Journal
EUROPEAN JOURNAL OF IMMUNOLOGY
Volume 40, Issue 1, Pages 186-196Publisher
WILEY
DOI: 10.1002/eji.200939819
Keywords
Antimicrobial peptide; CCL28; Chemokines; Innate Immunity
Categories
Funding
- National Institutes of Health [RAI072769A]
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R15AI072769] Funding Source: NIH RePORTER
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Several chemokines have been shown to act as antimicrobial proteins, suggesting a direct contribution to innate immune protection. Based on the study of defensins and other antimicrobial peptides, it has been proposed that cationic amino acids in these proteins play a key role in their antimicrobial activity. The primary structure requirements necessary for the antimicrobial activity of chemokines, however, have not yet been elucidated. Using mouse CCL28, we have identified a C-terminal region of highly-charged amino acids (RKDRK) that is essential to the antimicrobial activity of the murine chemokine. Additionally, other positively-charged amino acids in the C-terminus of the protein contribute to the observed antimicrobial effect. Charge reversal and deletion mutations support our hypothesis that C-terminal positively-charged amino acids are essential for the antimicrobial activity of CCL28. Results also demonstrate that although the C-terminal region of the chemokine is essential, it is not sufficient for full antimicrobial activity of CCL28.
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