Type IX Secretion System Cargo Proteins Are Glycosylated at the C Terminus with a Novel Linking Sugar of the Wbp/Vim Pathway
Paul D Veith, Mikio Shoji, Richard AJ O'Hair, Michael G Leeming, Shuai Nie, Michelle D Glew, Gavin E Reid, Koji Nakayama, Eric C Reynolds
MBIO | AMER SOC MICROBIOLOGY | Published : 2020
Porphyromonas gingivalis and Tannerella forsythia use the type IX secretion system to secrete cargo proteins to the cell surface where they are anchored via glycolipids. In P. gingivalis, the glycolipid is anionic lipopolysaccharide (A-LPS), of partially known structure. Modified cargo proteins were deglycosylated using trifluoromethanesulfonic acid and digested with trypsin or proteinase K. The residual modifications were then extensively analyzed by tandem mass spectrometry. The C terminus of each cargo protein was amide-bonded to a linking sugar whose structure was deduced to be 2-N-seryl, 3-N-acetylglucuronamide in P. gingivalis and 2-N-glycyl, 3-N-acetylmannuronic acid in T. forsythia T..View full abstract
Related Projects (1)
Awarded by Australian National Health and Medical Research Council
Awarded by Australian Government Department of Industry, Innovation and Science
This work was supported by the Australian National Health and Medical Research Council (grant 1123866) and the Australian Government Department of Industry, Innovation and Science (grant 20080108).