Show simple item record

The Haemophilus influenzae HMW1C protein is a glycosyltransferase that transfers hexose residues to asparagine sites in the HMW1 adhesin.

dc.contributor.author Geme, JWS III
dc.contributor.author Grass, S
dc.contributor.author Gross, Julia
dc.contributor.author Lichti, CF
dc.contributor.author Townsend, RR
dc.date.accessioned 2011-06-21T17:32:23Z
dc.date.issued 2010
dc.identifier.issn 1553-7374
dc.identifier.uri https://hdl.handle.net/10161/4601
dc.description.abstract The Haemophilus influenzae HMW1 adhesin is a high-molecular weight protein that is secreted by the bacterial two-partner secretion pathway and mediates adherence to respiratory epithelium, an essential early step in the pathogenesis of H. influenzae disease. In recent work, we discovered that HMW1 is a glycoprotein and undergoes N-linked glycosylation at multiple asparagine residues with simple hexose units rather than N-acetylated hexose units, revealing an unusual N-glycosidic linkage and suggesting a new glycosyltransferase activity. Glycosylation protects HMW1 against premature degradation during the process of secretion and facilitates HMW1 tethering to the bacterial surface, a prerequisite for HMW1-mediated adherence. In the current study, we establish that the enzyme responsible for glycosylation of HMW1 is a protein called HMW1C, which is encoded by the hmw1 gene cluster and shares homology with a group of bacterial proteins that are generally associated with two-partner secretion systems. In addition, we demonstrate that HMW1C is capable of transferring glucose and galactose to HMW1 and is also able to generate hexose-hexose bonds. Our results define a new family of bacterial glycosyltransferases.
dc.language.iso en_US
dc.relation.ispartof PLoS pathogens
dc.relation.isversionof 10.1371/journal.ppat.1000919
dc.title The Haemophilus influenzae HMW1C protein is a glycosyltransferase that transfers hexose residues to asparagine sites in the HMW1 adhesin.
dc.title.alternative
dc.type Journal article
dc.description.version Version of Record
duke.date.pubdate 2010-5-0
duke.description.issue 5
duke.description.volume 6
dc.relation.journal Plos Pathogens
pubs.begin-page e1000919
pubs.issue 5
pubs.organisational-group Duke
pubs.organisational-group Faculty
pubs.volume 6


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record