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Publication Abstract from PubMed

Defensins constitute a major family of natural antimicrobial peptides that protect the host against microbial invasion. Here, we report on the antibacterial properties and cellular interaction of Human Defensin 5 as a function of its positive charge and hydrophobicity. We find that selective replacement of arginine residues in HD-5 by alanine or charge-neutral lysine residues reduces antibacterial killing as well as host cell interaction. We identify arginines at positions 9 and 28 in the HD-5 sequence as particularly important for its function. Replacement of arginine at position 13 to Histidine, as observed in a Crohn's disease patient, reduced bacterial killing strain-selectively. Finally, we find that HD-5 interacts with host cells via receptor-mediated mechanisms.

Selective arginines are important for the antibacterial activity and host cell interaction of human alpha-defensin 5.,de Leeuw E, Rajabi M, Zou G, Pazgier M, Lu W FEBS Lett. 2009 Aug 6;583(15):2507-12. Epub 2009 Jul 7. PMID:19589339^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.