Mietzner T A, Barnes R C, JeanLouis Y A, Shafer W M, Morse S A
Infect Immun. 1986 Jan;51(1):60-8. doi: 10.1128/iai.51.1.60-68.1986.
Several iron-regulated proteins of Neisseria gonorrhoeae have been reported. One of these, a 37,000-molecular-weight protein (37K protein), appears to be common to all gonococcal isolates. Recently, the occurrence of a similar protein has also been noted in N. meningitidis. The gonococcal 37K protein has been purified and used to produce both rabbit monospecific antiserum and murine monoclonal antibodies. Using these antibody reagents, we analyzed 57 strains from nine species of Neisseria and the closely related organism Branhamella catarrhalis for the presence of proteins antigenically related to the gonococcal 37K protein. Strains grown on medium with low iron content were probed for antigenic reactivity by Western blot techniques and an enzyme-linked immunosorbent assay. Proteins which cross-reacted with the rabbit monospecific antiserum were designated as AgR-37K proteins. The data indicated that the AgR-37K proteins were conserved among the 40 strains of N. gonorrhoeae, N. meningitidis, N. lactamica, and N. cinerea tested. Seventeen strains from other species of Neisseria and Branhamella did not express AgR-37K proteins with the exception of one N. subflava isolate. All AgR-37K proteins appeared to be regulated by the amount of available iron in the growth medium. Murine monoclonal antibodies were used to probe the antigenic heterogeneity of the AgR-37K proteins from different Neisseria spp. Two of seven monoclonal antibodies were broadly cross-reactive, recognizing the AgR-37K proteins from all species examined. The remaining five monoclonal antibodies were more discriminating, recognizing the AgR-37K proteins from certain species. The antigenic conservation of these AgR-37K proteins, particularly among the pathogenic members of the genus Neisseria, may imply that these proteins serve a common function in pathogenicity.
已有多篇报道称淋病奈瑟菌存在几种铁调节蛋白。其中一种分子量为37,000的蛋白质(37K蛋白)似乎在所有淋病奈瑟菌分离株中都存在。最近,在脑膜炎奈瑟菌中也发现了一种类似的蛋白质。已纯化淋病奈瑟菌的37K蛋白,并用于制备兔单特异性抗血清和鼠单克隆抗体。利用这些抗体试剂,我们分析了来自9种奈瑟菌属的57株菌株以及密切相关的卡他布兰汉菌,检测是否存在与淋病奈瑟菌37K蛋白抗原相关的蛋白质。通过蛋白质印迹技术和酶联免疫吸附测定法,检测在低铁含量培养基上生长的菌株的抗原反应性。与兔单特异性抗血清发生交叉反应的蛋白质被指定为AgR-37K蛋白。数据表明,在测试的40株淋病奈瑟菌、脑膜炎奈瑟菌、乳酸奈瑟菌和灰色奈瑟菌中,AgR-37K蛋白是保守的。除了一株微黄奈瑟菌分离株外,来自奈瑟菌属其他种和卡他布兰汉菌的17株菌株不表达AgR-37K蛋白。所有AgR-37K蛋白似乎都受生长培养基中可利用铁含量的调节。使用鼠单克隆抗体检测来自不同奈瑟菌属的AgR-37K蛋白的抗原异质性。七种单克隆抗体中的两种具有广泛的交叉反应性,能识别所有检测物种的AgR-37K蛋白。其余五种单克隆抗体的识别能力更强,只能识别某些物种的AgR-37K蛋白。这些AgR-37K蛋白的抗原保守性,尤其是在奈瑟菌属的致病成员中,可能意味着这些蛋白质在致病性方面发挥着共同作用。