Abstract
The pathogenic bacterium Staphylococcus aureus has evolved to actively evade many aspects of the human innate immune system by expressing a series of secreted inhibitory proteins. Among these, the extracellular adherence protein (Eap) has been shown to inhibit the classical and lectin pathways of the complement system. By binding to complement component C4b, Eap is able to inhibit formation of the CP/LP C3 pro-convertase. Secreted full-length, mature Eap consists of four ~98 residue domains, all of which adopt a similar beta-grasp fold, and are connected through a short linker region. Through multiple biochemical approaches, it has been determined that the third and fourth domains of Eap are responsible for C4b binding. Here we report the backbone and side-chain resonance assignments of the 11.3 kDa fourth domain of Eap. The assignment data has been deposited in the BMRB database under the accession number 26726.
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This work was supported by the American Heart Association Midwest Affiliate Pre-doctoral Research Fellowship 15PRE25750013 and by National Institutes of Health (NIH) Grant AI111203.
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Woehl, J.L., Takahashi, D., Herrera, A.I. et al. 1H, 15N, and 13C resonance assignments of Staphylococcus aureus extracellular adherence protein domain 4. Biomol NMR Assign 10, 301–305 (2016). https://doi.org/10.1007/s12104-016-9688-5
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DOI: https://doi.org/10.1007/s12104-016-9688-5