Abstract
Pili of Gram-positive bacteria are unique structures on the bacterial surface, assembled from covalently linked polypeptide subunits. Pilus assembly proceeds by transpeptidation reactions catalyzed by sortases, followed by covalent anchoring of the filament in the peptidoglycan layer. Another distinctive property is the presence of intramolecular isopeptide bonds, conferring extraordinary chemical and mechanical stability to these elongated structures. Besides their function in cell adhesion and biofilm formation, this section discusses possible application of pilus constituents as vaccine components against Gram-positive pathogens.
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Abbreviations
- BP:
-
Backbone protein
- AP:
-
Ancillary protein
- CWSS:
-
Cell wall sorting signal
- m-Dap:
-
Meso-2,6-diaminopimelic acid
- GAS:
-
Group A streptococcus (S. pyogenes)
- GBS:
-
Group B streptococcus (S. agalactiae)
- MIDAS:
-
Metal ion-dependent adhesion site
- MSCRAMMs:
-
Microbial surface components recognizing adhesive matrix molecules
- PI:
-
Pilus islet
- vWFA:
-
von Willebrand factor type A domain
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The authors are grateful to Markus Hilleringmann for critical reading of the manuscript and numerous highly appreciated suggestions.
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Pansegrau, W., Bagnoli, F. (2015). Pilus Assembly in Gram-Positive Bacteria. In: Bagnoli, F., Rappuoli, R. (eds) Protein and Sugar Export and Assembly in Gram-positive Bacteria . Current Topics in Microbiology and Immunology, vol 404. Springer, Cham. https://doi.org/10.1007/82_2015_5016
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