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- Title
A cinetobacter strains carry two functional oligosaccharyltransferases, one devoted exclusively to type IV pilin, and the other one dedicated to O-glycosylation of multiple proteins.
- Authors
Harding, Christian M.; Nasr, Mohamed A.; Kinsella, Rachel L.; Scott, Nichollas E.; Foster, Leonard J.; Weber, Brent S.; Fiester, Steve E.; Actis, Luis A.; Tracy, Erin N.; Munson, Robert S.; Feldman, Mario F.
- Abstract
Multiple species within the A cinetobacter genus are nosocomial opportunistic pathogens of increasing relevance worldwide. Among the virulence factors utilized by these bacteria are the type IV pili and a protein O-glycosylation system. Glycosylation is mediated by O-oligosaccharyltransferases ( O-OTases), enzymes that transfer the glycan from a lipid carrier to target proteins. O-oligosaccharyltransferases are difficult to identify due to similarities with the WaaL ligases that catalyze the last step in lipopolysaccharide synthesis. A bioinformatics analysis revealed the presence of two genes encoding putative O- OTases or WaaL ligases in most of the strains within the genus A cinetobacter. Employing A . nosocomialis M2 and A . baylyi ADP1 as model systems, we show that these genes encode two O- OTases, one devoted uniquely to type IV pilin, and the other one responsible for glycosylation of multiple proteins. With the exception of ADP1, the pilin-specific OTases in Acinetobacter resemble the TfpO/PilO O-OTase from P seudomonas aeruginosa. In ADP1 instead, the two O-OTases are closely related to PglL, the general O-OTase first discovered in N eisseria. However, one of them is exclusively dedicated to the glycosylation of the pilin-like protein ComP. Our data reveal an intricate and remarkable evolutionary pathway for bacterial O-OTases and provide novel tools for glycoengineering.
- Subjects
OLIGOSACCHARYLTRANSFERASE; PILIN (Bacterial proteins); GLYCOSYLATION; GLYCANS; ACINETOBACTER; BACTERIAL enzymes
- Publication
Molecular Microbiology, 2015, Vol 96, Issue 5, p1023
- ISSN
0950-382X
- Publication type
Article
- DOI
10.1111/mmi.12986