Morsy M A, Panangala V S, Gresham M M, Toivio-Kinnucan M
Department of Pathobiology, College of Veterinary Medicine, Auburn University, Alabama.
Avian Dis. 1992 Jan-Mar;36(1):149-53.
An agglutinating monoclonal antibody (MAb S2) specific for a 55,000-molecular-weight surface protein of Mycoplasma synoviae was developed by fusion of spleen cells from immunized BALB/c mice with P3X63 Ag8.653 myeloma cells. Immunogold labeling experiments confirmed the cell surface location of the MAb-recognized antigen. MAb S2-coated Staphylococcus aureus was used in a rapid slide coagglutination assay. Eleven M. synoviae strains, including the type strain WVU 1853, coagglutinated with MAb-coated S. aureus, but five M. gallisepticum strains (PG31, S6, R, F, and A5969) did not.
通过将免疫后的BALB/c小鼠的脾细胞与P3X63 Ag8.653骨髓瘤细胞融合，研制出了一种针对鸡滑液支原体55000分子量表面蛋白的凝集性单克隆抗体（单克隆抗体S2）。免疫金标记实验证实了单克隆抗体识别抗原的细胞表面定位。用包被有单克隆抗体S2的金黄色葡萄球菌进行快速玻片凝集试验。包括标准菌株WVU 1853在内的11株鸡滑液支原体菌株与包被有单克隆抗体的金黄色葡萄球菌发生凝集反应，但5株鸡毒支原体菌株（PG31、S6、R、F和A5969）未发生凝集反应。
