Human p-defensin

Howell MD The role of human p defensins and cathelicidins in atopic dermatitis. Curr Opin Allergy Clin Immunol 2007 7 413-417. 

VSL 3 probiotic mixture Improves epithelial barrier function Induces human p-defensin, hBD-2 gene expression Schlee et al. (2008)... 

Wehkamp, J., Harder, J., Wehkamp, K., Wehkamp-von Meissner, B., Schlee, M., Enders, C., Sonnenborn, U., Nuding, S., Bengmark, S., Fellermann, K., Schroder, J. M., and Stange, E. F. (2004). NF-kB- and AP-l-mediated induction of human p-defensin-2 in intestinal epithelial cells by Escherichia coli Nissle 1917 A novel effect of a probiotic bacterium. Infect. Immun. 72(10), 5750-5758. 

Goldman Ml, Stotzenberg ED, Karl UP, Zasloff M, Wilson JM Human p-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis. Cell 1997 88 553-560. 

Figure 31-7 Ribbon structures of some defensins. (A) Structure of a human P-defensin showing the three disulfide bonds. From Bauer rf Courtesy of Heinrich Sticht. (B) Comparison of the folding patterns of four types of defensins. Mammalian a- and P-defensins are all P sheets with somewhat different arrangements of disulfide bridges. Insect and plant defensins have an a helix joined to the P sheet. Mammalian and insect defensins have three disulfide bridges, while plant defensins have four. From Hoffmann ef Courtesy of Jules A. Hoffmarm.

Defensin-fold family, a peptide family consisting of a short helix or turn followed by a small twisted anti-parallel /3-sheet. This fold is very similar to that of /3-defensins defensins). The six Cys are paired in a 1 5, 2 4, 3 6 alignment. Members of this family include peptides with 35-50 aa in sea anemones anthopleurin A, Shi), snakes crotamine), platypus defensin-like peptides) and humans (/3-defensins) possessing disparate activities, such as antimicrobial, myonecrotic, analgesic, and ion-channel-inhibiting [A. M. Torres, P. 

Figure 2.9. Amino acid sequences of human defensins. The conserved positions of six cysteine residues are shown in hatched boxes. Abbreviations A, alanine C, cysteine D, aspartic acid E, glutamic acid F, phenylalanine G, glycine H, histidine I, isoleucine K, lysine L, leucine M, methionine N, asparagine P, proline Q, glutamic acid R, arginine S, serine T, threonine V, valine W, tryptophan Y, tyrosine.

Peschel, A., Jack, R., Otto, M., Collins, L., Staubitz, P., Nicholson, G., Kalbacher, H., Nieuwenhuizen, W., Jung, G., Tarkowski, A., van Kessel, K., van Strijp, J. Staphylococcus aureus resistance to human defensins and evasion of neutrophil killing via the novel virulence factor MprF is based on modification of membrane lipids with 1-lysine. J Exp Med 193 (2001) 1067-1076. 

The data base PORINS consisted of seven porins and two defensins all with known or proposed transmembrane P-strand structure. The porins with known X-ray structure were porin from Rhodobacter capsulatus [10,28] and porins PhoE and OmpF from Escherichia coli [39,11]. Porins with proposed transmembrane P-barrel topology were anion-selective porin Omp32 from Comamonas acidovorans [40], outer membrane protein OmpA from Escherichia coli K12 membrane (membrane-embedded fragment residues 1 to 177, [41,42]), and mitochondrial outer membrane porin from human B-lymphocytes [43] and from Neurospora crassa [44]. Two defensins of known structure were HNP-3 [45] and defensin from larvae of the dragonfly Aeschna cyanea [46]. 

Mammalian defensins 3 P Sttands 3 disulfides Rat, rabbit, guinea pig, human neucrophifs. rabbit alveolar macrophages, human, mouse Paneth cells MCP,NP,HNP,GNCP. rat NP, ciyptidins... 

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