小柯机器人

芬兰图尔库大学Anton V. Zavialov研究小组揭示古老纤毛组装的结构基础。这一研究成果于2022年7月19日在线发表在国际学术期刊《自然》上。

Author: Pakharukova, Natalia, Malmi, Henri, Tuittila, Minna, Dahlberg, Tobias, Ghosal, Debnath, Chang, Yi-Wei, Myint, Si Lhyam, Paavilainen, Sari, Knight, Stefan David, Lamminmki, Urpo, Uhlin, Bernt Eric, Andersson, Magnus, Jensen, Grant, Zavialov, Anton V.

Issue&Volume: 2022-07-19

Abstract: Adhesive pili assembled via the chaperone-usher pathway (CUP) are hair-like appendages that mediate host tissue colonization and biofilm formation of Gram-negative bacteria 1-3. Archaic CUP pili, the most diverse and widespread CUP adhesins, are promising vaccine and drug targets due to their prevalence in the most troublesome multidrug-resistant (MDR) pathogens 1,4,5. However, their architecture and assembly-secretion process remain unknown. Here, we present the 3.4 resolution cryo-electron microscopy structure of the prototypical archaic Csu pilus that mediates biofilm formation of Acinetobacter baumannii, a notorious MDR nosocomial pathogen. In contrast to the thick helical tubes of the classical type 1 and P pili, archaic pili assemble into a conceptually novel ultrathin zigzag architecture secured by an elegant clinch mechanism. The molecular clinch provides the pilus with high mechanical stability as well as superelasticity, a property observed now for the first time in biomolecules, while enabling a more economical and faster pilus production. Furthermore, we demonstrate that clinch formation at the cell surface drives pilus secretion through the outer membrane. These findings suggest that clinch-formation inhibitors might represent a new strategy to fight MDR bacterial infections.

DOI: 10.1038/s41586-022-05095-0

Source: https://www.nature.com/articles/s41586-022-05095-0

Nature：《自然》，创刊于1869年。隶属于施普林格·自然出版集团，最新IF：69.504
官方网址：http://www.nature.com/
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