Polyproline and triple helix motifs in host-pathogen recognition.

Polyproline and triple helix motifs in host-pathogen recognition.
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DOI:
10.2174/138920312804871157
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发表时间:
2012-12
影响因子:
2.8
通讯作者:
Vitagliano L
Vitagliano L
中科院分区:
生物学3区
文献类型:
--
作者:
Berisio R;Vitagliano L

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二级结构元件通常介导蛋白质之间的相互作用。尽管它们在折叠蛋白质中的丰度很低,但聚脯氨酸II (PPII)及其变体三螺旋结构经常参与蛋白质-蛋白质相互作用,这可能是由于它们特有的溶剂暴露倾向。我们在这里回顾了PPII和三螺旋在介导宿主-病原体相互作用中的作用,特别强调了这些过程的结构方面。在简要描述了这些元件的基本结构特征之后,还举例说明了涉及这些基序的宿主-病原体相互作用。文献资料表明,PPII基序在这些过程中发挥的作用是双重的。事实上,PPII区域可能直接介导宿主和病原体蛋白质之间的相互作用。或者,PPII可以作为结构间隔剂,用于粘附和感染性所需元件的正确定位。最近的研究表明,胶原蛋白三螺旋也是细菌粘附素的共同目标。虽然粘连素和胶原模型之间复合物的结构数据相当有限,但实验和理论研究已经揭示了一些有趣的识别过程线索。有趣的是,最近的数据表明,三螺旋结构不仅被病原体用作宿主-病原体相互作用的靶标,而且在这些过程中也可能充当诱饵,因为含有三螺旋区域的细菌蛋白质已被证明与宿主蛋白质相互作用。由于PPII和三螺旋都暴露了几个主链不满足的氢键受体和供体,这两个元素都是高度溶剂化的。在蛋白质-蛋白质相互作用中,PPII和三螺旋的溶剂化状态的保存是一个新兴的方面,将在这里进行彻底的讨论。
Secondary structure elements often mediate protein-protein interactions. Despite their low abundance in folded proteins, polyproline II (PPII) and its variant, the triple helix, are frequently involved in protein-protein interactions, likely due to their peculiar propensity to be solvent-exposed. We here review the role of PPII and triple helix in mediating host-pathogen interactions, with a particular emphasis to the structural aspects of these processes. After a brief description of the basic structural features of these elements, examples of host-pathogen interactions involving these motifs are illustrated. Literature data suggest that the role played by PPII motif in these processes is twofold. Indeed, PPII regions may directly mediate interactions between proteins of the host and the pathogen. Alternatively, PPII may act as structural spacers needed for the correct positioning of the elements needed for adhesion and infectivity. Recent investigations have highlighted that collagen triple helix is also a common target for bacterial adhesins. Although structural data on complexes between adhesins and collagen models are rather limited, experimental and theoretical studies have unveiled some interesting clues of the recognition process. Interestingly, very recent data show that not only is the triple helix used by pathogens as a target in the host-pathogen interaction but it may also act as a bait in these processes since bacterial proteins containing triple helix regions have been shown to interact with host proteins. As both PPII and triple helix expose several main chain non-satisfied hydrogen bond acceptors and donors, both elements are highly solvated. The preservation of the solvation state of both PPII and triple helix upon protein-protein interaction is an emerging aspect that will be here thoroughly discussed.
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