Human defensins facilitate local unfolding of thermodynamically unstable regions of bacterial protein toxins.
Human defensins facilitate local unfolding of thermodynamically unstable regions of bacterial protein toxins.
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DOI：
10.1016/j.immuni.2014.10.018
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发表时间：
2014-11-20
期刊：
影响因子：
32.4
通讯作者：
Kudryashov, Dmitri S.
中科院分区：
文献类型：
--
作者：
Kudryashova, Elena;Quintyn, Royston;Seveau, Stephanie;Lu, Wuyuan;Wysocki, Vicki H.;Kudryashov, Dmitri S.
Defensins are short cationic, amphiphilic, cysteine-rich peptides that constitute the front line immune defense against various pathogens. In addition to exerting direct antibacterial activities, defensins inactivate several classes of unrelated bacterial exotoxins. To date, no coherent mechanism has been proposed that would explain defensins’ enigmatic efficiency towards various toxins. We showed that binding of neutrophil α-defensin HNP1 to affected bacterial toxins caused their local unfolding, potentiated their thermal melting and precipitation, exposed new regions for proteolysis, and increased susceptibility to collisional quenchers, without causing similar affects on tested mammalian structural and enzymatic proteins. Enteric α-defensin HD5 and β-defensin hBD2 shared similar toxin-unfolding effects with HNP1, albeit to different degrees. We propose that protein susceptibility to inactivation by defensins is contingent to their thermolability and conformational plasticity and that the defensin-induced unfolding is a key element in the general mechanism of toxin inactivation by human defensins.
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影响因子：
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作者：
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DOI：
10.1083/jcb.200201081
发表时间：
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期刊：
The Journal of cell biology
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DOI：
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发表时间：
2005-03-29
影响因子：
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作者：
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通讯作者：
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