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Home / Equine Research Bank / Vet Microbiol / Structural characterisation of the virulence-associated prot...
Veterinary microbiology2015; 179(1-2); 42-52; doi: 10.1016/j.vetmic.2015.01.027

Structural characterisation of the virulence-associated protein VapG from the horse pathogen Rhodococcus equi.

Abstract: Virulence and host range in Rhodococcus equi depends on the variable pathogenicity island of their virulence plasmids. Notable gene products are a family of small secreted virulence-associated proteins (Vaps) that are critical to intramacrophagic proliferation. Equine-adapted strains, which cause severe pyogranulomatous pneumonia in foals, produce a cell-associated VapA that is necessary for virulence, alongside five other secreted homologues. In the absence of biochemical insight, attention has turned to the structures of these proteins to develop a functional hypothesis. Recent studies have described crystal structures for VapD and a truncate of the VapA orthologue of porcine-adapted strains, VapB. Here, we crystallised the full-length VapG and determined its structure by molecular replacement. Electron density corresponding to the N-terminal domain was not visible suggesting that it is disordered. The protein core adopted a compact elliptical, anti-parallel β-barrel fold with β1-β2-β3-β8-β5-β6-β7-β4 topology decorated by a single peripheral α-helix unique to this family. The high glycine content of the protein allows close packing of secondary structural elements. Topologically, the surface has no indentations that indicate a nexus for molecular interactions. The distribution of polar and apolar groups on the surface of VapG is markedly uneven. One-third of the surface is dominated by exposed apolar side-chains, with no ionisable and only four polar side-chains exposed, giving rise to an expansive flat hydrophobic surface. Other surface regions are more polar, especially on or near the α-helix and a belt around the centre of the β-barrel. Possible functional significance of these recent structures is discussed.
Copyright © 2015. Published by Elsevier B.V.
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Publication Date: 2015-02-09 PubMed ID: 25746683PubMed Central: PMC4518536DOI: 10.1016/j.vetmic.2015.01.027Google Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This study focuses on understanding the structure of the virulence-associated protein VapG in the horse-disease causing bacterium Rhodococcus equi, aiming to provide biochemical insight that might aid in finding treatment strategies.

Background of the Study

  • The pathogenic bacterium Rhodococcus equi causes potentially lethal pneumonia in foals and is adaptable to a host’s environment thanks to a family of small secreted virulence-associated proteins (Vaps).
  • Among these, the VapA protein and its five secreted homologues are particularly significant as they are critical for the bacterium’s survival and proliferation within the host cells (macrophages).
  • In the face of limited biochemical understanding, researchers are turning to decoding the structure of these vital proteins as a way to hypothesize their functionality.

Research Methodology and Findings

  • In this study, the researchers crystallised and analysed the full-length VapG protein from Rhodococcus equi.
  • The researchers were unable to visualize the electron density corresponding to the N-terminal domain, indicating that it may be disordered or flexible.
  • The core of the VapG protein was found to have a compact elliptical β-barrel fold with a unique α-helix (a common secondary structure of proteins) supporting it.
  • The protein’s high glycine content (an amino acid) allows for a close packing of these secondary structural elements.
  • Further, the protein surface did not display any significant indentations signalling probable interaction points with other molecules.
  • The distribution of polar and non-polar groups on the surface of VapG was found to be uneven. One-third of the surface was dominated by exposed non-polar side-chains, manifesting as a large flat hydrophobic surface. Other surface regions were more polar, especially near the α-helix and around the center of the β-barrel.

Conclusions and Potential Functional Significance

  • Knowledge of the VapG protein’s structure adds to the understanding of the Vap family’s structural characteristics, particularly their surface characteristics.
  • This uneven distribution of polar and non-polar groups may well play a role in the protein’s functionality and possibly its adaptability.
  • The potential functional importance and overall implications of these structural findings need additional exploration.

Cite This Article

APA
Okoko T, Blagova EV, Whittingham JL, Dover LG, Wilkinson AJ. (2015). Structural characterisation of the virulence-associated protein VapG from the horse pathogen Rhodococcus equi. Vet Microbiol, 179(1-2), 42-52. https://doi.org/10.1016/j.vetmic.2015.01.027

Publication

Veterinary microbiology
ISSN: 1873-2542
NlmUniqueID: 7705469
Country: Netherlands
Language: English
Volume: 179
Issue: 1-2
Pages: 42-52
PII: S0378-1135(15)00057-7

Researcher Affiliations

Okoko, Tebekeme
  • Department of Applied Sciences, Faculty of Health and Life Sciences, Northumbria University, Newcastle upon Tyne NE1 8ST, UK.
Blagova, Elena V
  • Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York YO10 5DD, UK.
Whittingham, Jean L
  • Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York YO10 5DD, UK. Electronic address: jean.whittingham@york.ac.uk.
Dover, Lynn G
  • Department of Applied Sciences, Faculty of Health and Life Sciences, Northumbria University, Newcastle upon Tyne NE1 8ST, UK.
Wilkinson, Anthony J
  • Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York YO10 5DD, UK.

MeSH Terms

  • Actinomycetales Infections / microbiology
  • Actinomycetales Infections / veterinary
  • Animals
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Crystallography, X-Ray / veterinary
  • Genomic Islands / genetics
  • Horse Diseases / microbiology
  • Horses
  • Plasmids / genetics
  • Protein Structure, Secondary
  • Rhodococcus equi / chemistry
  • Rhodococcus equi / genetics
  • Rhodococcus equi / pathogenicity
  • Swine
  • Virulence

Grant Funding

  • BB/J007900/1 / Biotechnology and Biological Sciences Research Council

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This article has been cited 9 times.
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