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Volumn 53, Issue 11, 2009, Pages 4647-4655

Primary structure and antibacterial activity of chicken bone marrow-derived β-defensins

Author keywords

[No Author keywords available]

Indexed keywords

BETA DEFENSIN; BETA DEFENSIN 1; BETA DEFENSIN 2; BETA DEFENSIN 7; UNCLASSIFIED DRUG;

EID: 70350279553     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.00301-09     Document Type: Article
Times cited : (44)

References (45)
  • 1
    • 0030842920 scopus 로고    scopus 로고
    • SEF17 fimbriae are essential for the convoluted colonial morphology of Salmonella Enteritidis
    • Allen-Vercoe, E., M. Dibb-Fuller, C. J. Thorns, and M. J. Woodward. 1997. SEF17 fimbriae are essential for the convoluted colonial morphology of Salmonella Enteritidis. FEMS Microbiol. Lett. 153:33-42.
    • (1997) FEMS Microbiol. Lett. , vol.153 , pp. 33-42
    • Allen-Vercoe, E.1    Dibb-Fuller, M.2    Thorns, C.J.3    Woodward, M.J.4
  • 2
    • 45749116474 scopus 로고    scopus 로고
    • Computational analysis suggests beta-defensins are processed to mature peptides by signal peptidase
    • Beckloff, N., and G. Diamond. 2008. Computational analysis suggests beta-defensins are processed to mature peptides by signal peptidase. Protein Pept. Lett. 15:536-540.
    • (2008) Protein Pept. Lett. , vol.15 , pp. 536-540
    • Beckloff, N.1    Diamond, G.2
  • 3
    • 0031694275 scopus 로고    scopus 로고
    • Characterization of beta-defensin prepropeptide mRNA from chicken and turkey bone marrow
    • Brockus, C. W., M. W. Jackwood, and B. G. Harmon. 1998. Characterization of beta-defensin prepropeptide mRNA from chicken and turkey bone marrow. Anim. Genet. 29:283-289.
    • (1998) Anim. Genet. , vol.29 , pp. 283-289
    • Brockus, C.W.1    Jackwood, M.W.2    Harmon, B.G.3
  • 4
    • 33748988741 scopus 로고    scopus 로고
    • Tryptophan- and arginine-rich antimicrobial peptides: Structures and mechanisms of action
    • Chan, D. I., E. J. Prenner, and H. J. Vogel. 2006. Tryptophan- and arginine-rich antimicrobial peptides: structures and mechanisms of action. Biochim. Biophys. Acta 1758:1184-1202.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1184-1202
    • Chan, D.I.1    Prenner, E.J.2    Vogel, H.J.3
  • 5
    • 67349178319 scopus 로고    scopus 로고
    • Differential modulation of beta-defensin gene expression by Salmonella Enteritidis in intestinal epithelial cells from resistant and susceptible chicken inbred lines
    • Derache, C., E. Esnault, C. Bonsergent, Y. Le Vern, P. Quéré, and A. Lalmanach. 2009. Differential modulation of beta-defensin gene expression by Salmonella Enteritidis in intestinal epithelial cells from resistant and susceptible chicken inbred lines. Dev. Comp. Immunol. 33:959-966.
    • (2009) Dev. Comp. Immunol. , vol.33 , pp. 959-966
    • Derache, C.1    Esnault, E.2    Bonsergent, C.3    Le Vern, Y.4    Quéré, P.5    Lalmanach, A.6
  • 6
    • 0030692830 scopus 로고    scopus 로고
    • Penaeidins, a new family of antimicrobial peptides isolated from the shrimp Penaeus vannamei (Decapoda)
    • DOI 10.1074/jbc.272.45.28398
    • Destoumieux, D., P. Bulet, D. Loew, A. Van Dorsselaer, J. Rodriguez, and E. Bachère. 1997. Penaeidins, a new family of antimicrobial peptides isolated from the shrimp penaeus vannamei (decapoda). J. Biol. Chem. 272:28398-28406. (Pubitemid 27517786)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.45 , pp. 28398-28406
    • Destoumieux, D.1    Bulet, P.2    Loew, D.3    Van Dorsselaer, A.4    Rodriguez, J.5    Bachere, E.6
  • 7
  • 9
    • 63249132178 scopus 로고    scopus 로고
    • Direct screening identifies mature {beta}-defensin 2 in avian heterophils
    • Kannan, L., N. C. Rath, R. Liyanage, and J. O. J. Lay. 2009. Direct screening identifies mature {beta}-defensin 2 in avian heterophils. Poult. Sci. 88:372-379.
    • (2009) Poult. Sci. , vol.88 , pp. 372-379
    • Kannan, L.1    Rath, N.C.2    Liyanage, R.3    Lay, J.O.J.4
  • 11
    • 3142779216 scopus 로고    scopus 로고
    • Solution structure of spheniscin, a beta-defensin from the penguin stomach
    • Landon, C., C. Thouzeau, H. Labbe, P. Bulet, and F. Vovelle. 2004. Solution structure of spheniscin, a beta-defensin from the penguin stomach. J. Biol. Chem. 279:30433-30439.
    • (2004) J. Biol. Chem. , vol.279 , pp. 30433-30439
    • Landon, C.1    Thouzeau, C.2    Labbe, H.3    Bulet, P.4    Vovelle, F.5
  • 13
    • 0023944202 scopus 로고
    • Effects on electrophoretic mobility and antibacterial spectrum of removal of two residues from synthetic sarcotoxin IA and addition of the same residues to cecropin B
    • Li, Z. Q., R. B. Merrifield, I. A. Boman, and H. G. Boman. 1988. Effects on electrophoretic mobility and antibacterial spectrum of removal of two residues from synthetic sarcotoxin IA and addition of the same residues to cecropin B. FEBS Lett. 231:299-302.
    • (1988) FEBS Lett. , vol.231 , pp. 299-302
    • Li, Z.Q.1    Merrifield, R.B.2    Boman, I.A.3    Boman, H.G.4
  • 14
    • 0028898423 scopus 로고
    • The pro region of human neutrophil defensin contains a motif that is essential for normal subcellular sorting
    • Liu, L., and T. Ganz. 1995. The pro region of human neutrophil defensin contains a motif that is essential for normal subcellular sorting. Blood 85:1095-1103.
    • (1995) Blood , vol.85 , pp. 1095-1103
    • Liu, L.1    Ganz, T.2
  • 17
    • 0028829183 scopus 로고
    • Peptides as weapons against microorganisms in the chemical defense system of vertebrates
    • Nicolas, P., and A. Mor. 1995. Peptides as weapons against microorganisms in the chemical defense system of vertebrates. Annu. Rev. Microbiol. 49:277-304.
    • (1995) Annu. Rev. Microbiol. , vol.49 , pp. 277-304
    • Nicolas, P.1    Mor, A.2
  • 18
    • 1042278915 scopus 로고    scopus 로고
    • The relationship between peptide structure and antibacterial activity
    • DOI 10.1016/j.peptides.2003.08.023
    • Powers, J. S., and R. E. W. Hancock. 2003. The relationship between peptide structure and antibacterial activity. Peptides 24:1681-1691. (Pubitemid 38198075)
    • (2003) Peptides , vol.24 , Issue.11 , pp. 1681-1691
    • Powers, J.-P.S.1    Hancock, R.E.W.2
  • 20
    • 9144260149 scopus 로고    scopus 로고
    • Salmonella carrier state in chicken: Comparison of expression of immune response genes between susceptible and resistant animals
    • Sadeyen, J., J. Trotereau, P. Velge, J. Marly, C. Beaumont, P. A. Barrow, N. Bumstead, and A. Lalmanach. 2004. Salmonella carrier state in chicken: comparison of expression of immune response genes between susceptible and resistant animals. Microbes Infect. 6:1278-1286.
    • (2004) Microbes Infect. , vol.6 , pp. 1278-1286
    • Sadeyen, J.1    Trotereau, J.2    Velge, P.3    Marly, J.4    Beaumont, C.5    Barrow, P.A.6    Bumstead, N.7    Lalmanach, A.8
  • 21
    • 50849124123 scopus 로고    scopus 로고
    • Glutaminyl cyclases from animals and plants: A case of functionally convergent protein evolution
    • Schilling, S., C. Wasternack, and H. Demuth. 2008. Glutaminyl cyclases from animals and plants: a case of functionally convergent protein evolution. Biol. Chem. 389:983-991.
    • (2008) Biol. Chem. , vol.389 , pp. 983-991
    • Schilling, S.1    Wasternack, C.2    Demuth, H.3
  • 22
    • 0036030617 scopus 로고    scopus 로고
    • Proteinases of common pathogenic bacteria degrade and inactivate the antibacterial peptide LL-37
    • Schmidtchen, A., I. Frick, E. Andersson, H. Tapper, and L. Björck. 2002. Proteinases of common pathogenic bacteria degrade and inactivate the antibacterial peptide LL-37. Mol. Microbiol. 46:157-168.
    • (2002) Mol. Microbiol. , vol.46 , pp. 157-168
    • Schmidtchen, A.1    Frick, I.2    Andersson, E.3    Tapper, H.4    Björck, L.5
  • 23
    • 20644462344 scopus 로고    scopus 로고
    • Mammalian defensins in the antimicrobial immune response
    • Selsted, M. E., and A. J. Ouellette. 2005. Mammalian defensins in the antimicrobial immune response. Nat. Immunol. 6:551-557.
    • (2005) Nat. Immunol. , vol.6 , pp. 551-557
    • Selsted, M.E.1    Ouellette, A.J.2
  • 24
    • 0030036479 scopus 로고    scopus 로고
    • Purification, primary structures, and antibacterial activities of beta-defensins, a new family of antimicrobial peptides from bovine neutrophils
    • Selsted, M. E., Y. Q. Tang, W. L. Morris, P. A. McGuire, M. J. Novotny, W. Smith, A. H. Henschen, and J. S. Cullor. 1996. Purification, primary structures, and antibacterial activities of beta-defensins, a new family of antimicrobial peptides from bovine neutrophils. J. Biol. Chem. 271:16430.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16430
    • Selsted, M.E.1    Tang, Y.Q.2    Morris, W.L.3    McGuire, P.A.4    Novotny, M.J.5    Smith, W.6    Henschen, A.H.7    Cullor, J.S.8
  • 25
    • 0036800086 scopus 로고    scopus 로고
    • G-CSF is an essential regulator of neutrophil trafficking from the bone marrow to the blood
    • DOI 10.1016/S1074-7613(02)00424-7
    • Semerad, C. L., F. Liu, A. D. Gregory, K. Stumpf, and D. C. Link. 2002. G-CSF is an essential regulator of neutrophil trafficking from the bone marrow to the blood. Immunity 17:413-423. (Pubitemid 35223531)
    • (2002) Immunity , vol.17 , Issue.4 , pp. 413-423
    • Semerad, C.L.1    Liu, F.2    Gregory, A.D.3    Stumpf, K.4    Link, D.C.5
  • 26
    • 33845349732 scopus 로고    scopus 로고
    • The changing of the guard: Molecular diversity and rapid evolution of beta-defensins
    • Semple, C. A., P. Gautier, K. Taylor, and J. R. Dorin. 2006. The changing of the guard: molecular diversity and rapid evolution of beta-defensins. Mol. Divers. 10:575-584.
    • (2006) Mol. Divers. , vol.10 , pp. 575-584
    • Semple, C.A.1    Gautier, P.2    Taylor, K.3    Dorin, J.R.4
  • 28
    • 0037062560 scopus 로고    scopus 로고
    • Structural consequences of carboxyamidation of dermaseptin S3
    • Shalev, D. E., A. Mor, and I. Kustanovich. 2002. Structural consequences of carboxyamidation of dermaseptin S3. Biochemistry 41:7312-7317.
    • (2002) Biochemistry , vol.41 , pp. 7312-7317
    • Shalev, D.E.1    Mor, A.2    Kustanovich, I.3
  • 29
    • 0034721871 scopus 로고    scopus 로고
    • Isolation and characterization of gomesin, an 18-residue cysteine-rich defense peptide from the spider acanthoscurria gomesiana hemocytes with sequence similarities to horseshoe crab antimicrobial peptides of the tachyplesin family
    • Silva, P. I. J., S. Daffre, and P. Bulet. 2000. Isolation and characterization of gomesin, an 18-residue cysteine-rich defense peptide from the spider acanthoscurria gomesiana hemocytes with sequence similarities to horseshoe crab antimicrobial peptides of the tachyplesin family. J. Biol. Chem. 275:33464-33470.
    • (2000) J. Biol. Chem. , vol.275 , pp. 33464-33470
    • Silva, P.I.J.1    Daffre, S.2    Bulet, P.3
  • 30
    • 67349133120 scopus 로고    scopus 로고
    • Discovery of anas platyrhynchos avian beta-defensin 2 (apl-avbd2) with antibacterial and chemotactic functions
    • Soman, S. S., D. S. Arathy, and E. Sreekumar. 2009. Discovery of anas platyrhynchos avian beta-defensin 2 (apl-avbd2) with antibacterial and chemotactic functions. Mol. Immunol. 46:2029-2038.
    • (2009) Mol. Immunol. , vol.46 , pp. 2029-2038
    • Soman, S.S.1    Arathy, D.S.2    Sreekumar, E.3
  • 31
    • 0030623934 scopus 로고    scopus 로고
    • Designer assays for antimicrobial peptides. Disputing the "one-size-fits-all" theory
    • Steinberg, D. A., and R. I. Lehrer. 1997. Designer assays for antimicrobial peptides. Disputing the "one-size-fits-all" theory. Methods Mol. Biol. 78:169-186.
    • (1997) Methods Mol. Biol. , vol.78 , pp. 169-186
    • Steinberg, D.A.1    Lehrer, R.I.2
  • 32
    • 59749089160 scopus 로고    scopus 로고
    • Evaluation of strategies for improving proteolytic resistance of antimicrobial peptides by using variants of EFK17, an internal segment of LL-37
    • Strömstedt, A. A., M. Pasupuleti, A. Schmidtchen, and M. Malmsten. 2009. Evaluation of strategies for improving proteolytic resistance of antimicrobial peptides by using variants of EFK17, an internal segment of LL-37. Antimicrob. Agents Chemother. 53:593-602.
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 593-602
    • Strömstedt, A.A.1    Pasupuleti, M.2    Schmidtchen, A.3    Malmsten, M.4
  • 33
    • 32644489098 scopus 로고    scopus 로고
    • Identification of three novel ostricacins: An update on the phylogenetic perspective of beta-defensins
    • Sugiarto, H., and P. Yu. 2006. Identification of three novel ostricacins: an update on the phylogenetic perspective of beta-defensins. Int. J. Antimicrob. Agents 27:229-235.
    • (2006) Int. J. Antimicrob. Agents , vol.27 , pp. 229-235
    • Sugiarto, H.1    Yu, P.2
  • 34
    • 33947131434 scopus 로고    scopus 로고
    • Mechanisms of action of ostrich beta-defensins against Escherichia coli
    • Sugiarto, H., and P. Yu. 2007. Mechanisms of action of ostrich beta-defensins against Escherichia coli. FEMS Microbiol. Lett. 270:195-200.
    • (2007) FEMS Microbiol. Lett. , vol.270 , pp. 195-200
    • Sugiarto, H.1    Yu, P.2
  • 35
    • 34250654522 scopus 로고    scopus 로고
    • Effects of cations on antimicrobial activity of ostricacins-1 and 2 on E. coli O157:H7 and S. aureus 1056MRSA
    • Sugiarto, H., and P. Yu. 2007. Effects of cations on antimicrobial activity of ostricacins-1 and 2 on E. coli O157:H7 and S. aureus 1056MRSA. Curr. Microbiol. 55:36-41.
    • (2007) Curr. Microbiol. , vol.55 , pp. 36-41
    • Sugiarto, H.1    Yu, P.2
  • 36
    • 0346435102 scopus 로고    scopus 로고
    • Spheniscins, avian beta-defensins in preserved stomach contents of the king penguin, Aptenodytes patagonicus
    • Thouzeau, C., Y. Le Maho, G. Froget, L. Sabatier, C. Le Bohec, J. A. Hoffmann, and P. Bulet. 2003. Spheniscins, avian beta-defensins in preserved stomach contents of the king penguin, Aptenodytes patagonicus. J. Biol. Chem. 278:51053-51058.
    • (2003) J. Biol. Chem. , vol.278 , pp. 51053-51058
    • Thouzeau, C.1    Le Maho, Y.2    Froget, G.3    Sabatier, L.4    Le Bohec, C.5    Hoffmann, J.A.6    Bulet, P.7
  • 37
    • 0026535104 scopus 로고
    • Posttranslational processing of defensins in immature human myeloid cells
    • Valore, E. V., and T. Ganz. 1992. Posttranslational processing of defensins in immature human myeloid cells. Blood 79:1538-1544.
    • (1992) Blood , vol.79 , pp. 1538-1544
    • Valore, E.V.1    Ganz, T.2
  • 39
    • 0029978338 scopus 로고    scopus 로고
    • Intramolecular inhibition of human defensin HNP-1 by its propiece
    • Valore, E. V., E. Martin, S. S. Harwig, and T. Ganz. 1996. Intramolecular inhibition of human defensin HNP-1 by its propiece. J. Clin. Investig. 97:1624-1629.
    • (1996) J. Clin. Investig. , vol.97 , pp. 1624-1629
    • Valore, E.V.1    Martin, E.2    Harwig, S.S.3    Ganz, T.4
  • 41
    • 33645967449 scopus 로고    scopus 로고
    • Identification of new immune induced molecules in the haemolymph of drosophila melanogaster by 2D-nanoLC MS/MS
    • Verleyen, P., G. Baggerman, W. D'Hertog, E. Vierstraete, S. J. Husson, and L. Schoofs. 2006. Identification of new immune induced molecules in the haemolymph of drosophila melanogaster by 2D-nanoLC MS/MS. J. Insect Physiol. 52:379-388.
    • (2006) J. Insect Physiol. , vol.52 , pp. 379-388
    • Verleyen, P.1    Baggerman, G.2    D'Hertog, W.3    Vierstraete, E.4    Husson, S.J.5    Schoofs, L.6
  • 42
    • 33749860977 scopus 로고    scopus 로고
    • Post-translational modifications in the context of therapeutic proteins
    • Walsh, G., and R. Jefferis. 2006. Post-translational modifications in the context of therapeutic proteins. Nat. Biotechnol. 24:1241-1252.
    • (2006) Nat. Biotechnol. , vol.24 , pp. 1241-1252
    • Walsh, G.1    Jefferis, R.2
  • 43
    • 9144261231 scopus 로고    scopus 로고
    • A genome-wide screen identifies a single β-defensin gene cluster in the chicken: Implications for the origin and evolution of mammalian defensins
    • DOI 10.1186/1471-2164-5-56
    • Xiao, Y., A. L. Hughes, J. Ando, Y. Matsuda, J. Cheng, D. Skinner-Noble, and G. Zhang. 2004. A genome-wide screen identifies a single beta-defensin gene cluster in the chicken: implications for the origin and evolution of mammalian defensins. BMC Genomics 5:56. (Pubitemid 39546661)
    • (2004) BMC Genomics , vol.5 , pp. 56
    • Xiao, Y.1    Hughes, A.L.2    Ando, J.3    Matsuda, Y.4    Cheng, J.-F.5    Skinner-Noble, D.6    Zhang, G.7
  • 44
    • 0036606951 scopus 로고    scopus 로고
    • Mammalian defensins in immunity: More than just microbicidal
    • DOI 10.1016/S1471-4906(02)02246-9, PII S1471490602022469
    • Yang, D., A. Biragyn, L. W. Kwak, and J. J. Oppenheim. 2002. Mammalian defensins in immunity: more than just microbicidal. Trends Immunol. 23:291-296. (Pubitemid 34628771)
    • (2002) Trends in Immunology , vol.23 , Issue.6 , pp. 291-296
    • Yang, D.1    Biragyn, A.2    Kwak, L.W.3    Oppenheim, J.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.