Structure-dependent functional properties of human defensin 5.

Abstract:

:The mucosal epithelium secretes a variety of antimicrobial peptides that act as part of the innate immune system to protect against invading microbes. Here, we describe the functional properties of human defensin (HD) 5, the major antimicrobial peptide produced by Paneth cells in the ileum, in relation to its structure. The antimicrobial activity of HD-5 against Escherichia coli proved to be independent of its structure, whereas the unstructured peptide showed greatly reduced antimicrobial activity against Staphylococcus aureus. We find that HD-5 binds to the cell membrane of intestinal epithelial cells and induced secretion of the chemokine interleukin (IL)-8 in a concentration- and structure-dependent fashion. Incubation of HD-5 in the presence of tumor necrosis factor alpha further increased IL-8 secretion synergistically, suggesting that HD-5 may act as a regulator of the intestinal inflammatory response.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

de Leeuw E,Burks SR,Li X,Kao JP,Lu W

doi

10.1016/j.febslet.2006.12.036

subject

Has Abstract

pub_date

2007-02-06 00:00:00

pages

515-20

issue

3

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(06)01492-X

journal_volume

581

pub_type

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