In:
Journal of Bacteriology, American Society for Microbiology, Vol. 193, No. 19 ( 2011-10), p. 5487-5497
Kurzfassung:
Findings from a number of studies suggest that the PilA pilin proteins may play an important role in the pathogenesis of disease caused by species within the genus Francisella . As such, a thorough understanding of PilA structure and chemistry is warranted. Here, we definitively identified the PglA protein-targeting oligosaccharyltransferase by virtue of its necessity for PilA glycosylation in Francisella tularensis and its sufficiency for PilA glycosylation in Escherichia coli . In addition, we used mass spectrometry to examine PilA affinity purified from Francisella tularensis subsp. tularensis and F. tularensis subsp. holarctica and demonstrated that the protein undergoes multisite, O -linked glycosylation with a pentasaccharide of the structure HexNac-Hex-Hex-HexNac-HexNac. Further analyses revealed microheterogeneity related to forms of the pentasaccharide carrying unusual moieties linked to the distal sugar via a phosphate bridge. Type A and type B strains of Francisella subspecies thus express an O -linked protein glycosylation system utilizing core biosynthetic and assembly pathways conserved in other members of the proteobacteria. As PglA appears to be highly conserved in Francisella species, O -linked protein glycosylation may be a feature common to members of this genus.
Materialart:
Online-Ressource
ISSN:
0021-9193
,
1098-5530
Sprache:
Englisch
Verlag:
American Society for Microbiology
Publikationsdatum:
2011
ZDB Id:
1481988-0
SSG:
12
