β-Defensins: multifunctional modulators of infection, inflammation and more? - PubMed (original) (raw)

Review

β-Defensins: multifunctional modulators of infection, inflammation and more?

Fiona Semple et al. J Innate Immun. 2012.

Abstract

Defensins comprise one of the largest groups of host defence peptides, present throughout evolution, in fungi and flowering plants as well as in invertebrates and vertebrates. These cysteine-rich, cationic peptides have a common ability to kill a broad range of microorganisms including bacteria, yeast and viruses. As such, they are a strong component of the arsenal that is an organism's innate immunity. It is becoming increasingly clear, however, that antimicrobial action is only one of the numerous roles of these multifunctional peptides. In recent years, the functions of defensins in immunomodulation have been widely investigated, and their involvement in other processes (such as fertility) is becoming evident. This review addresses recent advances in the immunomodulatory activity of β-defensins as well as the involvement of β-defensins in fertility, development, wound healing and cancer.

Copyright © 2012 S. Karger AG, Basel.

PubMed Disclaimer

Figures

Fig. 1

Fig. 1

β-Defensin structure. Homology model of β-defensin Defb14 based on the structure of hBD3, with antimicrobially potent residues 6–17 highlighted in yellow and β-sheets in blue [32].

Fig. 2

Fig. 2

Structural integrity is required for hBD3 immunosuppressive effect. Treatment of RAW264.7 macrophage cell line with LPS results in an increase in TNFα levels (measured by ELISA). In the presence of LPS, oxidized and canonically folded hBD3 (hBD3-F; black bars) inhibits this induction of TNFα. In contrast, linear hBD3 (hBD3-L) does not inhibit LPS-induced TNFα.

Fig. 3

Fig. 3

hBD3 rapidly enters macrophages. The image shows a single cell (from the macrophage-like cell line RAW264.7) 10 min after the addition of hBD3 labeled with a TAMRA fluorochrome (red). Nuclear staining with DAPI (blue) demonstrates that at this time-point, hBD3 accumulates in the cytoplasm. Picture kindly provided by Dr. Heather MacPherson, MRC Human Genetics Unit, Edinburgh, UK.

Similar articles

Cited by

References

    1. Lynn DJ, Bradley DG. Discovery of alpha-defensins in basal mammals. Dev Comp Immunol. 2007;31:963–967. - PubMed
    1. Lehrer RI. Primate defensins. Nat Rev Microbiol. 2004;2:727–738. - PubMed
    1. Pazgier M, Hoover DM, Yang D, Lu W, Lubkowski J. Human beta-defensins. Cell Mol Life Sci. 2006;63:1294–1313. - PMC - PubMed
    1. Nguyen TX, Cole AM, Lehrer RI. Evolution of primate theta-defensins: a serpentine path to a sweet tooth. Peptides. 2003;24:1647–1654. - PubMed
    1. Schutte BC, Mitros JP, Bartlett JA, Walters JD, Jia HP, Welsh MJ, Casavant TL, McCray PB., Jr Discovery of five conserved beta-defensin gene clusters using a computational search strategy. Proc Natl Acad Sci USA. 2002;99:2129–2133. - PMC - PubMed

Publication types

MeSH terms

Substances

LinkOut - more resources