The type IV secretion system core component VirB8 interacts via the β1-strand with VirB10

FEBS Lett. 2017 Aug;591(16):2491-2500. doi: 10.1002/1873-3468.12770. Epub 2017 Aug 11.

Abstract

In this work, we provide evidence for the interactions between VirB8 and VirB10, two core components of the type IV secretion system (T4SS). Using nuclear magnetic resonance experiments, we identified residues on the β1-strand of Brucella VirB8 that undergo chemical shift changes in the presence of VirB10. Bacterial two-hybrid experiments confirm the importance of the β1-strand, whereas phage display experiments suggest that the α2-helix of VirB8 may also contribute to the interaction with VirB10. Conjugation assays using the VirB8 homolog TraE as a model show that several residues on the β1-strand of TraE are important for T4SS function. Together, our results suggest that the β1-strand of VirB8-like proteins is essential for their interaction with VirB10 in the T4SS complex.

Keywords: NMR analysis; VirB10; VirB8; antibiotic resistance; conjugation assay; phage display; type IV secretion system; β1-strand.

Publication types

  • Letter
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism*
  • Brucella / metabolism
  • Models, Molecular
  • Protein Binding
  • Protein Conformation, beta-Strand
  • Type IV Secretion Systems / metabolism*

Substances

  • Bacterial Proteins
  • Type IV Secretion Systems

Associated data

  • PDB/2BHM

Grants and funding