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

Xiaobo Liang, Bing Liu, Fan Zhu, Frank A. Scannapieco, Elaine M. Haase, Steve Matthews, Hui Wu

Research output: Contribution to journalArticlepeer-review

13 Scopus citations

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.

Original languageEnglish (US)
Article number30966
JournalScientific Reports
Volume6
DOIs
StatePublished - Aug 5 2016
Externally publishedYes

ASJC Scopus subject areas

  • General

Fingerprint

Dive into the research topics of 'A distinct sortase SrtB anchors and processes a streptococcal adhesin AbpA with a novel structural property'. Together they form a unique fingerprint.

Cite this