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

D Elezagic; M Mörgelin; G Hermes; A Hamprecht; G Sengle; D Lau; S Höllriegl; R Wagener; M Paulsson; T Streichert; A R Klatt

doi:10.1016/j.joca.2019.06.007

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

Standard

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. / Elezagic, D; Mörgelin, M; Hermes, G; Hamprecht, A; Sengle, G; Lau, D; Höllriegl, S; Wagener, R; Paulsson, M; Streichert, T; Klatt, A R.

in: OSTEOARTHR CARTILAGE, Jahrgang 27, Nr. 10, 10.2019, S. 1564-1573.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Elezagic, D, Mörgelin, M, Hermes, G, Hamprecht, A, Sengle, G, Lau, D, Höllriegl, S, Wagener, R, Paulsson, M, Streichert, T & Klatt, AR 2019, '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', OSTEOARTHR CARTILAGE, Jg. 27, Nr. 10, S. 1564-1573. https://doi.org/10.1016/j.joca.2019.06.007

APA

Elezagic, D., Mörgelin, M., Hermes, G., Hamprecht, A., Sengle, G., Lau, D., Höllriegl, S., Wagener, R., Paulsson, M., Streichert, T., & Klatt, A. R. (2019). 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. OSTEOARTHR CARTILAGE, 27(10), 1564-1573. https://doi.org/10.1016/j.joca.2019.06.007

Vancouver

Elezagic D, Mörgelin M, Hermes G, Hamprecht A, Sengle G, Lau D et al. 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. OSTEOARTHR CARTILAGE. 2019 Okt;27(10):1564-1573. https://doi.org/10.1016/j.joca.2019.06.007

Bibtex

@article{0864a2c1b5084cf289ffe6a1bab86374,

title = "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",

abstract = "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.",

author = "D Elezagic and M M{\"o}rgelin and G Hermes and A Hamprecht and G Sengle and D Lau and S H{\"o}llriegl and R Wagener and M Paulsson and T Streichert and Klatt, {A R}",

year = "2019",

month = oct,

doi = "10.1016/j.joca.2019.06.007",

language = "English",

volume = "27",

pages = "1564--1573",

journal = "OSTEOARTHR CARTILAGE",

issn = "1063-4584",

publisher = "W.B. Saunders Ltd",

number = "10",

}

RIS

TY - JOUR

T1 - 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

AU - Elezagic, D

AU - Mörgelin, M

AU - Hermes, G

AU - Hamprecht, A

AU - Sengle, G

AU - Lau, D

AU - Höllriegl, S

AU - Wagener, R

AU - Paulsson, M

AU - Streichert, T

AU - Klatt, A R

PY - 2019/10

Y1 - 2019/10

N2 - 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.

AB - 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.

U2 - 10.1016/j.joca.2019.06.007

DO - 10.1016/j.joca.2019.06.007

M3 - SCORING: Journal article

C2 - 31279936

VL - 27

SP - 1564

EP - 1573

JO - OSTEOARTHR CARTILAGE

JF - OSTEOARTHR CARTILAGE

SN - 1063-4584

IS - 10

ER -