1H, 15N, and 13C resonance assignments of the third domain from the S. aureus innate immune evasion protein Eap
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Staphylococcus aureus is a widespread and persistent pathogen of humans and livestock. The bacterium expresses a wide variety of virulence proteins, many of which serve to disrupt the host’s innate immune system from recognizing and clearing bacteria with optimal efficiency. The extracellular adherence protein (Eap) is a multidomain protein that participates in various protein–protein interactions that inhibit the innate immune response, including both the complement system (Woehl et al in J Immunol 193:6161–6171, 2014) and Neutrophil Serine Proteases (NSPs) (Stapels et al in Proc Natl Acad Sci USA 111:13187–13192, 2014). The third domain of Eap, Eap3, is an ~ 11 kDa protein that was recently shown to bind complement component C4b (Woehl et al in Protein Sci 26:1595–1608, 2017) and therefore play an essential role in inhibiting the classical and lectin pathways of complement (Woehl et al in J Immunol 193:6161–6171, 2014). Since structural characterization of Eap3 is still incomplete, we acquired a series of 2D and 3D NMR spectra of Eap3 in solution. Here we report the backbone and side-chain 1H, 15N, and 13C resonance assignments of Eap3 and its predicted secondary structure via the TALOS-N server. The assignment data have been deposited in the BMRB data bank under accession number 27087.
KeywordsNMR assignment Staphylococcus aureus Virulence protein Extracellular adherence protein (Eap)
This research was funded by awards from the National Institutes of Health to B.V.G. (GM121511 and AI111203). We are thankful to Dr. Justin Douglas of University of Kansas for helping with NMR spectroscopy. We also thank Center of Biomedical Research Excellence in Protein Structure and Function (COBRE-PSF) at The University of Kansas (NIH Grant P30 GM110761) for support in NMR studies.
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Conflict of interest
The authors declare no conflicts of interest.
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