In this section
@article{Liang:2016:10.1038/srep30966,
author = {Liang, X and Liu, B and Zhu, F and Scannapieco, FA and Haase, EM and Matthews, S and Wu, H},
doi = {10.1038/srep30966},
journal = {Scientific Reports},
title = {A distinct sortase SrtB anchors and processes a streptococcal adhesin AbpA with a novel structural property.},
url = {http://dx.doi.org/10.1038/srep30966},
volume = {6},
year = {2016}
}
TY - JOUR
AB - 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.
AU - Liang,X
AU - Liu,B
AU - Zhu,F
AU - Scannapieco,FA
AU - Haase,EM
AU - Matthews,S
AU - Wu,H
DO - 10.1038/srep30966
PY - 2016///
SN - 2045-2322
TI - A distinct sortase SrtB anchors and processes a streptococcal adhesin AbpA with a novel structural property.
T2 - Scientific Reports
UR - http://dx.doi.org/10.1038/srep30966
UR - http://hdl.handle.net/10044/1/39289
VL - 6
ER -
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