Mycoplasma hyopneumoniae evades complement activation by binding to factor H via elongation factor thermo unstable (EF-Tu).
Mycoplasma hyopneumoniae evades complement activation by binding to factor H via elongation factor thermo unstable (EF-Tu).
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猪肺炎支原体通过热不稳定延伸因子 (EF-Tu) 与 H 因子结合来逃避补体激活
DOI：
10.1080/21505594.2020.1806664
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发表时间：
2020-12
期刊：
影响因子：
5.2
通讯作者：
Xiong Q
中科院分区：
文献类型：
--
作者：
Yu Y;Wang J;Han R;Wang L;Zhang L;Zhang AY;Xin J;Li S;Zeng Y;Shao G;Feng Z;Xiong Q
支原体在宿主体内存在很长时间，表明它们具有免疫逃避机制。因子H是补体系统的负调节因子，其结合宿主细胞以避免意外的补体激活。在这项研究中，我们发现许多支原体，如猪肺炎支原体、猪鼻支原体、猪滑液支原体、鸡毒支原体、肺炎支原体、生殖支原体、絮状支原体和牛支原体可以劫持因子H，使它们作为宿主组织出现，从而逃避补体攻击。此外，在M.下丘脑M.猪肺炎支原体通过因子H结合蛋白结合因子H，例如延伸因子热不稳定（EF-Tu）、P146、丙酮酸脱氢酶（乙酰转移）E1组分亚基α（PdhA）、P46、丙酮酸脱氢酶E1组分亚基β（PdhB）、甘油醛-3-磷酸脱氢酶（GAPDH）和三种不同的假设蛋白。EF-Tu与H因子的结合进一步有助于减少M上的C3沉积。并最终阻断进一步的补体激活。事实上，H因子的结合是以多因素的方式发生的; H因子不仅被M利用。猪肺炎支原体通过其调节活性帮助支原体逃避补体杀伤，但也增加了支原体。部分通过EF-Tu将猪气管上皮细胞粘附于猪气管上皮细胞。同时，上述支原体EF-Tu蛋白之间的高度序列同源性暗示了该机制的普遍性。这是首次报道支原体可以通过与H因子结合而逃避补体杀伤。
Mycoplasmas persist in the host for a long time, suggesting that they possess mechanisms for immune evasion. Factor H is a negative regulator of the complement system, which binds to host cells to avoid unexpected complement activation. In this study, we revealed that many mycoplasmas, such as Mycoplasma hyopneumoniae, Mycoplasma hyorhinis, Mycoplasma hyosynoviae, Mycoplasma gallisepticum, Mycoplasma pneumoniae, Mycoplasma genitalium, Mycoplasma flocculare, and Mycoplasma bovis could hijack factor H such that they present themselves as a host tissue and thus escape from complement attack. Furthermore, the mechanism of recruiting factor H was identified in M. hyopneumoniae. M. hyopneumoniae binds factor H via factor H binding proteins, such as elongation factor thermo unstable (EF-Tu), P146, pyruvate dehydrogenase (acetyl-transferring) E1 component subunit alpha (PdhA), P46, Pyruvate dehydrogenase E1 component subunit beta (PdhB), glyceraldehyde-3-phosphate dehydrogenase (GAPDH), and three different hypothetical proteins. The binding of factor H by EF-Tu further contributes to decreased C3 deposition on the M. hyopneumoniae surface and ultimately blocks further complement activation. In fact, binding of factor H occurs in a multifactorial manner; factor H is not only exploited by M. hyopneumoniae via its regulator activity to help mycoplasmas escape from complement killing, but also increases M. hyopneumoniae adhesion to swine tracheal epithelial cells, partially through EF-Tu. Meanwhile, the high sequence identity among EF-Tu proteins in the above-mentioned mycoplasmas implied the universality of the mechanism. This is the first report that mycoplasmas can escape complement killing by binding to factor H.
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影响因子：
4.8
作者：
Agarwal, Vaibhav;Asmat, Tauseef M.;Hammerschmidt, Sven
通讯作者：
Hammerschmidt, Sven
影响因子：
7.3
作者：
Langford-Smith A;Day AJ;Bishop PN;Clark SJ
通讯作者：
Clark SJ
DOI：
10.1111/j.1439-0442.1997.tb01111.x
发表时间：
1997-07-01
期刊：
JOURNAL OF VETERINARY MEDICINE SERIES A-PHYSIOLOGY PATHOLOGY CLINICAL MEDICINE
影响因子：
--
作者：
Buttenschon, J;Friis, NF;Mousing, J
通讯作者：
Mousing, J
影响因子：
4.4
作者：
Ferreira, Viviana P.;Herbert, Andrew P.;Pangburn, Michael K.
通讯作者：
Pangburn, Michael K.
影响因子：
2.6
作者：
Overesch, Gudrun;Kuhnert, Peter
通讯作者：
Kuhnert, Peter