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Staphylokinase has distinct modes of interaction with antimicrobial peptides, modulating its plasminogen-activation properties

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Author
Nguyen, Leonard, T.
Vogel, Hans J.
Accessioned
2017-01-18T17:24:23Z
Available
2017-01-18T17:24:23Z
Issued
2016-08-24
Subject
Biophysical chemistry
Solution-state NMR
Molecular biophysics
Type
journal article
Metadata
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Abstract
Staphylokinase (Sak) is a plasminogen activator protein that is secreted by many Staphylococcus aureus strains. Sak also offers protection by binding and inhibiting specific antimicrobial peptides (AMPs). Here, we evaluate Sak as a more general interaction partner for AMPs. Studies with melittin, mCRAMP, tritrpticin and bovine lactoferricin indicate that the truncation of the first ten residues of Sak (SakΔN10), which occurs in vivo and uncovers important residues in a bulge region, improves its affinity for AMPs. Melittin and mCRAMP have a lower affinity for SakΔN10, and in docking studies, they bind to the N-terminal segment and bulge region of SakΔN10. By comparison, lactoferricin and tritrpticin form moderately high affinity 1:1 complexes with SakΔN10 and their cationic residues form several electrostatic interactions with the protein’s α-helix. Overall, our work identifies two distinct AMP binding surfaces on SakΔN10 whose occupation would lead to either inhibition or promotion of its plasminogen activating properties.
Grantingagency
Canadian Institutes for Health Research
Refereed
Yes
Sponsorship
HJV currently holds the Armstrong Chair in Molecular Cancer Research.
Citation
Scientific Reports 6, Article number: 31817 (2016) doi:10.1038/srep31817
Department
Biological Sciences
Faculty
Science
Institution
University of Calgary
Url
http://www.nature.com/articles/srep31817
Publisher
Springer Nature
Doi
http://dx.doi.org/10.11575/PRISM/35088
Uri
http://hdl.handle.net/1880/51789
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