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Citrullination Alters the Antibacterial and Anti-Inflammatory Functions of the Host Defense Peptide Canine Cathelicidin K9CATH In Vitro
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för biokemi och biofysik.ORCID-id: 0000-0003-4464-1769
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Antal upphovsmän: 102021 (Engelska)Ingår i: Journal of Immunology, ISSN 0022-1767, E-ISSN 1550-6606, Vol. 207, nr 3, s. 974-984Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

K9CATH is the sole cathelicidin in canines (dogs) and exhibits broad antimicrobial activity against both Gram-positive and Gram-negative bacteria. K9CATH also modulates inflammatory responses and binds to LPS. These activities depend on the secondary structure and a net-positive charge of the peptide. Peptidylarginine deiminases (PAD) convert cationic peptidyl arginine to neutral citrulline. Thus, we hypothesized that citrullination is a biologically relevant modification of the peptide that would reduce the antibacterial and LPS-binding activities of K9CATH. Recombinant PAD2 and PAD4 citrullinated K9CATH to various extents and circular dichroism spectroscopy revealed that both native and citrullinated K9CATH exhibited similar α-helical secondary structures. Notably, citrullination of K9CATH reduced its bactericidal activity, abolished its ability to permeabilize the membrane of Gram-negative bacteria and reduced the hemolytic capacity. Electron microscopy showed that citrullinated K9CATH did not cause any morphological changes of Gram-negative bacteria, whereas the native peptide caused clear alterations of membrane integrity, concordant with a rapid bactericidal effect. Finally, citrullination of K9CATH impaired its capacity to inhibit LPS-mediated release of proinflammatory molecules from mouse and canine macrophages. In conclusion, citrullination attenuates the antibacterial and the LPS-binding properties of K9CATH, demonstrating the importance of a net positive charge for antibacterial lysis of bacteria and LPS-binding effects and suggests that citrullination is a means to regulate cathelicidin activities.

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2021. Vol. 207, nr 3, s. 974-984
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Biologiska vetenskaper
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URN: urn:nbn:se:su:diva-200959DOI: 10.4049/jimmunol.2001374ISI: 000731634700011PubMedID: 34282000OAI: oai:DiVA.org:su-200959DiVA, id: diva2:1627786
Tillgänglig från: 2022-01-14 Skapad: 2022-01-14 Senast uppdaterad: 2022-02-25Bibliografiskt granskad

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Mörman, CeciliaGräslund, AstridVégvári, ÁkosRising, AnnaBergman, Peter

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Mörman, CeciliaGräslund, AstridVégvári, ÁkosRising, AnnaBergman, Peter
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