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InvB is a type III secretion chaperone specific for SspA.

Publication ,  Journal Article
Bronstein, PA; Miao, EA; Miller, SI
Published in: J Bacteriol
December 2000

A wide variety of gram-negative bacteria utilize a specialized apparatus called the type III secretion system (TTSS) to translocate virulence factors directly into the cytoplasm of eukaryotic cells. These translocated effectors contribute to the pathogen's ability to infect and replicate within plant and animal hosts. The amino terminus of effector proteins contains sequences that are necessary and sufficient for both secretion and translocation by TTSS. Portions of these sequences contain binding sites for type III chaperones, which facilitate efficient secretion and translocation of specific effectors through TTSS. In this study, we have utilized the yeast two-hybrid assay to identify protein-protein interactions between effector and chaperone proteins encoded within Salmonella pathogenicity island 1 (SPI-1). Several interactions were identified including a novel interaction between the effector protein, SspA (SipA), and a putative chaperone, InvB. InvB was demonstrated to bind to the amino terminus of SspA in the bacterial cytoplasm. Furthermore, InvB acts as a type III chaperone for the efficient secretion and translocation of SspA by SPI-1. InvB also permitted translocation of SspA through the SPI-2 TTSS, indicating that it is an important regulator in the recognition of SspA as a target of TTSS. Finally, it was determined that InvB does not alter the transcription of sspA but that its absence results in reduced SspA protein levels in Salmonella enterica serovar Typhimurium.

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Published In

J Bacteriol

DOI

ISSN

0021-9193

Publication Date

December 2000

Volume

182

Issue

23

Start / End Page

6638 / 6644

Location

United States

Related Subject Headings

  • Two-Hybrid System Techniques
  • Transcription, Genetic
  • Salmonella typhimurium
  • Saccharomyces cerevisiae
  • Recombinant Fusion Proteins
  • Rabbits
  • Precipitin Tests
  • Molecular Chaperones
  • Microbiology
  • Cytoplasm
 

Citation

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Bronstein, P. A., Miao, E. A., & Miller, S. I. (2000). InvB is a type III secretion chaperone specific for SspA. J Bacteriol, 182(23), 6638–6644. https://doi.org/10.1128/JB.182.23.6638-6644.2000
Bronstein, P. A., E. A. Miao, and S. I. Miller. “InvB is a type III secretion chaperone specific for SspA.J Bacteriol 182, no. 23 (December 2000): 6638–44. https://doi.org/10.1128/JB.182.23.6638-6644.2000.
Bronstein PA, Miao EA, Miller SI. InvB is a type III secretion chaperone specific for SspA. J Bacteriol. 2000 Dec;182(23):6638–44.
Bronstein, P. A., et al. “InvB is a type III secretion chaperone specific for SspA.J Bacteriol, vol. 182, no. 23, Dec. 2000, pp. 6638–44. Pubmed, doi:10.1128/JB.182.23.6638-6644.2000.
Bronstein PA, Miao EA, Miller SI. InvB is a type III secretion chaperone specific for SspA. J Bacteriol. 2000 Dec;182(23):6638–6644.

Published In

J Bacteriol

DOI

ISSN

0021-9193

Publication Date

December 2000

Volume

182

Issue

23

Start / End Page

6638 / 6644

Location

United States

Related Subject Headings

  • Two-Hybrid System Techniques
  • Transcription, Genetic
  • Salmonella typhimurium
  • Saccharomyces cerevisiae
  • Recombinant Fusion Proteins
  • Rabbits
  • Precipitin Tests
  • Molecular Chaperones
  • Microbiology
  • Cytoplasm