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dc.contributor.author Grass, Susan
dc.contributor.author Lichti, CF
dc.contributor.author Townsend, RR
dc.contributor.author Gross, J
dc.contributor.author St. Geme, Joseph William III
dc.date.accessioned 2011-06-21T17:32:23Z
dc.date.issued 2010
dc.identifier.citation PLoS pathogens, 2010, 6 (5), pp. e1000919 - ?
dc.identifier.issn 1553-7374
dc.identifier.uri http://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.format.extent e1000919 - ?
dc.language.iso en_US 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 en_US
dc.type Journal Article
dc.description.version Version of Record en_US
duke.date.pubdate 2010-5-0 en_US
duke.description.endpage e1000919 en_US
duke.description.issue 5 en_US
duke.description.startpage e1000919 en_US
duke.description.volume 6 en_US
dc.relation.journal Plos Pathogens en_US
pubs.issue 5
pubs.organisational-group /Duke
pubs.organisational-group /Duke/School of Medicine
pubs.organisational-group /Duke/School of Medicine/Basic Science Departments
pubs.organisational-group /Duke/School of Medicine/Basic Science Departments/Molecular Genetics and Microbiology
pubs.organisational-group /Duke/School of Medicine/Clinical Science Departments
pubs.organisational-group /Duke/School of Medicine/Clinical Science Departments/Pediatrics
pubs.volume 6

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