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Selective arginines are important for the antibacterial activity and host cell interaction of human α‐defensin 5
Author(s) -
de Leeuw Erik,
Rajabi Mohsen,
Zou Guozhang,
Pazgier Marzena,
Lu Wuyuan
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.06.051
Subject(s) - defensin , histidine , arginine , beta defensin , lysine , antimicrobial peptides , peptide sequence , function (biology) , alanine , host (biology) , biology , chemistry , antimicrobial , biochemistry , amino acid , microbiology and biotechnology , bacterial cell structure , bacteria , genetics , gene
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.