A Distinct Type of Pilus from the Human Microbiome

Overview

Journal Cell

Publisher Cell Press

Specialty Cell Biology

Date 2016 Apr 12

PMID 27062925

Citations 53

Authors

Qingping Xu

Mikio Shoji

Satoshi Shibata

Mariko Naito

Keiko Sato

Marc-Andre Elsliger

Joanna C Grant

Herbert L Axelrod

Hsiu-Ju Chiu

Carol L Farr

Lukasz Jaroszewski

Mark W Knuth

Ashley M Deacon

Adam Godzik

Scott A Lesley

Michael A Curtis

Koji Nakayama

Ian A Wilson

Affiliations

Soon will be listed here.

Abstract

Pili are proteinaceous polymers of linked pilins that protrude from the cell surface of many bacteria and often mediate adherence and virulence. We investigated a set of 20 Bacteroidia pilins from the human microbiome whose structures and mechanism of assembly were unknown. Crystal structures and biochemical data revealed a diverse protein superfamily with a common Greek-key β sandwich fold with two transthyretin-like repeats that polymerize into a pilus through a strand-exchange mechanism. The assembly mechanism of the central, structural pilins involves proteinase-assisted removal of their N-terminal β strand, creating an extended hydrophobic groove that binds the C-terminal donor strands of the incoming pilin. Accessory pilins at the tip and base have unique structural features specific to their location, allowing initiation or termination of the assembly. The Bacteroidia pilus, therefore, has a biogenesis mechanism that is distinct from other known pili and likely represents a different type of bacterial pilus.

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