Sticky and Sweet: The Role of Post-Translational Modifications on Neisserial Pili

Charlene M Kahler

doi:10.3389/fmicb.2011.00087

Abstract

Sticky and Sweet: The Role of Post-Translational Modifications on Neisserial Pili

Highlights

Is Tfp required for the initial attachment events to the host cell surface, it is involved in twitching motility (Merz et al, 2000)
PilE is expressed as a prepilin which undergoes processing by a prepilin peptidase, PilD, during export into the periplasm where subunits are arranged in a helix for extrusion through PilQ to form the shaft of the pilus
The addition of PC and PE to PilE is catalyzed by the pilin phosphoethanolamine transferase (PptA; Aas et al, 2006) which can add up to five residues to serine 68 and serine 156 of PilE from N. gonorrhoeae strain MS11 (Aas et al, 2006)

Summary

Introduction

Is Tfp required for the initial attachment events to the host cell surface, it is involved in twitching motility (Merz et al, 2000). Recent work has shown that post-translational modifications to the pilin subunit, PilE, are the major contributors to the formation and disaggregation of bundled pili. Both PilE structures are glycosylated with different glycans at serine 63 and these attachments may influence the availability of serine 68/69 to PptB.

Results

Conclusion