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利什曼原虫无鞭毛体:对补体介导的细胞溶解的抗性并非由于无法固定C3。

Leishmania amastigotes: resistance to complement-mediated lysis is not due to a failure to fix C3.

作者信息

Mosser D M, Wedgwood J F, Edelson P J

出版信息

J Immunol. 1985 Jun;134(6):4128-31.

PMID:3886796
Abstract

Amastigote forms of Leishmania major are sensitive to lysis by fresh serum, whereas those of L. donovani are resistant. To understand the basis for this resistance we have examined the interaction of complement with amastigotes of seven strains of leishmania. Complement activation was determined by measuring the ability of amastigotes to consume complement from normal serum and by identifying parasite surface-bound C3. All of the strains that were tested activated complement, including both those that are resistant and those that are susceptible to inactivation by fresh serum. Complement consumption by amastigotes was measured as a decrease in the ACH 50 titers of serum exposed to parasites. L. major, L. donovani, and L. mexicana mexicana (strain 1VLM) amastigotes decrease titers by 35.7, 33.5, and 40.3%, respectively. The binding of C3 to amastigotes was judged qualitatively by immunofluorescence and quantitatively by a C3 radiobinding assay. L. major amastigotes bind an average of 6.6 X 10(4) molecules of C3 per parasite. L. mexicana amazonensis, L. mexicana mexicana, and L. donovani bind an average of 3.9 X 10(4), 5.9 X 10(4), and 3.7 X 10(4) molecules, respectively. In all cases, C3 binding is the result of alternative pathway activation requiring Mg++ but not Ca++. Amastigotes of the disseminating strains of leishmania represent the first example of a group of protozoa that activate early complement components leading to fixation of C3, but that are resistant to inactivation by complement.

摘要

硕大利什曼原虫的无鞭毛体形式对新鲜血清的溶解敏感,而杜氏利什曼原虫的无鞭毛体则具有抗性。为了解这种抗性的基础,我们研究了补体与七种利什曼原虫菌株的无鞭毛体之间的相互作用。通过测量无鞭毛体从正常血清中消耗补体的能力以及鉴定寄生虫表面结合的C3来确定补体激活。所有测试的菌株都激活了补体,包括那些具有抗性的菌株和那些对新鲜血清灭活敏感的菌株。无鞭毛体消耗补体的量通过测定暴露于寄生虫的血清的ACH 50滴度的降低来衡量。硕大利什曼原虫、杜氏利什曼原虫和墨西哥利什曼原虫(1VLM株)的无鞭毛体分别使滴度降低35.7%、33.5%和40.3%。通过免疫荧光定性判断C3与无鞭毛体的结合,并通过C3放射结合试验进行定量。硕大利什曼原虫的无鞭毛体每个寄生虫平均结合6.6×10⁴个C3分子。亚马逊利什曼原虫、墨西哥利什曼原虫和杜氏利什曼原虫分别平均结合3.9×10⁴、5.9×10⁴和3.7×10⁴个分子。在所有情况下,C3结合是替代途径激活的结果,需要Mg²⁺但不需要Ca²⁺。利什曼原虫传播菌株的无鞭毛体代表了一组原生动物的第一个例子,这些原生动物激活早期补体成分导致C3固定,但对补体灭活具有抗性。

相似文献

1
Leishmania amastigotes: resistance to complement-mediated lysis is not due to a failure to fix C3.利什曼原虫无鞭毛体:对补体介导的细胞溶解的抗性并非由于无法固定C3。
J Immunol. 1985 Jun;134(6):4128-31.
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Complement-mediated serum cytotoxicity for Leishmania major amastigotes: killing by serum deficient in early components of the membrane attack complex.补体介导的针对硕大利什曼原虫无鞭毛体的血清细胞毒性:由缺乏膜攻击复合物早期成分的血清导致的杀伤作用。
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Secreted proteophosphoglycan of Leishmania mexicana amastigotes activates complement by triggering the mannan binding lectin pathway.墨西哥利什曼原虫无鞭毛体分泌的蛋白磷酸聚糖通过触发甘露聚糖结合凝集素途径激活补体。
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Serum resistance of metacyclic stage Leishmania major promastigotes is due to release of C5b-9.大型利什曼原虫前鞭毛体循环后期阶段的血清抗性归因于C5b-9的释放。
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Complement receptor 3 deficiency influences lesion progression during Leishmania major infection in BALB/c mice.
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Infect Immun. 2009 Dec;77(12):5668-75. doi: 10.1128/IAI.00802-08. Epub 2009 Sep 21.
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Lipophosphoglycan is not required for infection of macrophages or mice by Leishmania mexicana.墨西哥利什曼原虫感染巨噬细胞或小鼠并不需要脂磷酸聚糖。
EMBO J. 2000 May 2;19(9):1953-62. doi: 10.1093/emboj/19.9.1953.
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Infect Immun. 1996 Nov;64(11):4769-75. doi: 10.1128/iai.64.11.4769-4775.1996.
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