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Antimicrobial pepti...
Antimicrobial peptides derived from the cartilage.-specific C-type Lectin Domain Family 3 Member A (CLEC3A) – potential in the prevention and treatment of septic arthritis
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- Elezagic, D. (author)
- University of Cologne
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- Mörgelin, M. (author)
- Lund University,Lunds universitet,Infektionsmedicin,Sektion III,Institutionen för kliniska vetenskaper, Lund,Medicinska fakulteten,Infection Medicine (BMC),Section III,Department of Clinical Sciences, Lund,Faculty of Medicine
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- Hermes, G. (author)
- University of Cologne
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- Hamprecht, A. (author)
- University of Cologne
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- Sengle, G. (author)
- University Hospital of Cologne,University of Cologne
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- Lau, D. (author)
- University of Cologne
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- Höllriegl, S. (author)
- Sana Dreifaltigkeits-Krankenhaus
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- Wagener, Raimund (author)
- University of Cologne
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- Paulsson, M. (author)
- University of Cologne
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- Streichert, T. (author)
- University of Cologne
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- Klatt, Andreas R. (author)
- University of Cologne
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(creator_code:org_t)
- Elsevier BV, 2019
- 2019
- English.
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In: Osteoarthritis and Cartilage. - : Elsevier BV. - 1063-4584.
- Related links:
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http://dx.doi.org/10...
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Abstract
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- Objective: To investigate the antimicrobial activity of peptides derived from C-type Lectin Domain Family 3 Member A (CLEC3A), shed light on the mechanism of antimicrobial activity and assess their potential application in prevention and treatment of septic arthritis. Design: We performed immunoblot to detect CLEC3A peptides in human cartilage extracts. To investigate their antimicrobial activity, we designed peptides and recombinantly expressed CLEC3A domains and used them to perform viable count assays using E.coli, P.aeruginosa and S.aureus. We investigated the mechanism of their antimicrobial activity by fluorescence and scanning electron microscopy, performed ELISA-style immunoassays and transmission electron microscopy to test for lipopolysaccharide binding and surface plasmon resonance to test for lipoteichoic acid (LTA) binding. We coated CLEC3A peptides on titanium, a commonly used prosthetic material, and performed fluorescence microscopy to quantify bacterial adhesion. Moreover, we assessed the peptides’ cytotoxicity against primary human chondrocytes using MTT cell viability assays. Results: CLEC3A fragments were detected in human cartilage extracts. Moreover, bacterial supernatants lead to fragmentation of recombinant and cartilage-derived CLEC3A. CLEC3A-derived peptides killed E.coli, P.aeruginosa and S.aureus, permeabilized bacterial membranes and bound lipopolysaccharide and LTA. Coating CLEC3A antimicrobial peptides (AMPs) on titanium lead to significantly reduced bacterial adhesion to the material. In addition, microbicidal concentrations of CLEC3A peptides in vitro displayed no direct cytotoxicity against primary human chondrocytes. Conclusions: We identify cartilage-specific AMPs originating from CLEC3A, resolve the mechanism of their antimicrobial activity and point to a novel approach in the prevention and treatment of septic arthritis using potent, non-toxic, AMPs.
Subject headings
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Läkemedelskemi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Medicinal Chemistry (hsv//eng)
Keyword
- Antimicrobial peptides
- Arthroplasty
- Coating of prostheses
- Septic arthritis
Publication and Content Type
- art (subject category)
- ref (subject category)
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- By the author/editor
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Elezagic, D.
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Mörgelin, M.
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Hermes, G.
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Hamprecht, A.
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Sengle, G.
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Lau, D.
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show more...
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Höllriegl, S.
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Wagener, Raimund
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Paulsson, M.
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Streichert, T.
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Klatt, Andreas R ...
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show less...
- About the subject
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- MEDICAL AND HEALTH SCIENCES
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MEDICAL AND HEAL ...
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and Basic Medicine
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and Medicinal Chemis ...
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Osteoarthritis a ...
- By the university
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Lund University