Logo image
Identification of a Pneumococcal Glycosidase That Modifies O-Linked Glycans
Journal article   Open access   Peer reviewed

Identification of a Pneumococcal Glycosidase That Modifies O-Linked Glycans

Carolyn Marion, Dominique H Limoli, Gregory S Bobulsky, Jessica L Abraham, Amanda M Burnaugh and Samantha J King
Infection and immunity, Vol.77(4), pp.1389-1396
04/2009
DOI: 10.1128/IAI.01215-08
PMCID: PMC2663135
PMID: 19139197
url
https://doi.org/10.1128/IAI.01215-08View
Published (Version of record) Open Access

Abstract

Colonization of the airway by Streptococcus pneumoniae is typically asymptomatic; however, progression of bacteria beyond the oronasopharynx can cause diseases including otitis media and pneumonia. The mechanisms by which S. pneumoniae establishes and maintains colonization remain poorly understood. Both N-linked and O-linked glycans are abundant in the airway. Our previous research demonstrated that S. pneumoniae can sequentially deglycosylate N-linked glycans and suggested that this modification of sugar structures may aid in colonization. There is published evidence that S. pneumoniae expresses a secreted O-glycosidase that cleaves galactose β1-3 N -acetylgalactosamine (Galβ1-3GalNAc) from core-1 O-linked glycans; however, the biological function of this enzyme has not previously been determined. We established that the activity is not secreted but is instead surface associated in a sortase-dependent manner. Genome analysis revealed an open reading frame predicted to encode a sortase-dependent surface protein with sequence similarity to the O-glycosidase of Bifidobacterium longum . Deletion of this pneumococcal open reading frame confirmed that this gene encodes an O-glycosidase. Experiments using a model glycoconjugate demonstrated that this O-glycosidase, together with the neuraminidase NanA, is required for S. pneumoniae to cleave sialylated core-1 O-linked glycans. The ability of the O-glycosidase mutant to cleave this glycan structure was restored by both genetic complementation and the addition of O-glycosidase. The mutant showed a reduction in adherence to human airway epithelial cells and a significantly decreased ability to colonize the upper respiratory tract, suggesting that cleavage of core-1 O-linked glycans enhances the ability of S. pneumoniae to colonize the human airway.
Molecular Pathogenesis

Details

Metrics

Logo image