Porro M, Costantino P, Viti S, Vannozzi F, Naggi A, Torri G
Mol Immunol. 1985 Aug;22(8):907-19. doi: 10.1016/0161-5890(85)90077-x.
A molecular model of a carbohydrate-protein conjugate is described, involving the non-toxic mutant protein CRM197, serologically related to the diphtheria toxin, covalently bound to a characterized oligosaccharide derived from the molecular structure of type 6A pneumococcal capsular polysaccharide. Physicochemical and immunochemical characteristics of this oligosaccharide-protein conjugate were consistent with a molecule showing a molar carbohydrate/protein ratio of 8, an av. mol. wt of 75,000, and retention of complete immunochemical identity when tested towards the homologous antisera. The immunological characteristics obtained after immunization of 2 animal models showed a high immunogenicity of the glycoconjugate specifically directed towards diphtheria toxin and the type 6A pneumococcal capsular polysaccharide.
描述了一种碳水化合物 - 蛋白质偶联物的分子模型，它涉及与白喉毒素血清学相关的无毒突变蛋白CRM197，该蛋白与源自6A型肺炎球菌荚膜多糖分子结构的特定寡糖共价结合。这种寡糖 - 蛋白质偶联物的物理化学和免疫化学特性与一种分子相符，该分子的碳水化合物/蛋白质摩尔比为8，平均分子量为75,000，并且在用同源抗血清检测时保留了完全的免疫化学同一性。在两种动物模型免疫后获得的免疫学特性表明，该糖偶联物具有高免疫原性，特异性针对白喉毒素和6A型肺炎球菌荚膜多糖。
