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Mol Microbiol:揭秘耐药菌毒力因子的特殊结构单元或可开发新型抗生素

来源:生物谷 2015-05-11 13:48

2015年5月11日 讯 /生物谷BIOON/ --近日,一项发表于国际杂志Molecular Microbiology上的研究论文中,来自阿德莱德大学的科学家通过研究发现了一种新型靶点,该靶点或为开发抵御引发疾病细菌的新型抗生素提供一定的帮助;文章中研究者鉴别出了对许多细菌毒力因子较为常见的结构单元,细菌的毒力因子是一种可以引发疾病的特殊蛋白质,比如毒素类或降解酶。

这种结构单元名为“旅客”相关的运输重复结构(PATR,Passenger-associated Transport Repeat),这种结构是在许多有害细菌的毒力因子中发现的,比如沙门氏菌、志贺氏菌、脑膜炎球菌以及一些引发囊性纤维化的细菌;而且这种结构在很多革兰氏阴性菌中都存在,其中就包括一些对很多抗生素产生耐药性的细菌。

PATR在细菌毒力因子运输至细胞表面的过程可以表现出较为完整的结构以便其作为致病因子发挥作用;研究者Matthew Doyle说道,当细菌毒力因子被适当产生并且被分泌到细胞表面时其就会引发疾病,我们的研究非常激动人心,我们不仅发现了存在于特殊病原体中的关键毒力分子,而且还发现了许多致病菌毒力常见毒力因子所共有的毒力结构单元,这就为后期开发广谱抑制细菌毒力的抑制剂提供了一定的帮助。

本文研究也可以用于生物技术领域来进行市场化产品的开发,研究者表示,这种毒力因子的特殊结构单元通常都会被忽略,而其对于后期进行耐药性细菌疗法的开发或许会带来巨大的帮助。(生物谷Bioon.com)

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The passenger-associated transport repeat promotes virulence factor secretion efficiency and delineates a distinct autotransporter subtype

Matthew Thomas Doyle, Elizabeth Ngoc Hoa Tran andRenato Morona*

Autotransporters are a superfamily of virulence factors secreted by Gram negative bacteria. They are comprised of an N-terminal passenger domain that is translocated across the outer membrane, and a C-terminal domain that inserts into the outer membrane forming a β-barrel anchor. It is still poorly understood how the passenger is efficiently translocated in the absence of external energy inputs. Several mechanisms have been proposed in solution of this problem, yet due to the vast diversity of size, sequence, and function of the passenger, it is not clear how widely these mechanisms are employed. In this study we functionally characterize a conserved repeat found in many passengers which we designate the Passenger-associated Transport Repeat (PATR). Using the autotransporter IcsA from the enteropathogen Shigella flexneri, we identified conserved PATR residues that are required for efficient export of the passenger during growth and infection. Furthermore, PATR-containing autotransporters are significantly larger than non-PATR autotransporters, with PATR copy number correlating with passenger size. We also show that PATR-containing autotransporters delineate a subgroup that associates with specific virulence traits and architectures. These results advance our understanding of autotransporter composition, and indicate that an additional transport mechanism is important for thousands of these proteins.

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