Pilins in gram‐positive bacteria: A structural perspective

Abstract Pilins or fimbrilins are a class of proteins found in bacterial surface pilus, a hair‐like surface appendage. Both the Gram‐negative and ‐positive bacteria produce pilins to assemble pili on their cell‐surface for different purposes including adherence, twitching motility, conjugation, immunomodulation, biofilm formation, and electron transfer. Immunogenic properties of the pilins make them attractive vaccine candidates. The polymerized pilins play a key role in the initiation of host adhesion, which is a critical step for bacterial colonization and infection. Because of their key role in adhesion and exposure on the cell surface, targeting the pilins‐mediated adhesion (anti‐adhesion therapy) is also seen as a promising alternative approach for preventing and treating bacterial infections, one that may overcome their ever‐increasing repertoires of resistance mechanisms. Individual pilins interact with each other non‐covalently to assemble the pilus fiber with the help of associated proteins like chaperones and Usher in Gram‐negative bacteria. In contrast, the pilins in Gram‐positive bacteria often connect with each other covalently, with the help of sortases. Certain unique structural features present on the pilins distinguish them from one another across different bacterial strains, and these dictate their cellular targets and functions. While the structure of pilins has been extensively studied in Gram‐negative pathogenic bacteria, the pilins in Gram‐positive pathogenic bacteria have been in only during the last decade. Recently, the discovery of pilins in non‐pathogenic bacteria, such as Lactobacillus rhamnosus GG, has received great attention, though traditionally the attention was on pathogenic bacteria. This review summarizes and discusses the current structural knowledge of pilins in Gram‐positive bacteria with emphasis on those pilins which are sortase substrates. © 2015 IUBMB Life, 67(7):533–543, 2015