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Characterization of a novel interaction between BLIP‐II and Staphylococcus aureus PBP2a
Author(s) -
Adamski Carolyn J,
Chow DarChone,
Brown Nicholas,
Palzkill Timothy
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.1013.2
Subject(s) - surface plasmon resonance , mutagenesis , staphylococcus aureus , penicillin binding proteins , binding site , plasma protein binding , protein–protein interaction , chemistry , biology , computational biology , gene , biochemistry , escherichia coli , genetics , mutation , nanotechnology , materials science , bacteria , nanoparticle
The prediction and manipulation of protein‐protein interactions remains a difficult task. Model systems such as the β‐lactamase inhibitory protein II (BLIP‐II) and β‐lactamases have been used to investigate the principles of protein‐protein interactions. Previous studies focused on the determinants of binding affinity and specificity between BLIP‐II and class A β‐lactamases. However, interactions between BLIP‐II and other proteins have yet to be explored. In this study, we characterized the novel interaction between BLIP‐II and penicillin binding protein 2a (PBP2a) from methicillin resistant Staphylococcus aureus . Mutagenesis and surface plasmon resonance experiments were used to determine how specificity is achieved between BLIP‐II and its binding partners. The results suggest that an outer ring of residues on the BLIP‐II interface plays a critical role in binding PBP2a while an inner ring of residues on the binding surface is primarily responsible for the binding of β‐lactamases. Changes in BLIP‐II binding affinity for PBP2a and β‐lactamases were found to be largely due to changes in k on and k off , respectively. In summary, the results of the study indicate BLIP‐II binds PBP2a in addition to β‐lactamases and provide insights into how BLIP‐II binds a wide range of target proteins. Research support provided by grants R01 A132956 and R21 A1092063 to T.P.