Avila J L, Rojas M
Instituto de Biomedicina, Caracas, Venezuela.
J Clin Microbiol. 1990 Jul;28(7):1530-7. doi: 10.1128/jcm.28.7.1530-1537.1990.
An immunoglobulin M antibody reactive with galactosyl(alpha 1-3)mannose [Gal(alpha 1-3)Man] residues present on phospholipids extracted from Leishmania mexicana and L. braziliensis was found to be present in high titer in the serum of every normal individual studied. Periodate oxidation, acid hydrolysis, or acetylation suppressed immunoreactivity, suggesting that an oligosaccharide chain was responsible for antibody binding. Interaction occurs only with alpha-Gal terminal residues, since treatment of purified glycophospholipids with alpha-galactosidase but not with beta-galactosidase abolished it. Antibody bound to galactosyl(alpha 1-3)galactose-linked synthetic antigens but did not bind to the same residues present in rabbit, rat, and guinea pig erythrocytes or in murine laminin. Antigen-antibody binding was strongly blocked with Gal(alpha 1-3)Man and Gal(beta 1-4)Man. These results plus inhibition studies with several oligosaccharides suggest that they are indeed different from antibodies against the galactosyl(alpha 1-3)galactose residue. Anti-Gal(alpha 1-3)Man antibody values were significantly elevated in 89% of patients with diffuse cutaneous leishmaniasis, 84% of patients with localized cutaneous leishmaniasis, 69% of patients with mucocutaneous leishmaniasis, and 44 and 62% of patients with Trypanosoma cruzi or T. rangeli infection, respectively, but not in patients with 15 other different infectious and inflammatory diseases. Anti-Gal(alpha 1-3)Man antibody readily absorbed to American Leishmania and Trypanosoma culture forms, suggesting a surface membrane localization of reactive epitope. Gal(alpha 1-3)Man-bearing glycophospholipid was easily extracted from American Leishmania promastigotes and T. cruzi trypomastigotes as well as from American Trypanosoma culture forms. The possibility that this antibody arises against parasitic glycophospholipid-linked Gal(alpha 1-3)Man terminal residues is proposed.
在从墨西哥利什曼原虫和巴西利什曼原虫中提取的磷脂上存在与半乳糖基（α1-3）甘露糖[Gal（α1-3）Man]残基反应的免疫球蛋白M抗体，发现在每个被研究的正常个体血清中都有高滴度存在。高碘酸盐氧化、酸水解或乙酰化会抑制免疫反应性，这表明寡糖链是抗体结合的原因。相互作用仅发生在α-半乳糖末端残基上，因为用α-半乳糖苷酶而非β-半乳糖苷酶处理纯化的糖脂会消除这种相互作用。抗体与半乳糖基（α1-3）半乳糖连接的合成抗原结合，但不与兔、大鼠和豚鼠红细胞或鼠层粘连蛋白中存在的相同残基结合。抗原-抗体结合被Gal（α1-3）Man和Gal（β1-4）Man强烈阻断。这些结果以及用几种寡糖进行的抑制研究表明，它们确实不同于针对半乳糖基（α1-3）半乳糖残基的抗体。在89%的弥漫性皮肤利什曼病患者、84%的局限性皮肤利什曼病患者、69%的黏膜皮肤利什曼病患者以及分别44%和62%的克氏锥虫或朗氏锥虫感染患者中，抗Gal（α1-3）Man抗体值显著升高，但在其他15种不同的感染性和炎症性疾病患者中未升高。抗Gal（α1-3）Man抗体很容易吸附到美洲利什曼原虫和锥虫培养形式上，这表明反应性表位位于表面膜。带有Gal（α1-3）Man的糖脂很容易从美洲利什曼原虫前鞭毛体、克氏锥虫锥鞭毛体以及美洲锥虫培养形式中提取出来。有人提出这种抗体是针对寄生糖脂连接的Gal（α1-3）Man末端残基产生的可能性。
