A distinct sortase SrtB anchors and processes a streptococcal adhesin AbpA with a novel structural property.

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Title: A distinct sortase SrtB anchors and processes a streptococcal adhesin AbpA with a novel structural property.
Authors: Liang, X
Liu, B
Zhu, F
Scannapieco, FA
Haase, EM
Matthews, S
Wu, H
Item Type: Journal Article
Abstract: Surface display of proteins by sortases in Gram-positive bacteria is crucial for bacterial fitness and virulence. We found a unique gene locus encoding an amylase-binding adhesin AbpA and a sortase B in oral streptococci. AbpA possesses a new distinct C-terminal cell wall sorting signal. We demonstrated that this C-terminal motif is required for anchoring AbpA to cell wall. In vitro and in vivo studies revealed that SrtB has dual functions, anchoring AbpA to the cell wall and processing AbpA into a ladder profile. Solution structure of AbpA determined by NMR reveals a novel structure comprising a small globular α/β domain and an extended coiled-coil heliacal domain. Structural and biochemical studies identified key residues that are crucial for amylase binding. Taken together, our studies document a unique sortase/adhesion substrate system in streptococci adapted to the oral environment rich in salivary amylase.
Issue Date: 5-Aug-2016
Date of Acceptance: 6-Jul-2016
URI: http://hdl.handle.net/10044/1/39289
DOI: https://dx.doi.org/10.1038/srep30966
ISSN: 2045-2322
Publisher: Nature Publishing Group
Journal / Book Title: Scientific Reports
Volume: 6
Copyright Statement: This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ © The Author(s) 2016
Sponsor/Funder: Wellcome Trust
Funder's Grant Number: 100280/Z/12/Z
Publication Status: Published
Article Number: 30966
Appears in Collections:Faculty of Natural Sciences

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