Backbone resonance assignments of innate immune evasion protein EapH2 from the S. aureus
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Staphylococcus aureus is a ubiquitous and persistent pathogen of humans and livestock. The bacterium disrupts the host’s innate immune system’s ability to recognize and clear bacteria with optimal efficiency by expressing a wide variety of virulence proteins. Two single domain protein homologs (EapH1, EapH2) of the extracellular adherence protein (Eap) have been reported. Eap is a multidomain protein that participates in various protein–protein interactions that inhibit the innate immune response, including both the complement and Neutrophil Serine Proteases (NSPs). EapH1 and EapH2 are also inhibitors of NSPs (Stapels et al., Proc Natl Acad Sci 111:13187–13192, 2014), but lack the ability to inhibit the classical, and lectin pathways of the complement activation system (Woehl et al., J Immunol 193:6161–6171, 2014). We continue the characterization of Eap domains, here with the experiments on EapH2, we acquired a series of 2D and 3D NMR spectra of EapH2 in solution. We completed 99% of expected non-proline backbone 1H, 15N, and 13C resonance assignments of EapH2 and predicted secondary structure via the TALOS-N server. The assignment data have been deposited in the BMRB data bank under Accession Number 27540.
KeywordsBackbone resonance assignment Staphylococcus aureus Virulence protein Extracellular adherence protein homolog (EapH)
This research was funded by awards from the National Institutes of Health to B.V.G. (GM121511 and AI111203).
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Conflict of interest
The authors declare that they have no conflict of interest.
- Centers for Disease Control and Prevention (2011) 2011 Progress towards implementation of: a public health action plan to combat antimicrobial resistance. Retrieved from http://www.cdc.gov/drugresistance/resources/
- Keller R (2004) The computer aided resonance assignment tutorial. ISBN 3-85600-112-3Google Scholar
- Stapels DA, Ramyar KX, Bischoff M, von Köckritz-Blickwede M, Milder FJ, Ruyken M, Eisenbeis J, McWhorter WJ, Herrmann M, van Kessel KP, Geisbrecht BV, Rooijakkers SH (2014) Staphylococcus aureus secretes a unique class of neutrophil serine protease inhibitors. Proc Natl Acad Sci USA 111:13187–13192ADSCrossRefGoogle Scholar
- Whitehead B, Craven CJ, Waltho JP (1997) Double and triple resonance NMR methods for protein assignment. In: Reid DG (eds) Protein NMR techniques. Methods in molecular biology, vol 60. Humana Press, TotowaGoogle Scholar
- Woehl JL, Stapels DAC, Garcia BL, Ramyar KX, Keightley A, Ruyken M, Syriga M, Sfyroera G, Weber AB, Zolkiewski M, Ricklin D, Lambris JD, Rooijakkers SHM, Geisbrecht BV (2014) The extracellular adherence protein from Staphylococcus aureus inhibits the classical and lectin pathways of complement by blocking formation of the C3 pro-convertase. J Immunol 193:6161–6171CrossRefGoogle Scholar