Article

 

Proteins Secreted via the Type II Secretion System: Smart Strategies of Vibrio cholerae to Maintain Fitness in Different Ecological Niches Public Deposited

Downloadable Content

Download PDF
https://ir.library.oregonstate.edu/concern/articles/h128nf53w

Descriptions

Attribute NameValues
Creator
Abstract
  • Many Gram-negative bacteria use the type II secretion (T2S) pathway to deliver proteins that contribute to disease in humans, animals, and plants. Vibrio cholerae, the causative agent of the life-threatening diarrheal disease cholera, utilizes the T2S system for translocation of at least 19 proteins, including the large hexameric protein cholera toxin (Table S1). The release of cholera toxin is predominantly responsible for the voluminous diarrhea in afflicted patients. The T2S machinery consists of 12 Eps (extracellular protein secretion) proteins and prepilin peptidase PilD. The secretion of the T2S substrates (exoproteins, cargo proteins) is a two-step process including their translocation via the inner membrane by the Sec or Tat pathway and subsequent transport of folded and/or oligomeric cargo proteins by the T2S into the extracellular milieu. The structure and function of the individual constituents of the T2S machinery in V. cholerae have been addressed in many elegant studies and recently reviewed. This review focuses rather on the T2S substrates, highlighting their importance in V. cholerae pathophysiology, functional interactions, and mechanisms regulating their expression.
License
Resource Type
DOI
Date Available
Date Issued
Citation
  • Sikora, A. E. (2013). Proteins secreted via the type II secretion system: Smart strategies of vibrio cholerae to maintain fitness in different ecological niches. PLoS Pathogens, 9(2), e1003126. doi:10.1371/journal.ppat.1003126
Journal Title
Journal Volume
  • 9
Journal Issue/Number
  • 2
Academic Affiliation
Rights Statement
Funding Statement (additional comments about funding)
  • The work was supported by the start-up funds provided to A.E. Sikoraby Oregon State University. The funders had no role in study design, datacollection and analysis, decision to publish, or preparation of the manuscript.
Publisher
Peer Reviewed
Language
Replaces
Additional Information
  • description.provenance : Made available in DSpace on 2013-05-22T16:46:33Z (GMT). No. of bitstreams: 2 license_rdf: 1232 bytes, checksum: bb87e2fb4674c76d0d2e9ed07fbb9c86 (MD5) SikoraAleksandraPharmacyProteinsSecretedVia.pdf: 438028 bytes, checksum: f5c26fe9136c441e77a74afbfb0ec698 (MD5) Previous issue date: 2013-02-21
  • description.provenance : Submitted by Deborah Campbell (deborah.campbell@oregonstate.edu) on 2013-05-22T16:45:26Z No. of bitstreams: 2 license_rdf: 1232 bytes, checksum: bb87e2fb4674c76d0d2e9ed07fbb9c86 (MD5) SikoraAleksandraPharmacyProteinsSecretedVia.pdf: 438028 bytes, checksum: f5c26fe9136c441e77a74afbfb0ec698 (MD5)
  • description.provenance : Approved for entry into archive by Deborah Campbell(deborah.campbell@oregonstate.edu) on 2013-05-22T16:46:33Z (GMT) No. of bitstreams: 2 license_rdf: 1232 bytes, checksum: bb87e2fb4674c76d0d2e9ed07fbb9c86 (MD5) SikoraAleksandraPharmacyProteinsSecretedVia.pdf: 438028 bytes, checksum: f5c26fe9136c441e77a74afbfb0ec698 (MD5)

Relationships

Parents:

This work has no parents.

Items