Journal: Cell host & microbe
Article Title: The Legionella pneumophila EnhC protein interferes with immunestimulatory muramyl peptide production to evade innate immunity
Figure Lengend Snippet: Transglycosylation of L. pneumophila peptidoglycan (PG) by SltL (A) Slt cleaves the β-1,4-glycosidic bond between MurNAc and GlcNAc in the glycan strand and generates an intramolecular 1,6-anhydro linkage between the C1 and C6 positions in the sugar ring of MurNAc, releasing GlcNAc-1,6-anhydro-MurNAc-tetrapeptide (MW = 921Da). (B) Identification of a product generated by SltL incubation with PG. L. pneumophila PG was incubated with SltL and subjected to HPLC (black line). The elution time of purified GlcNAc-1,6-anhydro-MurNAc-tetrapeptide (anhDSTP) is indicated by the asterisk and overlaps with the SltL product (inserted image). (C) Peak in 2(B) was subjected to MALDI-TOF mass spectrometry. Four forms of modified anhDSTP were identified.
Article Snippet: The main fraction was collected, lyophilized, and identified by MS with a Voyager DE Pro matrix-assisted laser desorption ionization—time-of-flight (MALDI-TOF) mass spectrometer (Applied Biosystems) at Tufts University Core Facility.
Techniques: Generated, Incubation, High Performance Liquid Chromatography, Purification, Mass Spectrometry, Modification