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Sökning: id:"swepub:oai:lup.lub.lu.se:42c87322-33f9-420b-84ef-34c7d785f820" > Antimicrobial pepti...

  • Elezagic, D.University of Cologne (författare)

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

  • Artikel/kapitelEngelska2019

Förlag, utgivningsår, omfång ...

  • Elsevier BV,2019

Nummerbeteckningar

  • LIBRIS-ID:oai:lup.lub.lu.se:42c87322-33f9-420b-84ef-34c7d785f820
  • https://lup.lub.lu.se/record/42c87322-33f9-420b-84ef-34c7d785f820URI
  • https://doi.org/10.1016/j.joca.2019.06.007DOI

Kompletterande språkuppgifter

  • Språk:engelska
  • Sammanfattning på:engelska

Ingår i deldatabas

Klassifikation

  • Ämneskategori:art swepub-publicationtype
  • Ämneskategori:ref swepub-contenttype

Anmärkningar

  • 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.

Ämnesord och genrebeteckningar

Biuppslag (personer, institutioner, konferenser, titlar ...)

  • Mörgelin, M.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(Swepub:lu)medk-mmn (författare)
  • Hermes, G.University of Cologne (författare)
  • Hamprecht, A.University of Cologne (författare)
  • Sengle, G.University Hospital of Cologne,University of Cologne (författare)
  • Lau, D.University of Cologne (författare)
  • Höllriegl, S.Sana Dreifaltigkeits-Krankenhaus (författare)
  • Wagener, RaimundUniversity of Cologne (författare)
  • Paulsson, M.University of Cologne (författare)
  • Streichert, T.University of Cologne (författare)
  • Klatt, Andreas R.University of Cologne (författare)
  • University of CologneInfektionsmedicin (creator_code:org_t)

Sammanhörande titlar

  • Ingår i:Osteoarthritis and Cartilage: Elsevier BV1063-4584

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