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Bacterial serine proteases secreted by the autotransporter pathway: classification, specificity, and role in virulence.

Authors
  • Ruiz-Perez, Fernando1
  • Nataro, James P
  • 1 Department of Pediatrics, School of Medicine, University of Virginia, P.O.Box 800326, MR4 Room 4012C, 409 Lane Road, Charlottesville, VA, 22908, USA, [email protected]
Type
Published Article
Journal
Cellular and Molecular Life Sciences
Publisher
Springer-Verlag
Publication Date
Mar 01, 2014
Volume
71
Issue
5
Pages
745–770
Identifiers
DOI: 10.1007/s00018-013-1355-8
PMID: 23689588
Source
Medline
License
Unknown

Abstract

Serine proteases exist in eukaryotic and prokaryotic organisms and have emerged during evolution as the most abundant and functionally diverse group. In Gram-negative bacteria, there is a growing family of high molecular weight serine proteases secreted to the external milieu by a fascinating and widely employed bacterial secretion mechanism, known as the autotransporter pathway. They were initially found in Neisseria, Shigella, and pathogenic Escherichia coli, but have now also been identified in Citrobacter rodentium, Salmonella, and Edwardsiella species. Here, we focus on proteins belonging to the serine protease autotransporter of Enterobacteriaceae (SPATEs) family. Recent findings regarding the predilection of serine proteases to host intracellular or extracellular protein-substrates involved in numerous biological functions, such as those implicated in cytoskeleton stability, autophagy or innate and adaptive immunity, have helped provide a better understanding of SPATEs' contributions in pathogenesis. Here, we discuss their classification, substrate specificity, and potential roles in pathogenesis.

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