Structural characterization of the carbohydrate-binding module of NanA sialidase, a pneumococcal virulence factor.

ABSTRACT:

Background

Streptococcus pneumoniae Neuraminidase A (NanA) is a multi-domain protein anchored to the bacterial surface. Upstream of the catalytic domain of NanA is a domain that conforms to the sialic acid-recognising CBM40 family of the CAZY (carbohydrate-active enzymes) database. This domain has been identified to play a critical role in allowing the bacterium to promote adhesion and invasion of human brain microvascular endothelial cells, and hence may play a key role in promoting bacterial meningitis. In addition, the CBM40 domain has also been reported to activate host chemokines and neutrophil recruitment during infection.

Results

Crystal structures of both apo- and holo- forms of the NanA CBM40 domain (residues 121 to 305), have been determined to 1.8 Å resolution. Th

SUBMITTER: Yang L 

PROVIDER: S-EPMC4546082 | biostudies-literature | 2015 Aug

REPOSITORIES: biostudies-literature