The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Degradation of Human Antimicrobial Peptide LL-37 by Staphylococcus aureus -Derived Proteinases
Open accessAbstract
Cathelicidin LL-37 is one of the few human bactericidal peptides with potent antistaphylococcal activity. In this study we examined the susceptibility of LL-37 to proteolytic degradation by two major proteinases produced by Staphylococcus aureus , a metalloproteinase (aureolysin) and a glutamylendopeptidase (V8 protease). We found that aureolysin cleaved and inactivated LL-37 in a time- and concentration-dependent manner. Analysis of the generated fragments by mass spectroscopy revealed that the initial cleavage of LL-37 by aureolysin occurred between the Arg19-Ile20, Arg23-Ile24, and Leu31-Val32 peptide bonds, instantly annihilating the antibacterial activity of LL-37. In contrast, the V8 proteinase hydrolyzed efficiently only the Glu16-Phe17 peptide bond, rendering the C-terminal fragment refractory to further degradation. This fragment (termed LL-17-37) displayed antibacterial activity against S. aureus at a molar level similar to that of the full-length LL-37 peptide, indicating that the antibacterial activity of LL-37 resides in the C-terminal region. In keeping with LL-37 degradation by aureolysin, S. aureus strains that produce significant amounts of this metalloprotease were found to be less susceptible to LL-17-37 than strains expressing no aureolysin activity. Taken together, these data suggest that aureolysin production by S. aureus contributes to the resistance of this pathogen to the innate immune system of humans mediated by LL-37.
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Cites
Endogenous Antimicrobial Peptides and Skin Infections in Atopic Dermatitis
Ong, P. Y., Ohtake, T., Brandt, C., Strickland, I., Boguniewicz, M., Ganz, T., Gallo, R. L., & Leung, D. Y. M. (2002) · New England Journal of Medicine · doi:10.1056/nejmoa021481 · Cited by 1,960
Innate antimicrobial peptide protects the skin from invasive bacterial infection
Nizet, V., Ohtake, T., Lauth, X., Trowbridge, J., Rudisill, J., Dorschner, R. A., Pestonjamasp, V., Piraino, J., Huttner, K., & Gallo, R. L. (2001) · Nature · doi:10.1038/35106587 · Cited by 1,198
Killing activity of neutrophils is mediated through activation of proteases by K+ flux
Reeves, E. P., Lu, H., Jacobs, H. L., Messina, C. G. M., Bolsover, S., Gabella, G., Potma, E. O., Warley, A., Roes, J., & Segal, A. W. (2002) · Nature · doi:10.1038/416291a · Cited by 1,153
Cathelicidins, multifunctional peptides of the innate immunity
Zanetti, M. (2004) · Journal of Leukocyte Biology · doi:10.1189/jlb.0403147 · Cited by 988
Dermcidin: A novel human antibiotic peptide secreted by sweat glands
Schittek, B., Hipfel, R., Sauer, B., Bauer, J., Kalbacher, H., Stevanovic, S., Schirle, M., Schroeder, K., Blin, N., Meier, F., et al. (2001) · Nature Immunology · doi:10.1038/ni732 · Cited by 730
Dorschner, R. A., Pestonjamasp, V. K., Tamakuwala, S., Ohtake, T., Rudisill, J., Nizet, V., Agerberth, B., Gudmundsson, G. H., & Gallo, R. L. (2001) · Journal of Investigative Dermatology · doi:10.1046/j.1523-1747.2001.01340.x · Cited by 567
Cathelicidin family of antimicrobial peptides: Proteolytic processing and protease resistance
Shinnar, A. E., Butler, K. L., & Park, H. J. (2003) · Bioorganic Chemistry · doi:10.1016/s0045-2068(03)00080-4 · Cited by 170
Cole, A. M., Shi, J., Ceccarelli, A., Kim, Y.-H., Park, A., & Ganz, T. (2001) · Blood · doi:10.1182/blood.v97.1.297 · Cited by 146
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Kong, H. H., Oh, J., Deming, C., Conlan, S., Grice, E. A., Beatson, M. A., Nomicos, E., Polley, E. C., Komarow, H. D., Program, N. C. S., et al. (2012) · Genome Research · doi:10.1101/gr.131029.111 · Cited by 1,808
Nakatsuji, T., Chen, T. H., Narala, S., Chun, K. A., Two, A. M., Yun, T., Shafiq, F., Kotol, P. F., Bouslimani, A., Melnik, A. V., et al. (2017) · Science Translational Medicine · doi:10.1126/scitranslmed.aah4680 · Cited by 1,095
The Alzheimer's Disease-Associated Amyloid β-Protein Is an Antimicrobial Peptide
Soscia, S. J., Kirby, J. E., Washicosky, K. J., Tucker, S. M., Ingelsson, M., Hyman, B., Burton, M. A., Goldstein, L. E., Duong, S., Tanzi, R. E., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009505 · Cited by 1,060
LL-37, the only human member of the cathelicidin family of antimicrobial peptides
Dürr, U. H. N., Sudheendra, U. S., & Ramamoorthy, A. (2006) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.03.030 · Cited by 1,049
Metadata
- Authors
- Sieprawska-Lupa, M., Mydel, P., Krawczyk, K., Wójcik, K., Puklo, M., Lupa, B., Suder, P., Silberring, J., Reed, M., Pohl, J., Shafer, W., McAleese, F., Foster, T., Travis, J., & Potempa, J.
- Venue
- Antimicrobial Agents and Chemotherapy
- Publisher
- American Society for Microbiology
- Published
- 2004-12
- Volume
- 48
- Issue
- 12
- Pages
- 4673-4679
- ISSN
- 0066-4804 (ISSN-L)
- 1098-6596
- OpenAlex
- W2098786490
- Cited by
- 551
- References
- 8
- FWCI
- 9.75
- Type
- journal article
- Language
- en
- Open access
- green
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- Sieprawska-Lupa, M., Mydel, P., Krawczyk, K., Wójcik, K., Puklo, M., Lupa, B., Suder, P., Silberring, J., Reed, M., Pohl, J., Shafer, W., McAleese, F., Foster, T., Travis, J., & Potempa, J. (2004). Degradation of Human Antimicrobial Peptide LL-37 by Staphylococcus aureus -Derived Proteinases. Antimicrobial Agents and Chemotherapy. https://doi.org/10.1128/aac.48.12.4673-4679.2004
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