Difference between revisions of "Part:BBa K3351002"

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HBD3, an antimicrobial peptide.

Summary

The three human β-defensins, HBD1-3, are 33-47-residue, cationic antimicrobial proteins expressed by epithelial cells. All three proteins have broad spectrum antimicrobial activity, with HBD3 consistently being the most potent. Additionally, HBD3 has significant bactericidal activity against Gram-positive Staphylococcus aureus at physiological salt concentrations.Defensins are small, 3–5 kDa cationic proteins constrained by three disulfide bonds. As a class of proteins, they have broad microbicidal activity against Gram-positive and -negative bacteria, yeast, and some enveloped viruses, although specific defensin peptides often have defined spectra of activity. Like many other antimicrobial peptides, the defensin class of peptides is known to disrupt the membranes of microbes . It has recently been reported that in addition to their antimicrobial activity, defensins may act as chemokines, activating the adaptive immune response .HBD3 possesses bactericidal activity against Gram-positive and -negative bacteria, including multi-drug-resistant S. aureus, vancomycin-resistant Enterococcus faecium, and Burkholderia cepacia in addition to the yeast C. albicans .

Reference

[1] David J,Schibli,Howard N,Hunter,Vladimir,Aseyev,Timothy D,Starner,John M,Wiencek,Paul B,McCray,Brian F,Tack,Hans J,Vogel.The solution structures of the human beta-defensins lead to a better understanding of the potent bactericidal activity of HBD3 against Staphylococcus aureus.[J].The Journal of biological chemistry,2002,277(10):8279-89.
[2] Schroder, J. M. (1999) Cell. Mol. Life Sci. 56, 32–46
[3] Epand, R. M., and Vogel, H. J. (1999) Biochim. Biophys. Acta 1462, 11–28
[4] Harder, J., Bartels, J., Christophers, E., and Schroder, J. M. (2001) J. Biol. Chem. 276, 5707–5713
Sequence and Features