Paul J. Hensbergen

This study identifies two novel biosynthetic intermediates and characterizes their enzymes in the unique glycan modification pathway of C. difficile flagellin.

This study identifies the unknown moiety in the b-type flagellin glycan of Pseudomonas aeruginosa PAO1 as N,N-dimethylthreonine using mass spectrometry and compares it to Type A glycan in C. difficile.

This study shows that HtrA proteolytic activity affects its expression level and is necessary for C. difficile survival under acidic conditions.

The paper characterizes the non-prime- and prime-side specificity of Pro-Pro endopeptidases using synthetic peptide libraries and mass spectrometry, identifying novel PPEPs and altered specificity in mutants.