Abstract
Secretion of proteins by the general secretory pathway (GSP) is a two-step process requiring the Sec translocase in the inner membrane and a separate substrate-specific secretion apparatus for translocation across the outer membrane. Gram-negative bacteria with pathogenic potential use the GSP to deliver virulence factors into the extracellular environment for interaction with the host. Well-studied examples of virulence determinants using the GSP for secretion include extracellular toxins, pili, curli, autotransporters, and crystaline S-layers. This article reviews our current understanding of the GSP and discusses examples of terminal branches of the GSP which are utilized by factors implicated in bacterial virulence.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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Adenosine Triphosphatases / metabolism
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Bacterial Outer Membrane Proteins / metabolism*
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Bacterial Proteins*
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Bacterial Toxins / metabolism
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Biological Transport
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Carrier Proteins / metabolism
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Escherichia coli Proteins*
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Fimbriae, Bacterial / metabolism
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Glycoside Hydrolases / metabolism
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Gram-Negative Bacteria / metabolism*
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Gram-Negative Bacteria / pathogenicity
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Membrane Transport Proteins*
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Molecular Chaperones / metabolism
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SEC Translocation Channels
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SecA Proteins
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Structure-Activity Relationship
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Virulence
Substances
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Bacterial Outer Membrane Proteins
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Bacterial Proteins
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Bacterial Toxins
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Carrier Proteins
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Escherichia coli Proteins
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Membrane Transport Proteins
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Molecular Chaperones
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SEC Translocation Channels
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Glycoside Hydrolases
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pullulanase
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Adenosine Triphosphatases
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SecA Proteins