1H 15N and 13C resonance assignments of the third domain from the S. aureus innate immune evasion protein Eap

摘要

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 () and Neutrophil Serine Proteases (NSPs) ().The third domain of Eap, Eap3, is an ~11 kDa protein that was recently shown to bind complement component C4b () and therefore play an essential role in inhibiting the classical and lectin pathways of complement (). 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.