Daniels Calvin C, Briles Travis C, Mirza Shaper, Håkansson Anders P, Briles David E
Department of Microbiology, University of Alabama at Birmingham, BBRB, 1530 3rd Ave North, Birmingham, AL 35294, USA.
Microb Pathog. 2006 May;40(5):228-33. doi: 10.1016/j.micpath.2006.01.007. Epub 2006 Mar 15.
Of the proteins on the surface of Streptococcus pneumoniae, one of those best able to elicit protection against pneumococcal infection is pneumococcal surface protein A (PspA). Although this protein is attached to the membrane molecule, lipoteichoic acid, which is well beneath the capsule, PspA's ability to inhibit complement deposition and killing by apolactoferrin, suggests that it must have surface exposure. This study provides quantitative data showing that the capsular polysaccharide on types 2 and 3 pneumococci provides little or no masking ability of antibodies to bind PspA. Capsule was even observed to enhance, rather than inhibit the binding of two protective monoclonal antibodies to their epitopes on cell surface PspA. These results with antibodies to PspA are in contrast to binding by antibodies to the phosphocholine (PC) epitope of the lipoteichoic and teichoic acids. The binding of antibody to PC was largely, but not completely, blocked by capsular polysaccharide.
在肺炎链球菌表面的蛋白质中,最能引发针对肺炎球菌感染的保护性反应的蛋白质之一是肺炎球菌表面蛋白A(PspA)。尽管这种蛋白质附着于膜分子脂磷壁酸上,而脂磷壁酸位于荚膜下方较深处,但PspA抑制补体沉积和脱铁乳铁蛋白杀伤作用的能力表明它必定暴露于表面。本研究提供了定量数据,表明2型和3型肺炎球菌上的荚膜多糖对抗体结合PspA几乎没有或根本没有屏蔽能力。甚至观察到荚膜增强而非抑制两种保护性单克隆抗体与其在细胞表面PspA上的表位的结合。这些针对PspA的抗体的结果与针对脂磷壁酸和磷壁酸的磷酸胆碱(PC)表位的抗体的结合情况形成对比。抗体与PC的结合在很大程度上但并非完全被荚膜多糖阻断。