Journal
PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY B-BIOLOGICAL SCIENCES
Volume 367, Issue 1592, Pages 1123-1139Publisher
ROYAL SOC
DOI: 10.1098/rstb.2011.0210
Keywords
type VII secretion; WXG protein; sortase; sorting signal; surface-layer homology domain; surface layer
Categories
Funding
- National Institutes of Allergy and Infectious Diseases, Infectious Diseases Branch [AI38897, AI52474, AI52767, AI69227]
- Region V 'Great Lakes' Regional Center of Excellence in Biodefense and Emerging Infectious Diseases Consortium (NIH) [1-U54-AI-057153]
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The cell wall peptidoglycan of Gram-positive bacteria functions as a surface organelle for the transport and assembly of proteins that interact with the environment, in particular, the tissues of an infected host. Signal peptide-bearing precursor proteins are secreted across the plasma membrane of Gram-positive bacteria. Some precursors carry C-terminal sorting signals with unique sequence motifs that are cleaved by sortase enzymes and linked to the cell wall peptidoglycan of vegetative forms or spores. The sorting signals of pilin precursors are cleaved by pilus-specific sortases, which generate covalent bonds between proteins leading to the assembly of fimbrial structures. Other precursors harbour surface (S)-layer homology domains (SLH), which fold into a three-pronged spindle structure and bind secondary cell wall polysaccharides, thereby associating with the surface of specific Gram-positive microbes. Type VII secretion is a non-canonical secretion pathway for WXG100 family proteins in mycobacteria. Gram-positive bacteria also secrete WXG100 proteins and carry unique genes that either contribute to discrete steps in secretion or represent distinctive substrates for protein transport reactions.
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