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Related Experiment Videos

InvB is a type III secretion chaperone specific for SspA.

P A Bronstein1, E A Miao, S I Miller

  • 1Department of Microbiology, University of Washington, Seattle, Washington 98195, USA.

Journal of Bacteriology
|November 14, 2000
PubMed
Summary

Type III secretion systems (TTSS) deliver bacterial effector proteins into host cells. This study identifies InvB as a novel chaperone for the SspA effector, crucial for its secretion and translocation by Salmonella.

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Bacterial Pathogenesis

Background:

  • Gram-negative bacteria use type III secretion systems (TTSS) to inject effector proteins into host cells, aiding infection.
  • Effector protein N-termini contain secretion and translocation signals, interacting with type III chaperones.

Purpose of the Study:

  • To identify protein-protein interactions between Salmonella pathogenicity island 1 (SPI-1) effector and chaperone proteins.
  • To characterize the role of the novel interaction between effector SspA and chaperone InvB in TTSS-mediated delivery.

Main Methods:

  • Yeast two-hybrid assay to detect effector-chaperone interactions.
  • In vitro binding assays to confirm cytoplasmic interaction between InvB and SspA N-terminus.
  • Translocation assays using TTSS.

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Main Results:

  • A novel interaction was identified between the effector SspA and the putative chaperone InvB.
  • InvB binds to the SspA N-terminus and functions as a type III chaperone for SspA secretion and translocation via SPI-1.
  • InvB facilitates SspA translocation through the SPI-2 TTSS, indicating its regulatory role.
  • InvB absence reduces SspA protein levels without affecting sspA transcription.

Conclusions:

  • InvB is a novel type III chaperone for the effector SspA in Salmonella.
  • InvB plays a critical role in regulating SspA secretion, translocation, and stability.
  • InvB is a key factor in Salmonella pathogenesis mediated by TTSS.