Nealon T J, Beachey E H, Courtney H S, Simpson W A
Infect Immun. 1986 Feb;51(2):529-35. doi: 10.1128/iai.51.2.529-535.1986.
Fibronectin binds to Streptococcus pyogenes, and this binding is inhibited by lipoteichoic acid (LTA). Previous studies have shown that LTA can be released from S. pyogenes by treatment with penicillin. Penicillin released LTA from both S. pyogenes and Staphylococcus aureus; however, the binding of fibronectin correlated with the amount of LTA released only in the case of S. pyogenes. Contrarily, clindamycin decreased the ability of S. aureus to bind fibronectin without affecting the binding of fibronectin to S. pyogenes. Further studies indicated that LTA does not inhibit the binding of fibronectin to S. aureus. Fibronectin bound to S. pyogenes could be released from the cell surface by penicillin. Immunological analysis of the released fibronectin indicated that LTA was the only surface component which could be detected as a soluble complex with the released fibronectin. These studies suggest that LTA plays a central role in the binding of fibronectin to S. pyogenes and is not involved in the binding of fibronectin to S. aureus.
纤连蛋白可与化脓性链球菌结合，而这种结合会受到脂磷壁酸（LTA）的抑制。先前的研究表明，用青霉素处理可使LTA从化脓性链球菌中释放出来。青霉素能从化脓性链球菌和金黄色葡萄球菌中释放LTA；然而，只有在化脓性链球菌的情况下，纤连蛋白的结合才与释放的LTA量相关。相反，克林霉素降低了金黄色葡萄球菌结合纤连蛋白的能力，而不影响纤连蛋白与化脓性链球菌的结合。进一步的研究表明，LTA并不抑制纤连蛋白与金黄色葡萄球菌的结合。与化脓性链球菌结合的纤连蛋白可被青霉素从细胞表面释放出来。对释放出的纤连蛋白进行免疫分析表明，LTA是唯一能被检测到与释放出的纤连蛋白形成可溶性复合物的表面成分。这些研究表明，LTA在纤连蛋白与化脓性链球菌的结合中起核心作用，而不参与纤连蛋白与金黄色葡萄球菌的结合。
