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Volumn 78, Issue 4, 2010, Pages 1781-1788

Broad-spectrum activity against bacterial mastitis pathogens and activation of mammary epithelial cells support a protective role of neutrophil cathelicidins in bovine mastitis

Author keywords

[No Author keywords available]

Indexed keywords

BOVINE MYELOID ANTIMICROBIAL PEPTIDE BMAP 27; BOVINE MYELOID ANTIMICROBIAL PEPTIDE BMAP 28; CATHELICIDIN; INDOLICIDIN; LIPOPOLYSACCHARIDE; PEPTIDE; PEPTIDE BAC5; POLYPEPTIDE ANTIBIOTIC AGENT; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

EID: 77950262727     PISSN: 00199567     EISSN: 10985522     Source Type: Journal    
DOI: 10.1128/IAI.01090-09     Document Type: Article
Times cited : (72)

References (57)
  • 2
    • 1042278913 scopus 로고    scopus 로고
    • In vitro and in vivo antimicrobial activity of two alpha-helical cathelicidin peptides and of their synthetic analogs
    • Benincasa, M., B. Skerlavaj, R. Gennaro, A. Pellegrini, and M. Zanetti. 2003. In vitro and in vivo antimicrobial activity of two alpha-helical cathelicidin peptides and of their synthetic analogs. Peptides 24:1723-1731
    • (2003) Peptides , vol.24 , pp. 1723-1731
    • Benincasa, M.1    Skerlavaj, B.2    Gennaro, R.3    Pellegrini, A.4    Zanetti, M.5
  • 3
    • 57749201362 scopus 로고    scopus 로고
    • Quantification of bovine casein fractions by direct chromatographic analysis of milk. Approaching the application to a real production context
    • Bonizzi, I., J. N. Buffoni, and M. Feligini. 2009. Quantification of bovine casein fractions by direct chromatographic analysis of milk. Approaching the application to a real production context. J. Chromatogr. A 1216:165-168
    • (2009) J. Chromatogr. A , vol.1216 , pp. 165-168
    • Bonizzi, I.1    Buffoni, J.N.2    Feligini, M.3
  • 4
    • 18244366046 scopus 로고    scopus 로고
    • Immunomodulatory activities of small host defense peptides. Antimicrob
    • Bowdish, D. M., D. J. Davidson, M. G. Scott, and R. E. Hancock. 2005. Immunomodulatory activities of small host defense peptides. Antimicrob. Agents Chemother. 49:1727-1732
    • (2005) Agents Chemother. , vol.49 , pp. 1727-1732
    • Bowdish, D.M.1    Davidson, D.J.2    Scott, M.G.3    Hancock, R.E.4
  • 5
    • 36448937856 scopus 로고    scopus 로고
    • Antimicrobial activity of bovine bactericidal permeability-increasing protein-derived peptides against gram-negative bacteria isolated from the milk of cows with clinical mastitis
    • Chockalingam, A., D. S. Zarlenga, and D. D. Bannerman. 2007. Antimicrobial activity of bovine bactericidal permeability-increasing protein-derived peptides against gram-negative bacteria isolated from the milk of cows with clinical mastitis. Am. J. Vet. Res. 68:1151-1159
    • (2007) Am. J. Vet. Res. , vol.68 , pp. 1151-1159
    • Chockalingam, A.1    Zarlenga, D.S.2    Bannerman, D.D.3
  • 9
    • 0036214967 scopus 로고    scopus 로고
    • Intracellular targets of antibacterial peptides
    • Cudic, M., and L. Otvos, Jr. 2002. Intracellular targets of antibacterial peptides. Curr. Drug Targets 3:101-106
    • (2002) Curr. Drug Targets , vol.3 , pp. 101-106
    • Cudic, M.1    Otvos Jr., L.2
  • 10
    • 0025811874 scopus 로고
    • Tracheal antimicrobial peptide, a cysteine-rich peptide from mammalian tracheal mucosa: Peptide isolation and cloning of a cDNA
    • Diamond, G., M. Zasloff, H. Eck, M. Brasseur, W. L. Maloy, and C. L. Bevins. 1991. Tracheal antimicrobial peptide, a cysteine-rich peptide from mammalian tracheal mucosa: peptide isolation and cloning of a cDNA. Proc. Natl. Acad. Sci. U. S. A. 88:3952-3956
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 3952-3956
    • Diamond, G.1    Zasloff, M.2    Eck, H.3    Brasseur, M.4    Maloy, W.L.5    Bevins, C.L.6
  • 11
    • 52249108453 scopus 로고    scopus 로고
    • Identification of novel host defense peptides and the absence of alpha-defensins in the bovine genome
    • Fjell, C. D., H. Jenssen, P. Fries, P. Aich, P. Griebel, K. Hilpert, R. E. Hancock, and A. Cherkasov. 2008. Identification of novel host defense peptides and the absence of alpha-defensins in the bovine genome. Proteins 73:420-430
    • (2008) Proteins , vol.73 , pp. 420-430
    • Fjell, C.D.1    Jenssen, H.2    Fries, P.3    Aich, P.4    Griebel, P.5    Hilpert, K.6    Hancock, R.E.7    Cherkasov, A.8
  • 12
    • 0035968224 scopus 로고    scopus 로고
    • Structure and mechanism of action of an indolicidin peptide derivative with improved activity against gram-positive bacteria
    • Friedrich, C. L., A. Rozek, A. Patrzykat, and R. E. Hancock. 2001. Structure and mechanism of action of an indolicidin peptide derivative with improved activity against gram-positive bacteria. J. Biol. Chem. 276:24015-24022
    • (2001) J. Biol. Chem. , vol.276 , pp. 24015-24022
    • Friedrich, C.L.1    Rozek, A.2    Patrzykat, A.3    Hancock, R.E.4
  • 13
    • 16844377323 scopus 로고    scopus 로고
    • Defensins and other antimicrobial peptides: A historical perspective and an update
    • Ganz, T. 2005. Defensins and other antimicrobial peptides: a historical perspective and an update. Comb. Chem. High Throughput Screen. 8:209-217
    • (2005) Comb. Chem. High Throughput Screen , vol.8 , pp. 209-217
    • Ganz, T.1
  • 14
    • 0036252094 scopus 로고    scopus 로고
    • Pro-rich antimicrobial peptides from animals: Structure, biological functions and mechanism of action
    • Gennaro, R., M. Zanetti, M. Benincasa, E. Podda, and M. Miani. 2002. Pro-rich antimicrobial peptides from animals: structure, biological functions and mechanism of action. Curr. Pharm. Des. 8:763-778
    • (2002) Curr. Pharm. Des. , vol.8 , pp. 763-778
    • Gennaro, R.1    Zanetti, M.2    Benincasa, M.3    Podda, E.4    Miani, M.5
  • 16
    • 70350314139 scopus 로고    scopus 로고
    • Isolation of caseins from whey proteins by microfiltration modifying the mineral balance in skim milk
    • Hernandez, A., and F. M. Harte. 2009. Isolation of caseins from whey proteins by microfiltration modifying the mineral balance in skim milk. J. Dairy Sci. 92:5357-5362
    • (2009) J. Dairy Sci. , vol.92 , pp. 5357-5362
    • Hernandez, A.1    Harte, F.M.2
  • 18
    • 2442542389 scopus 로고    scopus 로고
    • Mammary expression of new genes to combat mastitis
    • Kerr, D. E., and O. Wellnitz. 2003. Mammary expression of new genes to combat mastitis. J. Anim. Sci. 81(Suppl 3):38-47
    • (2003) J. Anim. Sci. , vol.81 , Issue.SUPPL. 3 , pp. 38-47
    • Kerr, D.E.1    Wellnitz, O.2
  • 19
    • 68349103189 scopus 로고    scopus 로고
    • Effect of milk on antibacterial activity of tetracycline against Escherichia coli and Staphylococcus aureus isolated from bovine mastitis
    • Kuang, Y., H. Jia, K. Miyanaga, and Y. Tanji. 2009. Effect of milk on antibacterial activity of tetracycline against Escherichia coli and Staphylococcus aureus isolated from bovine mastitis. Appl. Microbiol. Biotechnol. 84:135-142
    • (2009) Appl. Microbiol. Biotechnol. , vol.84 , pp. 135-142
    • Kuang, Y.1    Jia, H.2    Miyanaga, K.3    Tanji, Y.4
  • 20
    • 61349169039 scopus 로고    scopus 로고
    • AMPed up immunity: How antimicrobial peptides have multiple roles in immune defense
    • Lai, Y., and R. L. Gallo. 2009. AMPed up immunity: how antimicrobial peptides have multiple roles in immune defense. Trends Immunol. 30:131-141
    • (2009) Trends Immunol. , vol.30 , pp. 131-141
    • Lai, Y.1    Gallo, R.L.2
  • 21
    • 33646200337 scopus 로고    scopus 로고
    • Characterization of cytokine expression in milk somatic cells during intramammary infections with Escherichia coli or Staphylococcus aureus by realtime PCR
    • Lee, J. W., D. D. Bannerman, M. J. Paape, M. K. Huang, and X. Zhao. 2006. Characterization of cytokine expression in milk somatic cells during intramammary infections with Escherichia coli or Staphylococcus aureus by realtime PCR. Vet. Res. 37:219-229
    • (2006) Vet. Res. , vol.37 , pp. 219-229
    • Lee, J.W.1    Bannerman, D.D.2    Paape, M.J.3    Huang, M.K.4    Zhao, X.5
  • 22
    • 7644238048 scopus 로고    scopus 로고
    • Antimicrobial proteins and peptides: Anti-infective molecules of mammalian leukocytes
    • Levy, O. 2004. Antimicrobial proteins and peptides: anti-infective molecules of mammalian leukocytes. J. Leukoc. Biol. 76:909-925
    • (2004) J. Leukoc. Biol. , vol.76 , pp. 909-925
    • Levy, O.1
  • 25
    • 33847762328 scopus 로고    scopus 로고
    • Effect of corticosteroids and neuropeptides on the expression of defensins in bovine tracheal epithelial cells
    • Mitchell, G. B., M. H. Al-Haddawi, M. E. Clark, J. D. Beveridge, and J. L. Caswell. 2007. Effect of corticosteroids and neuropeptides on the expression of defensins in bovine tracheal epithelial cells. Infect. Immun. 75:1325-1334
    • (2007) Infect. Immun. , vol.75 , pp. 1325-1334
    • Mitchell, G.B.1    Al-Haddawi, M.H.2    Clark, M.E.3    Beveridge, J.D.4    Caswell, J.L.5
  • 26
    • 59849118467 scopus 로고    scopus 로고
    • Primate cathelicidin orthologues display different structures and membrane interactions
    • Morgera, F., L. Vaccari, N. Antcheva, D. Scaini, S. Pacor, and A. Tossi. 2009. Primate cathelicidin orthologues display different structures and membrane interactions. Biochem. J. 417:727-735
    • (2009) Biochem. J. , vol.417 , pp. 727-735
    • Morgera, F.1    Vaccari, L.2    Antcheva, N.3    Scaini, D.4    Pacor, S.5    Tossi, A.6
  • 27
    • 0038601510 scopus 로고    scopus 로고
    • Synergy, antagonism, and what the chequerboard puts between them
    • Odds, F. C. 2003. Synergy, antagonism, and what the chequerboard puts between them. J. Antimicrob. Chemother. 52:1
    • (2003) J. Antimicrob. Chemother. , vol.52 , pp. 1
    • Odds, F.C.1
  • 29
    • 0035038578 scopus 로고    scopus 로고
    • Synergy of histone-derived peptides of coho salmon with lysozyme and flounder pleurocidin
    • Patrzykat, A., L. Zhang, V. Mendoza, G. K. Iwama, and R. E. Hancock. 2001. Synergy of histone-derived peptides of coho salmon with lysozyme and flounder pleurocidin. Antimicrob. Agents Chemother. 45:1337-1342
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 1337-1342
    • Patrzykat, A.1    Zhang, L.2    Mendoza, V.3    Iwama, G.K.4    Hancock, R.E.5
  • 31
    • 48749128095 scopus 로고    scopus 로고
    • Mechanism and fitness costs of PR-39 resistance in Salmonella enterica serovar Typhimurium LT2
    • Pranting, M., A. Negrea, M. Rhen, and D. I. Andersson. 2008. Mechanism and fitness costs of PR-39 resistance in Salmonella enterica serovar Typhimurium LT2. Antimicrob. Agents Chemother. 52:2734-2741
    • (2008) Antimicrob. Agents Chemother. , vol.52 , pp. 2734-2741
    • Pranting, M.1    Negrea, A.2    Rhen, M.3    Andersson, D.I.4
  • 32
    • 2442538316 scopus 로고    scopus 로고
    • Primary structure and in vitro antibacterial properties of the Drosophila melanogaster attacin C Pro-domain
    • Rabel, D., M. Charlet, L. Ehret-Sabatier, L. Cavicchioli, M. Cudic, L. Otvos, Jr., and P. Bulet. 2004. Primary structure and in vitro antibacterial properties of the Drosophila melanogaster attacin C Pro-domain. J. Biol. Chem. 279:14853-14859
    • (2004) J. Biol. Chem. , vol.279 , pp. 14853-14859
    • Rabel, D.1    Charlet, M.2    Ehret-Sabatier, L.3    Cavicchioli, L.4    Cudic, M.5    Otvos Jr., L.6    Bulet, P.7
  • 33
    • 0034241772 scopus 로고    scopus 로고
    • Phagocytosis and killing of Staphylococcus aureus by bovine neutrophils after priming by tumor necrosis factor-alpha and the des-arginine derivative of C5a
    • Rainard, P., C. Riollet, B. Poutrel, and M. J. Paape. 2000. Phagocytosis and killing of Staphylococcus aureus by bovine neutrophils after priming by tumor necrosis factor-alpha and the des-arginine derivative of C5a. Am. J. Vet. Res. 61:951-959
    • (2000) Am. J. Vet. Res. , vol.61 , pp. 951-959
    • Rainard, P.1    Riollet, C.2    Poutrel, B.3    Paape, M.J.4
  • 34
    • 10944258717 scopus 로고    scopus 로고
    • Bovine beta-defensins: Identification and characterization of novel bovine beta-defensin genes and their expression in mammary gland tissue
    • Roosen, S., K. Exner, S. Paul, J. M. Schroder, E. Kalm, and C. Looft. 2004. Bovine beta-defensins: identification and characterization of novel bovine beta-defensin genes and their expression in mammary gland tissue. Mamm. Genome 15:834-842
    • (2004) Mamm. Genome , vol.15 , pp. 834-842
    • Roosen, S.1    Exner, K.2    Paul, S.3    Schroder, J.M.4    Kalm, E.5    Looft, C.6
  • 35
    • 0028902757 scopus 로고
    • Epithelial antibiotics induced at sites of inflammation
    • Schonwetter, B. S., E. D. Stolzenberg, and M. A. Zasloff. 1995. Epithelial antibiotics induced at sites of inflammation. Science 267:1645-1648
    • (1995) Science , vol.267 , pp. 1645-1648
    • Schonwetter, B.S.1    Stolzenberg, E.D.2    Zasloff, M.A.3
  • 36
    • 0242608441 scopus 로고    scopus 로고
    • Production effects related to mastitis and mastitis economics in dairy cattle herds
    • Seegers, H., C. Fourichon, and F. Beaudeau. 2003. Production effects related to mastitis and mastitis economics in dairy cattle herds. Vet. Res. 34:475-491
    • (2003) Vet. Res. , vol.34 , pp. 475-491
    • Seegers, H.1    Fourichon, C.2    Beaudeau, F.3
  • 37
    • 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
  • 38
    • 0029961492 scopus 로고    scopus 로고
    • Biological characterization of two novel cathelicidin-derived peptides and identification of structural requirements for their antimicrobial and cell lytic activities
    • Skerlavaj, B., R. Gennaro, L. Bagella, L. Merluzzi, A. Risso, and M. Zanetti. 1996. Biological characterization of two novel cathelicidin-derived peptides and identification of structural requirements for their antimicrobial and cell lytic activities. J. Biol. Chem. 271:28375-28381
    • (1996) J. Biol. Chem. , vol.271 , pp. 28375-28381
    • Skerlavaj, B.1    Gennaro, R.2    Bagella, L.3    Merluzzi, L.4    Risso, A.5    Zanetti, M.6
  • 40
    • 20444465568 scopus 로고    scopus 로고
    • Lipopolysaccharide and lipoteichoic acid induce different innate immune responses in bovine mammary epithelial cells
    • Strandberg, Y., C. Gray, T. Vuocolo, L. Donaldson, M. Broadway, and R. Tellam. 2005. Lipopolysaccharide and lipoteichoic acid induce different innate immune responses in bovine mammary epithelial cells. Cytokine 31:72-86
    • (2005) Cytokine , vol.31 , pp. 72-86
    • Strandberg, Y.1    Gray, C.2    Vuocolo, T.3    Donaldson, L.4    Broadway, M.5    Tellam, R.6
  • 41
    • 0032031434 scopus 로고    scopus 로고
    • Mechanism of antimicrobial action of indolicidin
    • Subbalakshmi, C., and N. Sitaram. 1998. Mechanism of antimicrobial action of indolicidin. FEMS Microbiol. Lett. 160:91-96
    • (1998) FEMS Microbiol. Lett. , vol.160 , pp. 91-96
    • Subbalakshmi, C.1    Sitaram, N.2
  • 42
    • 9244261939 scopus 로고    scopus 로고
    • Expression of a beta-defensin mRNA, lingual antimicrobial peptide, in bovine mammary epithelial tissue is induced by mastitis
    • Swanson, K., S. Gorodetsky, L. Good, S. Davis, D. Musgrave, K. Stelwagen, V. Farr, and A. Molenaar. 2004. Expression of a beta-defensin mRNA, lingual antimicrobial peptide, in bovine mammary epithelial tissue is induced by mastitis. Infect. Immun. 72:7311-7314
    • (2004) Infect. Immun. , vol.72 , pp. 7311-7314
    • Swanson, K.1    Gorodetsky, S.2    Good, L.3    Davis, S.4    Musgrave, D.5    Stelwagen, K.6    Farr, V.7    Molenaar, A.8
  • 43
    • 58349119593 scopus 로고    scopus 로고
    • Transcriptome profiling of Streptococcus uberis-induced mastitis reveals fundamental differences between immune gene expression in the mammary gland and in a primary cell culture model
    • Swanson, K. M., K. Stelwagen, J. Dobson, H. V. Henderson, S. R. Davis, V. C. Farr, and K. Singh. 2009. Transcriptome profiling of Streptococcus uberis-induced mastitis reveals fundamental differences between immune gene expression in the mammary gland and in a primary cell culture model. J. Dairy Sci. 92:117-129
    • (2009) J. Dairy Sci. , vol.92 , pp. 117-129
    • Swanson, K.M.1    Stelwagen, K.2    Dobson, J.3    Henderson, H.V.4    Davis, S.R.5    Farr, V.C.6    Singh, K.7
  • 46
    • 0036855464 scopus 로고    scopus 로고
    • Inducible expression of an antimicrobial peptide of the innate immunity in polymorphonuclear leukocytes
    • Tomasinsig, L., M. Scocchi, C. Di Loreto, D. Artico, and M. Zanetti. 2002. Inducible expression of an antimicrobial peptide of the innate immunity in polymorphonuclear leukocytes. J. Leukoc. Biol. 72:1003-1010
    • (2002) J. Leukoc. Biol. , vol.72 , pp. 1003-1010
    • Tomasinsig, L.1    Scocchi, M.2    Di Loreto, C.3    Artico, D.4    Zanetti, M.5
  • 47
    • 33644856596 scopus 로고    scopus 로고
    • Mechanistic and functional studies of the interaction of a proline-rich antimicrobial peptide with mammalian cells
    • Tomasinsig, L., B. Skerlavaj, N. Papo, B. Giabbai, Y. Shai, and M. Zanetti. 2006. Mechanistic and functional studies of the interaction of a proline-rich antimicrobial peptide with mammalian cells. J. Biol. Chem. 281:383-391
    • (2006) J. Biol. Chem. , vol.281 , pp. 383-391
    • Tomasinsig, L.1    Skerlavaj, B.2    Papo, N.3    Giabbai, B.4    Shai, Y.5    Zanetti, M.6
  • 48
    • 13844322065 scopus 로고    scopus 로고
    • The cathelicidins - Structure, function and evolution
    • Tomasinsig, L., and M. Zanetti. 2005. The cathelicidins - structure, function and evolution. Curr. Protein Pept. Sci. 6:23-34
    • (2005) Curr. Protein Pept. Sci. , vol.6 , pp. 23-34
    • Tomasinsig, L.1    Zanetti, M.2
  • 49
    • 0033864862 scopus 로고    scopus 로고
    • Amphipathic, alpha-helical antimicrobial peptides
    • Tossi, A., L. Sandri, and A. Giangaspero. 2000. Amphipathic, alpha-helical antimicrobial peptides. Biopolymers 55:4-30
    • (2000) Biopolymers , vol.55 , pp. 4-30
    • Tossi, A.1    Sandri, L.2    Giangaspero, A.3
  • 50
    • 0001479670 scopus 로고
    • A simple ultraviolet spectrophotometric method for the determination of protein
    • Waddell, W. J. 1956. A simple ultraviolet spectrophotometric method for the determination of protein. J. Lab. Clin. Med. 48:311-314
    • (1956) J. Lab. Clin. Med. , vol.48 , pp. 311-314
    • Waddell, W.J.1
  • 51
    • 0842326097 scopus 로고    scopus 로고
    • Cathelicidins, multifunctional peptides of the innate immunity
    • Zanetti, M. 2004. Cathelicidins, multifunctional peptides of the innate immunity. J. Leukoc. Biol. 75:39-48
    • (2004) J. Leukoc. Biol. , vol.75 , pp. 39-48
    • Zanetti, M.1
  • 52
    • 22944458199 scopus 로고    scopus 로고
    • The role of cathelicidins in the innate host defenses of mammals
    • Zanetti, M. 2005. The role of cathelicidins in the innate host defenses of mammals. Curr. Issues Mol. Biol. 7:179-196
    • (2005) Curr. Issues Mol. Biol. , vol.7 , pp. 179-196
    • Zanetti, M.1
  • 53
    • 0028844134 scopus 로고
    • Cathelicidins: A novel protein family with a common proregion and a variable C-terminal antimicrobial domain
    • Zanetti, M., R. Gennaro, and D. Romeo. 1995. Cathelicidins: a novel protein family with a common proregion and a variable C-terminal antimicrobial domain. FEBS Lett. 374:1-5
    • (1995) FEBS Lett. , vol.374 , pp. 1-5
    • Zanetti, M.1    Gennaro, R.2    Romeo, D.3
  • 54
    • 0025953533 scopus 로고
    • Stimulus-induced maturation of probactenecins, precursors of neutrophil antimicrobial polypeptides
    • Zanetti, M., L. Litteri, G. Griffiths, R. Gennaro, and D. Romeo. 1991. Stimulus-induced maturation of probactenecins, precursors of neutrophil antimicrobial polypeptides. J. Immunol. 146:4295-4300
    • (1991) J. Immunol. , vol.146 , pp. 4295-4300
    • Zanetti, M.1    Litteri, L.2    Griffiths, G.3    Gennaro, R.4    Romeo, D.5
  • 55
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff, M. 2002. Antimicrobial peptides of multicellular organisms. Nature 415:389-395
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 56
    • 33746014692 scopus 로고    scopus 로고
    • Evolution of the primate cathelicidin. Correlation between structural variations and antimicrobial activity
    • Zelezetsky, I., A. Pontillo, L. Puzzi, N. Antcheva, L. Segat, S. Pacor, S. Crovella, and A. Tossi. 2006. Evolution of the primate cathelicidin. Correlation between structural variations and antimicrobial activity. J. Biol. Chem. 281:19861-19871
    • (2006) J. Biol. Chem. , vol.281 , pp. 19861-19871
    • Zelezetsky, I.1    Pontillo, A.2    Puzzi, L.3    Antcheva, N.4    Segat, L.5    Pacor, S.6    Crovella, S.7    Tossi, A.8
  • 57
    • 52149109984 scopus 로고    scopus 로고
    • Mammary tissue damage during bovine mastitis: Causes and control
    • Zhao, X., and P. Lacasse. 2008. Mammary tissue damage during bovine mastitis: causes and control. J. Anim. Sci. 86:57-65
    • (2008) J. Anim. Sci. , vol.86 , pp. 57-65
    • Zhao, X.1    Lacasse, P.2


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