolymerized by the bacteriophages phi K13 and phi K20 to almost similar oligomer profiles as shown by polyacrylamide gel electrophoresis. The phage-polysaccharide interactions were followed by an increase of reducing 2-keto-3-deoxyoctulosonic acid due to a phage-associated glycanase that catalyzed the hydrolytic cleavage of common beta-ketopyranosidic 2-keto-3-deoxyoctulosonic acid linkages. The related E. coli K antigens K18, K22, and K100 as well as the Haemophilus influenzae type b capsular polysaccharide were degraded by bacteriophage phi K100 with different efficacy. It is suggested that phi K100 enzymatically cleaves ribitol-5-phosphate bonds as the only structural feature present in all the polysaccharides investigated.
血清学和结构上相关的大肠杆菌荚膜多糖（K抗原）K13、K20和K23被噬菌体φK13和φK20解聚，聚丙烯酰胺凝胶电泳显示其寡聚物谱几乎相似。噬菌体与多糖的相互作用表现为还原型2-酮-3-脱氧辛糖酸增加，这是由于一种噬菌体相关的聚糖酶催化了常见的β-酮吡喃糖苷2-酮-3-脱氧辛糖酸键的水解裂解。相关的大肠杆菌K抗原K18、K22和K100以及b型流感嗜血杆菌荚膜多糖被噬菌体φK100以不同的效率降解。有人提出，φK100酶促切割核糖醇-5-磷酸键，这是所有研究的多糖中唯一存在的结构特征。
