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Volumn 66, Issue 11, 2005, Pages 1922-1930

Effects of cecropin B transgene expression on Mannheimia haemolytica serotype 1 colonization of the nasal mucosa of calves

Author keywords

[No Author keywords available]

Indexed keywords

CECROPIN B; PLASMID DNA; POLYPEPTIDE ANTIBIOTIC AGENT;

EID: 30744448983     PISSN: 00029645     EISSN: None     Source Type: Journal    
DOI: 10.2460/ajvr.2005.66.1922     Document Type: Article
Times cited : (3)

References (45)
  • 1
    • 0024696490 scopus 로고
    • The evolution of vaccines for bovine pneumonic pasteurellosis
    • Mosier JW, Confer AW, Panciera RJ. The evolution of vaccines for bovine pneumonic pasteurellosis. Res Vet Sci 1989;47:1-10.
    • (1989) Res Vet Sci , vol.47 , pp. 1-10
    • Mosier, J.W.1    Confer, A.W.2    Panciera, R.J.3
  • 2
    • 30744436612 scopus 로고
    • Update: Bovine pneumonic pasteurellosis
    • Dalgleish R. Update: bovine pneumonic pasteurellosis. In Pract 1990;12:223-226.
    • (1990) Pract , vol.12 , pp. 223-226
    • Dalgleish, R.1
  • 3
    • 0000857007 scopus 로고
    • The role of Pasteurella haemolytica in the bovine respiratory disease complex
    • Frank GH. The role of Pasteurella haemolytica in the bovine respiratory disease complex. Vet Med 1986;81:838-846.
    • (1986) Vet Med , vol.81 , pp. 838-846
    • Frank, G.H.1
  • 4
    • 0022760311 scopus 로고
    • Colonization of the nasal passages of calves with Pasteurella haemolytica serotype 1 and regeneration of colonization after experimentally induced viral infection of the respiratory tract
    • Frank GH, Briggs RE, Gillette KG. Colonization of the nasal passages of calves with Pasteurella haemolytica serotype 1 and regeneration of colonization after experimentally induced viral infection of the respiratory tract. Am J Vet Res 1986;47:1704-1707.
    • (1986) Am J Vet Res , vol.47 , pp. 1704-1707
    • Frank, G.H.1    Briggs, R.E.2    Gillette, K.G.3
  • 5
    • 0026487901 scopus 로고
    • Pasteurella haemolytica A1 and bovine respiratory disease: Pathogenesis
    • Whiteley LO, Maheswaran SK, Weiss DJ, et al. Pasteurella haemolytica A1 and bovine respiratory disease: pathogenesis. J Vet Intern Med 1992;6:11-22.
    • (1992) J Vet Intern Med , vol.6 , pp. 11-22
    • Whiteley, L.O.1    Maheswaran, S.K.2    Weiss, D.J.3
  • 6
    • 0027732139 scopus 로고
    • Comparison between the minimal inhibitory concentration of tilmicosin and oxytetracycline for bovine pneumonic Pasteurella haemolytica isolates
    • Hartman EG, Geryl J. Comparison between the minimal inhibitory concentration of tilmicosin and oxytetracycline for bovine pneumonic Pasteurella haemolytica isolates. Vet Q 1993; 15:184.
    • (1993) Vet Q , vol.15 , pp. 184
    • Hartman, E.G.1    Geryl, J.2
  • 7
    • 0028069427 scopus 로고
    • A 4-year survey of antimicrobial susceptibility trends for isolates from cattle with bovine respiratory disease in North America
    • Watts JL, Yancey RJ, Salmon SA, et al. A 4-year survey of antimicrobial susceptibility trends for isolates from cattle with bovine respiratory disease in North America. J Clin Microbial 1994;32:725-731.
    • (1994) J Clin Microbial , vol.32 , pp. 725-731
    • Watts, J.L.1    Yancey, R.J.2    Salmon, S.A.3
  • 8
    • 0041429350 scopus 로고    scopus 로고
    • WHO advises kicking the livestock antibiotic habit
    • Ferber D. WHO advises kicking the livestock antibiotic habit. Science 2003;301:1027.
    • (2003) Science , vol.301 , pp. 1027
    • Ferber, D.1
  • 9
    • 0025778681 scopus 로고
    • Cell-free immunity in Cecropia. A model system for antibacterial proteins
    • Boman HG, Faye I, Gudmundson GH, et al. Cell-free immunity in Cecropia. A model system for antibacterial proteins. Eur J Biochem 1991;201:23-31.
    • (1991) Eur J Biochem , vol.201 , pp. 23-31
    • Boman, H.G.1    Faye, I.2    Gudmundson, G.H.3
  • 11
    • 0030746525 scopus 로고    scopus 로고
    • Effects of the anti-bacterial peptide cecropin B and its analogs, cecropins B-1 and B-2, on liposomes, bacteria, and cancer cells
    • Chen HM, Wang W, Smith D, et al. Effects of the anti-bacterial peptide cecropin B and its analogs, cecropins B-1 and B-2, on liposomes, bacteria, and cancer cells. Biochem Biophys Acta 1997; 1336:171-179.
    • (1997) Biochem Biophys Acta , vol.1336 , pp. 171-179
    • Chen, H.M.1    Wang, W.2    Smith, D.3
  • 12
    • 0023864293 scopus 로고
    • Binding and action of cecropin and cecropin analogues: Antibacterial peptides from insects
    • Steiner H, Andreu D, Merrifield RB. Binding and action of cecropin and cecropin analogues: antibacterial peptides from insects. Biochem Biophys Acta 1988;939:260-266.
    • (1988) Biochem Biophys Acta , vol.939 , pp. 260-266
    • Steiner, H.1    Andreu, D.2    Merrifield, R.B.3
  • 13
    • 0034840485 scopus 로고    scopus 로고
    • Effect of monodose intraperitoneal cecropins in experimental septic shock
    • Giacometti A, Cirioni O, Ghiselli R, et al. Effect of monodose intraperitoneal cecropins in experimental septic shock. Crit Care Med 2001;29:1666-1669.
    • (2001) Crit Care Med , vol.29 , pp. 1666-1669
    • Giacometti, A.1    Cirioni, O.2    Ghiselli, R.3
  • 14
    • 0042830450 scopus 로고    scopus 로고
    • Antibacterial peptides: Basic facts and emerging concepts
    • Boman HG. Antibacterial peptides: basic facts and emerging concepts. J Intern Med 2003;254:197-215.
    • (2003) J Intern Med , vol.254 , pp. 197-215
    • Boman, H.G.1
  • 15
    • 0032007854 scopus 로고    scopus 로고
    • Cationic peptides: A new source of antibiotics
    • Hancock RE, Lehrer R. Cationic peptides: a new source of antibiotics. Trends Biotechnol 1998;16:82-88.
    • (1998) Trends Biotechnol , vol.16 , pp. 82-88
    • Hancock, R.E.1    Lehrer, R.2
  • 16
    • 0027990232 scopus 로고
    • Ability of cecropin B to penetrate the enterobacterial outer membrane
    • Vaara M, Vaara T. Ability of cecropin B to penetrate the enterobacterial outer membrane. Antimicrob Agents Chemother 1994;38:2498-2501.
    • (1994) Antimicrob Agents Chemother , vol.38 , pp. 2498-2501
    • Vaara, M.1    Vaara, T.2
  • 17
    • 0036077853 scopus 로고    scopus 로고
    • Effect of cecropin B and a synthetic analogue on propagation of fish viruses in vitro
    • Chiou PP, Lin CM, Perez L, et al. Effect of cecropin B and a synthetic analogue on propagation of fish viruses in vitro. Mar Biotechnol (NY) 2002;4:294-302.
    • (2002) Mar Biotechnol (NY) , vol.4 , pp. 294-302
    • Chiou, P.P.1    Lin, C.M.2    Perez, L.3
  • 18
    • 30744441684 scopus 로고    scopus 로고
    • Transposon-based transformation vectors
    • Awarded February
    • Cooper RK. Transposon-based transformation vectors. Awarded February 1998. U. S. Patent No. 5,719,055.
    • (1998) U. S. Patent No. 5,719,055
    • Cooper, R.K.1
  • 19
    • 30744439618 scopus 로고    scopus 로고
    • Transformation of vertebrate cells with lytic peptide genes
    • 93A5. Awarded August
    • Cooper RK, Enright FM. Transformation of vertebrate cells with lytic peptide genes. 93A5. Awarded August 1996. U. S. Patent No. 5,556,782.
    • (1996) U. S. Patent No. 5,556,782
    • Cooper, R.K.1    Enright, F.M.2
  • 20
    • 0036069316 scopus 로고    scopus 로고
    • Enhanced bacterial disease resistance of transgenic channel catfish Ictalurus punctatus possessing cecropin genes
    • Dunham RA, Warr GW, Nichols A, et al. Enhanced bacterial disease resistance of transgenic channel catfish Ictalurus punctatus possessing cecropin genes. Mar Biotechnol (NY) 2002;4:338-344.
    • (2002) Mar Biotechnol (NY) , vol.4 , pp. 338-344
    • Dunham, R.A.1    Warr, G.W.2    Nichols, A.3
  • 21
    • 0029257202 scopus 로고
    • Expression of giant silk-moth cecropin B genes in tobacco
    • Florack D, Allefs S, Bollen R, et al. Expression of giant silk-moth cecropin B genes in tobacco. Transgenic Res 1995;4:132-141.
    • (1995) Transgenic Res , vol.4 , pp. 132-141
    • Florack, D.1    Allefs, S.2    Bollen, R.3
  • 22
    • 0036079373 scopus 로고    scopus 로고
    • Production of transgenic Medaka with increased resistance to bacterial pathogens
    • Sarmasik A, Warr G, Chen TT. Production of transgenic Medaka with increased resistance to bacterial pathogens. Mar Biotechnol (NY) 2002;4:310-322.
    • (2002) Mar Biotechnol (NY) , vol.4 , pp. 310-322
    • Sarmasik, A.1    Warr, G.2    Chen, T.T.3
  • 23
    • 0020367920 scopus 로고
    • Demonstration of age dependent capsular material on Pasteurella haemolytica serotype 1
    • Corstvet RE, Gentry MJ, Newman PR, et al. Demonstration of age dependent capsular material on Pasteurella haemolytica serotype 1. J Clin Microbiol 1982;16:1123-1126.
    • (1982) J Clin Microbiol , vol.16 , pp. 1123-1126
    • Corstvet, R.E.1    Gentry, M.J.2    Newman, P.R.3
  • 24
    • 0020046867 scopus 로고
    • Distribution of Pasteurella haemolytica and Pasteurella multocida in the bovine lung following vaccination and challenge exposure as an indicator of lung resistance
    • Newman PR, Corstvet RE, Panciera RJ. Distribution of Pasteurella haemolytica and Pasteurella multocida in the bovine lung following vaccination and challenge exposure as an indicator of lung resistance. Am J Vet Res 1982;43:417-422.
    • (1982) Am J Vet Res , vol.43 , pp. 417-422
    • Newman, P.R.1    Corstvet, R.E.2    Panciera, R.J.3
  • 25
    • 84957913750 scopus 로고    scopus 로고
    • Development of in vitro susceptibility testing criteria and quality control parameters
    • National Committee for Clinical Laboratory Standards (NCCLS). 2nd ed. Villanova, Pa: NCCLS
    • National Committee for Clinical Laboratory Standards (NCCLS). Development of in vitro susceptibility testing criteria and quality control parameters. Approved guideline M23-A2. 2nd ed. Villanova, Pa: NCCLS, 2001.
    • (2001) Approved Guideline M23-A2
  • 26
    • 0032091803 scopus 로고    scopus 로고
    • Antibody responses to Pasteurella haemolytica 1:A and three of its outer membrane proteins in serum, nasal secretions, and bronchoalveolar lavage fluid from calves
    • Brennan RE, Corstvet RE, Paulson DB. Antibody responses to Pasteurella haemolytica 1:A and three of its outer membrane proteins in serum, nasal secretions, and bronchoalveolar lavage fluid from calves. Am J Vet Res 1998;59:727-732.
    • (1998) Am J Vet Res , vol.59 , pp. 727-732
    • Brennan, R.E.1    Corstvet, R.E.2    Paulson, D.B.3
  • 27
    • 0026935563 scopus 로고
    • Systemic and pulmonary antibody responses of calves to Pasteurella haemolytica after intrapulmonary inoculation
    • McBride JW, Corstvet RE, Paulsen DB, et al. Systemic and pulmonary antibody responses of calves to Pasteurella haemolytica after intrapulmonary inoculation. Am J Vet Res 1992;53:1889-1894.
    • (1992) Am J Vet Res , vol.53 , pp. 1889-1894
    • McBride, J.W.1    Corstvet, R.E.2    Paulsen, D.B.3
  • 28
    • 0035850212 scopus 로고    scopus 로고
    • Evaluation of polyplexes as gene transfer agents
    • Gebhart CL, Kabanov AV. Evaluation of polyplexes as gene transfer agents. J Control Release 2001;73:401-416.
    • (2001) J Control Release , vol.73 , pp. 401-416
    • Gebhart, C.L.1    Kabanov, A.V.2
  • 29
    • 4243077669 scopus 로고    scopus 로고
    • Polyplexes and lipoplexes for mammalian gene delivery: From traditional to microarray screening
    • How SE, Yingyongnarongkul B, Fara MA, et al. Polyplexes and lipoplexes for mammalian gene delivery: from traditional to microarray screening. Comb Chem High Throughput Screen 2004;7:423-430.
    • (2004) Comb Chem High Throughput Screen , vol.7 , pp. 423-430
    • How, S.E.1    Yingyongnarongkul, B.2    Fara, M.A.3
  • 30
    • 0038793496 scopus 로고    scopus 로고
    • Synthesis of novel cationic lipids having polyamidoamine dendrons and their transfection activity
    • Takahasi T, Kono K, Itoh T, et al. Synthesis of novel cationic lipids having polyamidoamine dendrons and their transfection activity. Bioconjug Chem 2003;14:764-773.
    • (2003) Bioconjug Chem , vol.14 , pp. 764-773
    • Takahasi, T.1    Kono, K.2    Itoh, T.3
  • 31
    • 0030293017 scopus 로고    scopus 로고
    • In vitro gene delivery by degraded polyamidoamine dendrimers
    • Tang MX, Redemann Ct, Szoka FC Jr. In vitro gene delivery by degraded polyamidoamine dendrimers. Bioconjug Chem 1996;7:703-714.
    • (1996) Bioconjug Chem , vol.7 , pp. 703-714
    • Tang, M.X.1    Redemann, Ct.2    Szoka Jr., F.C.3
  • 32
    • 0034814129 scopus 로고    scopus 로고
    • Transfection of eastern oyster (Crassatrea virginica) embryos
    • Buchanan JT, Nickens AD, Cooper RK, et al. Transfection of eastern oyster (Crassatrea virginica) embryos. Mar Biotechnol (NY) 2001;3:322-335.
    • (2001) Mar Biotechnol (NY) , vol.3 , pp. 322-335
    • Buchanan, J.T.1    Nickens, A.D.2    Cooper, R.K.3
  • 33
    • 0032541317 scopus 로고    scopus 로고
    • Inducible expression of green fluorescent protein within channel catfish cells by a cecropin gene promoter
    • Zhang Q, Tiersch TR, Cooper RK. Inducible expression of green fluorescent protein within channel catfish cells by a cecropin gene promoter. Gene 1998;216:207-213.
    • (1998) Gene , vol.216 , pp. 207-213
    • Zhang, Q.1    Tiersch, T.R.2    Cooper, R.K.3
  • 34
    • 3042781052 scopus 로고    scopus 로고
    • Antimicrobial peptides: A natural alternative to chemical antibiotics and a potential for applied biotechnology
    • Available at: ejbiotechnology.info/content/vol6/issue3/abstract/1/index.html. Accessed Feb 22
    • Marshall SH, Arenas G. Antimicrobial peptides: a natural alternative to chemical antibiotics and a potential for applied biotechnology. Electronic J Biotech 2003;6. Available at: ejbiotechnology.info/content/vol6/issue3/abstract/1/index.html. Accessed Feb 22, 2004.
    • (2003) Electronic J Biotech , vol.6 , pp. 2004
    • Marshall, S.H.1    Arenas, G.2
  • 35
    • 0032459135 scopus 로고    scopus 로고
    • Origins and development of peptide antibiotic research. From extracts to abstracts to contracts
    • Spitznagel JK. Origins and development of peptide antibiotic research. From extracts to abstracts to contracts. Mol Biotechnol 1998;10:237-245.
    • (1998) Mol Biotechnol , vol.10 , pp. 237-245
    • Spitznagel, J.K.1
  • 36
    • 0024331982 scopus 로고
    • Antibacterial peptides from pig intestine: Isolation of a mammalian cecropin
    • Lee J, Boman A, Chuanxin S, et al. Antibacterial peptides from pig intestine: isolation of a mammalian cecropin. Proc Natl Acad Sci U S A 1989;86:9159-9162.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 9159-9162
    • Lee, J.1    Boman, A.2    Chuanxin, S.3
  • 37
    • 0028904007 scopus 로고
    • PMAP-37, a novel antibacterial peptide from pig myeloid cells. cDNA cloning, chemical synthesis and activity
    • Tossi A, Scocchi M, Zanetti M, et al. PMAP-37, a novel antibacterial peptide from pig myeloid cells. cDNA cloning, chemical synthesis and activity. Eur J Biochem 1995;228:941-946.
    • (1995) Eur J Biochem , vol.228 , pp. 941-946
    • Tossi, A.1    Scocchi, M.2    Zanetti, M.3
  • 38
    • 0031910574 scopus 로고    scopus 로고
    • Antibacterial peptides are present in chromaffin cell secretory granules
    • Metz-Boutigue MH, Goumon Y, Lugardon K, et al. Antibacterial peptides are present in chromaffin cell secretory granules. Cell Mol Neurobiol 1998;18:249-266.
    • (1998) Cell Mol Neurobiol , vol.18 , pp. 249-266
    • Metz-Boutigue, M.H.1    Goumon, Y.2    Lugardon, K.3
  • 39
    • 85047690831 scopus 로고
    • Processing of chromogranin B in bovine adrenal medulla. Identification of secretolytin, the endogenous C-terminal fragment of residues 614-626 with antibacterial activity
    • Strub JM, Garcia-Sablone P, Lonning K, et al. Processing of chromogranin B in bovine adrenal medulla. Identification of secretolytin, the endogenous C-terminal fragment of residues 614-626 with antibacterial activity. Eur J Biochem 1995;229:356-368.
    • (1995) Eur J Biochem , vol.229 , pp. 356-368
    • Strub, J.M.1    Garcia-Sablone, P.2    Lonning, K.3
  • 40
    • 0030031520 scopus 로고    scopus 로고
    • Antibacterial activity of secretolytin, a chromogranin B-derived peptide (614-626), is correlated with peptide structure
    • Strub JM, Hubert P, Nullans G, et al. Antibacterial activity of secretolytin, a chromogranin B-derived peptide (614-626), is correlated with peptide structure. FEBS Lett 1996;379:273-278.
    • (1996) FEBS Lett , vol.379 , pp. 273-278
    • Strub, J.M.1    Hubert, P.2    Nullans, G.3
  • 41
    • 0000433817 scopus 로고
    • When Pasteurella haemolytica colonizes the nasal passages of cattle
    • Frank GH. When Pasteurella haemolytica colonizes the nasal passages of cattle. Vet Med 1988;83:1060-1064.
    • (1988) Vet Med , vol.83 , pp. 1060-1064
    • Frank, G.H.1
  • 42
    • 0026847440 scopus 로고
    • Colonization of the tonsils of calves with Pasteurella haemolytica
    • Frank GH, Briggs RE. Colonization of the tonsils of calves with Pasteurella haemolytica. Am J Vet Res 1992;53:481-484.
    • (1992) Am J Vet Res , vol.53 , pp. 481-484
    • Frank, G.H.1    Briggs, R.E.2
  • 43
    • 0034721744 scopus 로고    scopus 로고
    • Transgenic expression of cecropin B, an antibacterial peptide from Bombyx mori, confers enhanced resistance to bacterial leaf blight in rice
    • Sharma A, Sharma R, Imamura M, et al. Transgenic expression of cecropin B, an antibacterial peptide from Bombyx mori, confers enhanced resistance to bacterial leaf blight in rice. FEBS Lett 2000;484:7-11.
    • (2000) FEBS Lett , vol.484 , pp. 7-11
    • Sharma, A.1    Sharma, R.2    Imamura, M.3
  • 44
    • 0025428223 scopus 로고
    • The effects of age, environmental temperature and relative humidity on the bacterial flora of the upper respiratory tract in calves
    • Woldehiwet Z, Mamache B, Rowan TG. The effects of age, environmental temperature and relative humidity on the bacterial flora of the upper respiratory tract in calves. Br Vet J 1990;146:211-218.
    • (1990) Br Vet J , vol.146 , pp. 211-218
    • Woldehiwet, Z.1    Mamache, B.2    Rowan, T.G.3
  • 45
    • 0014582028 scopus 로고
    • Nasal bacterial flora of calves in healthy and in pneumonia-prone herds
    • Magwood SE, Barnum DA, Thomson RG. Nasal bacterial flora of calves in healthy and in pneumonia-prone herds. Can J Comp Med 1969;33:237-243.
    • (1969) Can J Comp Med , vol.33 , pp. 237-243
    • Magwood, S.E.1    Barnum, D.A.2    Thomson, R.G.3


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