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

Veterinary Microbiology
Tebekeme OkokoAnthony J Wilkinson

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 ...Continue Reading

References

Apr 27, 2002·Acta Crystallographica. Section D, Biological Crystallography·Marjorie M Harding
Jul 10, 2004·Nature·Eugenio SantelliRobert C Liddington
Dec 2, 2004·Acta Crystallographica. Section D, Biological Crystallography·E Krissinel, K Henrick
May 15, 2007·Journal of Bacteriology·Gavin A ByrneWim G Meijer
Oct 4, 2007·Equine Veterinary Journal·G MuscatelloJ A Vazquez-Boland
Jun 9, 2009·Journal of Molecular Biology·Vladimir M LevdikovAnthony J Wilkinson
Jan 9, 2010·Acta Crystallographica. Section D, Biological Crystallography·Alexei Vagin, Alexei Teplyakov
Jan 13, 2010·Veterinary Immunology and Immunopathology·Tamsin R M Y DawsonGary Muscatello
Feb 4, 2010·Acta Crystallographica. Section D, Biological Crystallography·Wolfgang Kabsch
Apr 13, 2010·Acta Crystallographica. Section D, Biological Crystallography·P EmsleyK Cowtan
Apr 5, 2011·Acta Crystallographica. Section D, Biological Crystallography·Philip R Evans
Jun 29, 2011·Journal of Molecular Biology·Vicki L ColledgeAnthony J Wilkinson
Nov 19, 2011·Journal of Veterinary Internal Medicine·S GiguèreJ F Prescott
May 11, 2013·Protein Science : a Publication of the Protein Society·Jenni LeppiniemiVesa P Hytönen
Sep 3, 2013·Veterinary Microbiology·José A Vázquez-BolandAna Valero-Rello
Apr 23, 2014·Nucleic Acids Research·Xavier Robert, Patrice Gouet
Aug 2, 2014·Acta Crystallographica. Section D, Biological Crystallography·Jean L WhittinghamAnthony J Wilkinson

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Citations

Dec 6, 2017·Molecular Microbiology·Lindsay M WrightVincent J Starai
Aug 4, 2021·Acta Crystallographica. Section F, Structural Biology Communications·Christina GeerdsHartmut H Niemann

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Methods Mentioned

BETA
circular dichroism
X-ray
size exclusion chromatography
gel
light scattering

Software Mentioned

REFMAC5
Astra V
CLUSTAL
COOT
XDS
MOLREP
CCP4mg
ESPript
Aimless

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