Marciano-Cabral F, Cline M L, Bradley S G
J Clin Microbiol. 1987 Apr;25(4):692-7. doi: 10.1128/jcm.25.4.692-697.1987.
Serum samples from adult humans in North Carolina and Pennsylvania were assayed for antibodies against four Naegleria species: N. australiensis, N. fowleri, N. gruberi, and N. lovaniensis. Agglutinating activities of serum samples from North Carolina subjects were higher for N. fowleri than were those from Pennsylvania subjects. The distributions of agglutination titers of human serum samples for N. australiensis, N. gruberi, and N. lovaniensis were heterogeneous. The agglutination capabilities of selected serum samples absorbed with rounded, killed trophozoites of N. australiensis and N. lovaniensis were distinctly different, as were those of serum samples absorbed with N. fowleri and N. gruberi. N. australiensis and N. gruberi shared some agglutinating antigens, as did N. fowleri and N. lovaniensis. The agglutinating activities of most serum samples correlated with the capability of their immunoglobulin M (IgM) to bind to antigens in extracts of Naegleria species but not with the capabilities of their IgG to bind to antigens of Naegleria species. Absorption of IgM binding capability with rounded, killed trophozoites established that N. gruberi was distinctly different from N. fowleri and N. lovaniensis but that N. fowleri and N. lovaniensis shared surface antigens. The proteins in extracts of the four Naegleria species were subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and tested for their ability to bind immunoglobulins in a serum sample. The antigens of the four species that bound IgM or IgG in the tested serum sample were separated by SDS-PAGE, and when they were incubated with anti-IgM or anti-IgG, they gave distinct profiles. There was one distinct, shared antigen that had a molecular size of 40,000 daltons. Absorption of the test serum with killed, rounded trophozoites did not markedly change the immunoglobulin binding profile for Naegleria internal antigens separated by SDS-PAGE and did not remove the shared 40,000-dalton protein(s). These results demonstrate that the four Naegleria species have antigenically distinct surfaces and that humans have been individually exposed to antigens of Naegleria species.
对来自北卡罗来纳州和宾夕法尼亚州的成年人类血清样本进行了检测，以确定其针对四种耐格里属物种的抗体：澳大利亚耐格里阿米巴、福氏耐格里阿米巴、格氏耐格里阿米巴和洛万耐格里阿米巴。北卡罗来纳州受试者血清样本对福氏耐格里阿米巴的凝集活性高于宾夕法尼亚州受试者的血清样本。人类血清样本对澳大利亚耐格里阿米巴、格氏耐格里阿米巴和洛万耐格里阿米巴的凝集滴度分布不均一。用圆形、灭活的澳大利亚耐格里阿米巴和洛万耐格里阿米巴滋养体吸收的选定血清样本的凝集能力明显不同，用福氏耐格里阿米巴和格氏耐格里阿米巴吸收的血清样本的凝集能力也明显不同。澳大利亚耐格里阿米巴和格氏耐格里阿米巴共享一些凝集抗原，福氏耐格里阿米巴和洛万耐格里阿米巴也是如此。大多数血清样本的凝集活性与其免疫球蛋白M（IgM）结合耐格里属物种提取物中抗原的能力相关，但与其IgG结合耐格里属物种抗原的能力无关。用圆形、灭活的滋养体吸收IgM结合能力表明，格氏耐格里阿米巴与福氏耐格里阿米巴和洛万耐格里阿米巴明显不同，但福氏耐格里阿米巴和洛万耐格里阿米巴共享表面抗原。对四种耐格里属物种提取物中的蛋白质进行十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（SDS-PAGE），并检测其结合血清样本中免疫球蛋白的能力。通过SDS-PAGE分离出在测试血清样本中结合IgM或IgG的四种物种的抗原，当它们与抗IgM或抗IgG孵育时，呈现出不同的图谱。有一种明显的共享抗原，其分子大小为40000道尔顿。用灭活的圆形滋养体吸收测试血清，并未显著改变通过SDS-PAGE分离的耐格里属内部抗原的免疫球蛋白结合图谱，也未去除共享的40000道尔顿蛋白质。这些结果表明，四种耐格里属物种具有抗原性不同的表面，并且人类个体已接触过耐格里属物种的抗原。
