ArticleArchives of biochemistry and biophysics2018
Identification and structural characterization of a novel myeloperoxidase inhibitor from Staphylococcus delphini.
Article in Archives of biochemistry and biophysics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- Review
- New advances in understanding inhibition of myeloperoxidase and neutrophil serine proteases by two families of staphylococcal innate immune evasion proteins.Archives of biochemistry and biophysics · 2024Review
- Staphylococcal peroxidase inhibitor (SPIN): Investigation of the inhibitory N-terminal domain via a stabilizing disulfide insertion.Archives of biochemistry and biophysics · 2024Article
- Staphylococcal peroxidase inhibitor (SPIN): Residue-level investigation of the helical bundle domain.Archives of biochemistry and biophysics · 2024Article
- Staphylococcus aureus host interactions and adaptation.Nature reviews. Microbiology · 2023Review
- Coupled binding and folding of disordered SPIN N-terminal region in myeloperoxidase inhibition.Frontiers in molecular biosciences · 2023Article
- Non-Canonical Functions of Myeloperoxidase in Immune Regulation, Tissue Inflammation and Cancer.International journal of molecular sciences · 2022Review
- Thirty Years of sRNA-Mediated Regulation inInternational journal of molecular sciences · 2022Review
- Group BJournal of immunology (Baltimore, Md. : 1950) · 2022Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 3 countries.
Funding
Abstract
Staphylococcus aureus and related species are highly adapted to their hosts and have evolved numerous strategies to evade the immune system. S. aureus shows resistance to killing following uptake into the phagosome, which suggests that the bacterium evades intracellular killing mechanisms used by neutrophils. We recently discovered an S. aureus protein (SPIN for Staphylococcal Peroxidase INhibitor) that binds to and inhibits myeloperoxidase (MPO), a major player in the oxidative defense of neutrophils. To allow for comparative studies between multiple SPIN sequences, we identified a panel of homologs from species closely related to S. aureus. Characterization of these proteins revealed that SPIN molecules from S. agnetis, S. delphini, S. schleiferi, and S. intermedius all bind human MPO with nanomolar affinities, and that those from S. delphini, S. schleiferi, and S. intermedius inhibit human MPO in a dose-dependent manner. A 2.4 Å resolution co-crystal structure of SPIN-delphini bound to recombinant human MPO allowed us to identify conserved structural features of SPIN proteins, and to propose sequence-dependent physical explanations for why SPIN-aureus binds human MPO with higher affinity than SPIN-delphini. Together, these studies expand our understanding of MPO binding and inhibition by a recently identified component of the staphylococcal innate immune evasion arsenal.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.