Pathogenic bacteria use a variety of mechanisms to combat the host immune response. New data indicate that Shigella spp. make a preemptive strike against the deployment of host antibacterial peptides (pages 180–185).
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References
Islam, D. et al. Nature Med. 7,180–185 (2001).
Nhieu, G.T. & Sansonetti, P.J. Mechanism of Shigella entry into epithelial cells. Curr. Opin. Microbiol. 2, 51–55 (1999).
Rathman, M., de Lanerolle, P., Ohayon, H., Gounon, P. & Sansonetti, P. Myosin light chain kinase plays an essential role in S. flexneri dissemination. J. Cell Sci. 113, 3375–3386 (2000).
Gallo, R.L. et al. Identification of CRAMP, a cathelin-related antimicrobial peptide expressed in the embryonic and adult mouse. J. Biol. Chem. 272, 13088–13093 (1997).
Morrison, G.M., Davidson, D.J. & Dorin, J.R. A novel mouse β defensin, Defb2, which is upregulated in the airways by lipopolysaccharide. FEBS Lett. 442, 112–116 (1999).
Bals, R. et al. Mouse β-defensin 3 is an inducible antimicrobial peptide expressed in the epithelia of multiple organs. Infect. Immun. 67, 3542–3547 (1999).
O'Neil, D.A. et al. Expression and regulation of the human β-defensins hBD-1 and hBD-2 in intestinal epithelium. J. Immunol. 163, 6718–6724 (1999).
Harder, J., Bartels, J., Christophers, E. & Schroder, J.M. Isolation and characterization of Human {β}-Defensin-3, a novel human inducible peptide antibiotic. J. Biol. Chem. (Nov 20, 2000, epub ahead of print).
Diamond, G., Kaiser, V., Rhodes, J., Russell, J.P. & Bevins, C.L. Transcriptional regulation of β-defensin gene expression in tracheal epithelial cells. Infect. Immun. 68, 113–119. (2000).
Frohm, M. et al. The expression of the gene coding for the antibacterial peptide LL-37 is induced in human keratinocytes during inflammatory disorders. J. Biol. Chem. 272, 15258–15263 (1997).
Turner, J., Cho, Y., Dinh, N.N., Waring, A.J. & Lehrer, R.I. Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils. Antimicrob. Agts. Chemother. 42, 2206–2214 (1998).
Gudmundsson, G.H. et al. The human gene FALL39 and processing of the cathelin precursor to the antibacterial peptide LL-37 in granulocytes. Eur. J. Biochem. 238, 325–332 (1996).
Wu, H., Zhang, G., Minton, J.E., Ross, C.R. & Blecha, F. Regulation of cathelicidin gene expression: induction by lipopolysaccharide, interleukin-6, retinoic acid, and Salmonella enterica serovar typhimurium infection. Infect. Immun. 68, 5552–5558 (2000).
Hemmi, H. et al. A Toll-like receptor recognizes bacterial DNA. Nature 408, 740–745 (2000).
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Lehrer, R. Shigellae control the Gates of LL. Nat Med 7, 158–159 (2001). https://doi.org/10.1038/84594
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DOI: https://doi.org/10.1038/84594
