Multi-Functional Characteristics of the Pseudomonas aeruginosa Type III Needle-Tip Protein, PcrV; Comparison to Orthologs in other Gram-negative Bacteria.

Multi-Functional Characteristics of the Pseudomonas aeruginosa Type III Needle-Tip Protein, PcrV; Comparison to Orthologs in other Gram-negative Bacteria.
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DOI:
10.3389/fmicb.2011.00142
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发表时间:
2011
影响因子:
5.2
通讯作者:
Frank DW
Frank DW
中科院分区:
生物学2区
文献类型:
--
作者:
Sato H;Frank DW

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铜绿假单胞菌具有III型分泌系统(T3SS),以使宿主细胞中毒并逃避先天性免疫。这种与毒力相关的机制由组装在细菌表面的分子注射器和针头组成,它允许将T3效应蛋白递送到受感染的细胞中。为了完成一步效应子易位,在T3针结构的顶端需要尖端蛋白。缺乏功能性顶端蛋白表达的菌株不能使宿主细胞中毒。铜绿假单胞菌编码与耶尔森氏菌属编码的蛋白高度同源的T3S。耶尔森氏菌LcrV和铜绿假单胞菌PcrV的针尖蛋白具有37%的同一性和65%的相似性。其它已知的尖端蛋白是AcrV(气单胞菌属)、iPad(志贺氏菌属)、SipD(沙门氏菌属)、BipD(伯克霍尔德氏菌属)、EspA(EPEC、EHEC)、Bsp 22(博德特氏菌属),以及从各种革兰氏阴性物种如弧菌属和博德特氏菌属鉴定的其它蛋白。尖端蛋白可以作为保护性抗原,或者对于感知宿主细胞和逃避先天免疫应答可能是至关重要的。宿主微环境的识别转录激活T3SS组分的合成。这一机制似乎是由该装置内特定连接点的组合来机械控制的。这些连接包括T3装置的尖端和基部、针蛋白和细菌细胞质内的组分。尖端蛋白可能具有转运子蛋白的伴侣蛋白功能,允许宿主膜中的转运通道的正确组装并完成效应蛋白向宿主细胞质中的载体递送。针尖蛋白质的多功能特征似乎受到复杂的控制。在这篇综述中,我们强调T3针尖蛋白的功能方面和复杂的控制,特别强调PcrV和LcrV。
Pseudomonas aeruginosa possesses a type III secretion system (T3SS) to intoxicate host cells and evade innate immunity. This virulence-related machinery consists of a molecular syringe and needle assembled on the bacterial surface, which allows delivery of T3 effector proteins into infected cells. To accomplish a one-step effector translocation, a tip protein is required at the top end of the T3 needle structure. Strains lacking expression of the functional tip protein fail to intoxicate host cells. P. aeruginosa encodes a T3S that is highly homologous to the proteins encoded by Yersinia spp. The needle-tip proteins of Yersinia, LcrV, and P. aeruginosa, PcrV, share 37% identity and 65% similarity. Other known tip proteins are AcrV (Aeromonas), IpaD (Shigella), SipD (Salmonella), BipD (Burkholderia), EspA (EPEC, EHEC), Bsp22 (Bordetella), with additional proteins identified from various Gram-negative species, such as Vibrio and Bordetella. The tip proteins can serve as a protective antigen or may be critical for sensing host cells and evading innate immune responses. Recognition of the host microenvironment transcriptionally activates synthesis of T3SS components. The machinery appears to be mechanically controlled by the assemblage of specific junctions within the apparatus. These junctions include the tip and base of the T3 apparatus, the needle proteins and components within the bacterial cytoplasm. The tip proteins likely have chaperone functions for translocon proteins, allowing the proper assembly of translocation channels in the host membrane and completing vectorial delivery of effector proteins into the host cytoplasm. Multi-functional features of the needle-tip proteins appear to be intricately controlled. In this review, we highlight the functional aspects and complex controls of T3 needle-tip proteins with particular emphasis on PcrV and LcrV.
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