메뉴 건너뛰기




Volumn 6, Issue 8, 2011, Pages

Mytilus galloprovincialis myticin C: A chemotactic molecule with antiviral activity and immunoregulatory properties

Author keywords

[No Author keywords available]

Indexed keywords

ANTIVIRUS AGENT; CELL EXTRACT; COMPLEMENT COMPONENT C1Q; COMPLEMENT COMPONENT MGC1Q; COMPLEMENTARY DNA; LYSOZYME; MYTICIN B; MYTICIN C; MYTILIN; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG; ANTIMICROBIAL CATIONIC PEPTIDE; CHEMOTACTIC FACTOR; GREEN FLUORESCENT PROTEIN; IMMUNOLOGIC FACTOR; ISOPROTEIN; MESSENGER RNA; MYTICIN; PEPTIDE; PLASMA PROTEIN;

EID: 79961197723     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0023140     Document Type: Article
Times cited : (86)

References (56)
  • 1
    • 38349164517 scopus 로고    scopus 로고
    • In vivo modulation of the rainbow trout (Oncorhynchus mykiss) immune response by the human alpha defensin 1, HNP1
    • Falcó A, Brocal I, Pérez L, Coll JM, Estepa A, et al. (2008) In vivo modulation of the rainbow trout (Oncorhynchus mykiss) immune response by the human alpha defensin 1, HNP1. Fish Shellfish Immunol 24: 102-112.
    • (2008) Fish Shellfish Immunol , vol.24 , pp. 102-112
    • Falcó, A.1    Brocal, I.2    Pérez, L.3    Coll, J.M.4    Estepa, A.5
  • 2
    • 11344268155 scopus 로고    scopus 로고
    • Antimicrobial peptides: Cooperative approaches to protection
    • Patrzykat A, Douglas SE, (2005) Antimicrobial peptides: Cooperative approaches to protection. Protein Peptide Lett 12: 19-25.
    • (2005) Protein Peptide Lett , vol.12 , pp. 19-25
    • Patrzykat, A.1    Douglas, S.E.2
  • 3
    • 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
  • 4
    • 0142218765 scopus 로고    scopus 로고
    • Roles of antimicrobial peptides such as defensins in innate and adaptive immunity
    • Oppenheim JJ, Biragyn A, Kwak LW, Yang D, (2003) Roles of antimicrobial peptides such as defensins in innate and adaptive immunity. Ann Rheum Dis 62 (suppl 2): ii17-ii21.
    • (2003) Ann Rheum Dis , vol.62 , Issue.SUPPL. 2
    • Oppenheim, J.J.1    Biragyn, A.2    Kwak, L.W.3    Yang, D.4
  • 5
    • 33745698864 scopus 로고    scopus 로고
    • Defensins in innate antiviral immunity
    • Klotman ME, Chang TL, (2006) Defensins in innate antiviral immunity. Nat Rev Immunol 6: 447-456.
    • (2006) Nat Rev Immunol , vol.6 , pp. 447-456
    • Klotman, M.E.1    Chang, T.L.2
  • 6
    • 0036796983 scopus 로고    scopus 로고
    • Proteases in Escherichia coli and Staphylococcus aureus confer reduced susceptibility to lactoferricin B
    • Ulvatne H, Haukland HH, Samuelsen Ø, Krämer M, Vorland LH, (2002) Proteases in Escherichia coli and Staphylococcus aureus confer reduced susceptibility to lactoferricin B. J Antimicrob Chemother 50: 461-467.
    • (2002) J Antimicrob Chemother , vol.50 , pp. 461-467
    • Ulvatne, H.1    Haukland, H.H.2    Samuelsen Ø3    Krämer, M.4    Vorland, L.H.5
  • 7
    • 30044452344 scopus 로고    scopus 로고
    • Cationic host defense (antimicrobial) peptides
    • Brown KL, Hancock RE, (2006) Cationic host defense (antimicrobial) peptides. Curr Opin Immunol 18: 24-30.
    • (2006) Curr Opin Immunol , vol.18 , pp. 24-30
    • Brown, K.L.1    Hancock, R.E.2
  • 8
    • 0034098230 scopus 로고    scopus 로고
    • Mytilin B and MGD2, two antimicrobial peptides of marine mussels: gene structure and expression analysis
    • Mitta G, Hubert F, Dyrynda EA, Boudry P, Roch P, (2000) Mytilin B and MGD2, two antimicrobial peptides of marine mussels: gene structure and expression analysis. Dev Comp Immunol 24: 381-393.
    • (2000) Dev Comp Immunol , vol.24 , pp. 381-393
    • Mitta, G.1    Hubert, F.2    Dyrynda, E.A.3    Boudry, P.4    Roch, P.5
  • 9
    • 0033214630 scopus 로고    scopus 로고
    • Myticin, a novel cysteine-rich antimicrobial peptide isolated from haemocytes and plasma of the mussel Mytilus galloprovincialis
    • Mitta G, Hubert F, Noel T, Roch P, (1999) Myticin, a novel cysteine-rich antimicrobial peptide isolated from haemocytes and plasma of the mussel Mytilus galloprovincialis. Eur J Biochem 265: 71-78.
    • (1999) Eur J Biochem , vol.265 , pp. 71-78
    • Mitta, G.1    Hubert, F.2    Noel, T.3    Roch, P.4
  • 10
    • 36549038033 scopus 로고    scopus 로고
    • NMR structure of mussel mytilin, and antiviral-antibacterial activities of derived synthetic peptides
    • Roch P, Yang Y, Toubiana M, Aumelas A, (2008) NMR structure of mussel mytilin, and antiviral-antibacterial activities of derived synthetic peptides. Dev Comp Immunol 32: 227-238.
    • (2008) Dev Comp Immunol , vol.32 , pp. 227-238
    • Roch, P.1    Yang, Y.2    Toubiana, M.3    Aumelas, A.4
  • 11
    • 54849430925 scopus 로고    scopus 로고
    • Evidence of high individual diversity on myticin C in mussel (Mytilus galloprovincialis)
    • Costa MM, Dios S, Alonso-Gutiérrez J, Romero A, Novoa B, et al. (2009) Evidence of high individual diversity on myticin C in mussel (Mytilus galloprovincialis). Dev Comp Immunol 33: 162-170.
    • (2009) Dev Comp Immunol , vol.33 , pp. 162-170
    • Costa, M.M.1    Dios, S.2    Alonso-Gutiérrez, J.3    Romero, A.4    Novoa, B.5
  • 12
    • 36549039976 scopus 로고    scopus 로고
    • High sequence variability of myticin transcripts in hemocytes of immune-stimulated mussels suggests ancient host-pathogen interactions
    • Pallavicini A, Costa MM, Gestal C, Dreos R, Figueras A, et al. (2008) High sequence variability of myticin transcripts in hemocytes of immune-stimulated mussels suggests ancient host-pathogen interactions. Dev Comp Immunol 32: 213-226.
    • (2008) Dev Comp Immunol , vol.32 , pp. 213-226
    • Pallavicini, A.1    Costa, M.M.2    Gestal, C.3    Dreos, R.4    Figueras, A.5
  • 13
    • 44649102625 scopus 로고    scopus 로고
    • Molecular diversity and evolution of myticin-C antimicrobial peptide variants in the Mediterranean mussel, Mytilus galloprovincialis
    • Padhi A, Verghese B, (2008) Molecular diversity and evolution of myticin-C antimicrobial peptide variants in the Mediterranean mussel, Mytilus galloprovincialis. Peptides 29: 1094-1101.
    • (2008) Peptides , vol.29 , pp. 1094-1101
    • Padhi, A.1    Verghese, B.2
  • 14
    • 44749083354 scopus 로고    scopus 로고
    • Isolation and characterisation of two antimicrobial peptides from haemocytes of the American lobster Homarus americanus
    • Battison AL, (2008) Isolation and characterisation of two antimicrobial peptides from haemocytes of the American lobster Homarus americanus. Fish Shellfish Immunol 25: 181-187.
    • (2008) Fish Shellfish Immunol , vol.25 , pp. 181-187
    • Battison, A.L.1
  • 15
    • 0033836893 scopus 로고    scopus 로고
    • Differential distribution and defence involvement of antimicrobial peptides in mussel
    • Mitta G, Vandenbulcke F, Noel T, Romestand B, Beauvillain JC, et al. (2000) Differential distribution and defence involvement of antimicrobial peptides in mussel. J Cell Sci 113 (Pt 15): 2759-2769.
    • (2000) J Cell Sci , vol.113 , Issue.PART 15 , pp. 2759-2769
    • Mitta, G.1    Vandenbulcke, F.2    Noel, T.3    Romestand, B.4    Beauvillain, J.C.5
  • 17
    • 77449142619 scopus 로고    scopus 로고
    • Role of bivalves in the depuration of seawaters contaminated by bacteria
    • Govorin I, (2000) Role of bivalves in the depuration of seawaters contaminated by bacteria. Russ J Mar Biol 26: 81-88.
    • (2000) Russ J Mar Biol , vol.26 , pp. 81-88
    • Govorin, I.1
  • 18
    • 0002788404 scopus 로고
    • Degradation of bacteria by Mytilus edulis
    • Birkbeck TH, McHenery JG, (1982) Degradation of bacteria by Mytilus edulis. Mar Biol 72: 7-15.
    • (1982) Mar Biol , vol.72 , pp. 7-15
    • Birkbeck, T.H.1    McHenery, J.G.2
  • 19
    • 0033490117 scopus 로고    scopus 로고
    • Mussel defensins are synthesised and processed in granulocytes then released into the plasma after bacterial challenge
    • Mitta G, Vandenbulcke F, Hubert F, Roch P, (1999) Mussel defensins are synthesised and processed in granulocytes then released into the plasma after bacterial challenge. J Cell Sci 112 (Pt 23): 4233-4242.
    • (1999) J Cell Sci , vol.112 , Issue.PART 23 , pp. 4233-4242
    • Mitta, G.1    Vandenbulcke, F.2    Hubert, F.3    Roch, P.4
  • 20
    • 33845699790 scopus 로고    scopus 로고
    • Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies
    • Hancock REW, Sahl H-G, (2006) Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat Biotechnol 24: 1551-1557.
    • (2006) Nat Biotechnol , vol.24 , pp. 1551-1557
    • Hancock, R.E.W.1    Sahl, H.-G.2
  • 22
    • 34548621750 scopus 로고    scopus 로고
    • Dual antiviral activity of human alpha-defensin-1 against viral haemorrhagic septicaemia rhabdovirus (VHSV): Inactivation of virus particles and induction of a type I interferon-related response
    • Falcó A, Mas V, Tafalla C, Pérez L, Coll JM, et al. (2007) Dual antiviral activity of human alpha-defensin-1 against viral haemorrhagic septicaemia rhabdovirus (VHSV): Inactivation of virus particles and induction of a type I interferon-related response. Antiviral Res 76: 111-123.
    • (2007) Antiviral Res , vol.76 , pp. 111-123
    • Falcó, A.1    Mas, V.2    Tafalla, C.3    Pérez, L.4    Coll, J.M.5
  • 23
    • 70450217037 scopus 로고    scopus 로고
    • Antimicrobial peptides as model molecules for the development of novel antiviral agents in aquaculture
    • Falcó A, Ortega-Villaizan M, Chico V, Brocal I, Perez L, et al. (2009) Antimicrobial peptides as model molecules for the development of novel antiviral agents in aquaculture. Mini Rev Med Chem 9: 1159-1164.
    • (2009) Mini Rev Med Chem , vol.9 , pp. 1159-1164
    • Falcó, A.1    Ortega-Villaizan, M.2    Chico, V.3    Brocal, I.4    Perez, L.5
  • 24
    • 24344442307 scopus 로고    scopus 로고
    • Antiprotozoan and antiviral activities of non-cytotoxic truncated and variant analogues of mussel defensin
    • Roch P, Beschin A, Bernard E, (2004) Antiprotozoan and antiviral activities of non-cytotoxic truncated and variant analogues of mussel defensin. Evid Based Complement Alternat Med 1: 167-174.
    • (2004) Evid Based Complement Alternat Med , vol.1 , pp. 167-174
    • Roch, P.1    Beschin, A.2    Bernard, E.3
  • 25
    • 77949911982 scopus 로고    scopus 로고
    • Expression of Mytilus immune genes in response to experimental challenges varied according to the site of collection
    • Li H, Venier P, Prado-Álvarez M, Gestal C, Toubiana M, et al. (2010) Expression of Mytilus immune genes in response to experimental challenges varied according to the site of collection. Fish Shellfish Immunol 28: 640-648.
    • (2010) Fish Shellfish Immunol , vol.28 , pp. 640-648
    • Li, H.1    Venier, P.2    Prado-Álvarez, M.3    Gestal, C.4    Toubiana, M.5
  • 26
    • 0034672657 scopus 로고    scopus 로고
    • Original involvement of antimicrobial peptides in mussel innate immunity
    • Mitta G, Vandenbulcke F, Roch P, (2000) Original involvement of antimicrobial peptides in mussel innate immunity. FEBS Lett 486: 185-190.
    • (2000) FEBS Lett , vol.486 , pp. 185-190
    • Mitta, G.1    Vandenbulcke, F.2    Roch, P.3
  • 27
    • 77954089746 scopus 로고    scopus 로고
    • MgC1q, a novel C1q-domain-containing protein involved in the immune response of Mytilus galloprovincialis
    • Gestal C, Pallavicini A, Venier P, Novoa B, Figueras A, (2010) MgC1q, a novel C1q-domain-containing protein involved in the immune response of Mytilus galloprovincialis. Dev Comp Immunol 34: 926-934.
    • (2010) Dev Comp Immunol , vol.34 , pp. 926-934
    • Gestal, C.1    Pallavicini, A.2    Venier, P.3    Novoa, B.4    Figueras, A.5
  • 28
    • 77952876929 scopus 로고    scopus 로고
    • AiC1qDC-1, a novel gC1q-domain-containing protein from bay scallop Argopecten irradians with fungi agglutinating activity
    • Kong P, Zhang H, Wang L, Zhou Z, Yang J, et al. (2010) AiC1qDC-1, a novel gC1q-domain-containing protein from bay scallop Argopecten irradians with fungi agglutinating activity. Dev Comp Immunol 34: 837-846.
    • (2010) Dev Comp Immunol , vol.34 , pp. 837-846
    • Kong, P.1    Zhang, H.2    Wang, L.3    Zhou, Z.4    Yang, J.5
  • 29
    • 50149106793 scopus 로고    scopus 로고
    • A novel C1q-domain-containing protein from Zhikong scallop Chlamys farreri with lipopolysaccharide binding activity
    • Zhang H, Song L, Li C, Zhao J, Wang H, et al. (2008) A novel C1q-domain-containing protein from Zhikong scallop Chlamys farreri with lipopolysaccharide binding activity. Fish Shellfish Immunol 25: 281-289.
    • (2008) Fish Shellfish Immunol , vol.25 , pp. 281-289
    • Zhang, H.1    Song, L.2    Li, C.3    Zhao, J.4    Wang, H.5
  • 30
    • 38249026408 scopus 로고
    • Effect of environmental factors and parasitism on hemolymph lysozyme and protein of American oysters (Crassostrea virginica)
    • Chu FL, La Peyre JF, (1989) Effect of environmental factors and parasitism on hemolymph lysozyme and protein of American oysters (Crassostrea virginica). J Invertebr Pathol 54: 224-232.
    • (1989) J Invertebr Pathol , vol.54 , pp. 224-232
    • Chu, F.L.1    la Peyre, J.F.2
  • 31
    • 0000742486 scopus 로고
    • Lysozyme in the hemolymph of the oyster, Crassostrea virginica
    • McDade JE, Tripp MR, (1967) Lysozyme in the hemolymph of the oyster, Crassostrea virginica. J Invertebr Pathol 9: 531-535.
    • (1967) J Invertebr Pathol , vol.9 , pp. 531-535
    • McDade, J.E.1    Tripp, M.R.2
  • 32
    • 0021490172 scopus 로고
    • What's new in lysozyme research?
    • Jollès P, Jollès J, (1984) What's new in lysozyme research? Mol Cell Biochem 63: 165-189.
    • (1984) Mol Cell Biochem , vol.63 , pp. 165-189
    • Jollès, P.1    Jollès, J.2
  • 33
    • 33745639450 scopus 로고    scopus 로고
    • The immunostimulating effect of bacterial genomic DNA on the innate immune responses of bivalve mussel, Hyriopsis cumingii Lea
    • Hong XT, Xiang LX, Shao JZ, (2006) The immunostimulating effect of bacterial genomic DNA on the innate immune responses of bivalve mussel, Hyriopsis cumingii Lea. Fish Shellfish Immunol 21: 357-364.
    • (2006) Fish Shellfish Immunol , vol.21 , pp. 357-364
    • Hong, X.T.1    Xiang, L.X.2    Shao, J.Z.3
  • 34
    • 34447265255 scopus 로고    scopus 로고
    • Construction of a recombinant plasmid containing multi-copy CpG motifs and its effects on the innate immune responses of aquatic animals
    • Chen Y, Xiang LX, Shao JZ, (2007) Construction of a recombinant plasmid containing multi-copy CpG motifs and its effects on the innate immune responses of aquatic animals. Fish Shellfish Immunol 23: 589-600.
    • (2007) Fish Shellfish Immunol , vol.23 , pp. 589-600
    • Chen, Y.1    Xiang, L.X.2    Shao, J.Z.3
  • 35
    • 66449088641 scopus 로고    scopus 로고
    • Pathogen recognition and inflammatory signaling in innate immune defenses
    • Mogensen TH, (2009) Pathogen recognition and inflammatory signaling in innate immune defenses. Clin Microbiol Rev 22: 240-273.
    • (2009) Clin Microbiol Rev , vol.22 , pp. 240-273
    • Mogensen, T.H.1
  • 36
    • 0026231061 scopus 로고
    • Plasma-dependent chemotactic activity of hemocytes derived from a juvenile estuarine gastropod mollusc, Clithon retropictus, to Vibrio parahaemolyticus and Escherichia coli strains
    • Kumazawa NH, Shimoji Y, (1991) Plasma-dependent chemotactic activity of hemocytes derived from a juvenile estuarine gastropod mollusc, Clithon retropictus, to Vibrio parahaemolyticus and Escherichia coli strains. J Vet Med Sci 53: 883-887.
    • (1991) J Vet Med Sci , vol.53 , pp. 883-887
    • Kumazawa, N.H.1    Shimoji, Y.2
  • 37
    • 0000272223 scopus 로고    scopus 로고
    • Phagocytic and chemotactic responses of manila and carpet shell clam haemocytes against Vibrio tapetis, the causative agent of brown ring disease
    • López-Cortés L, Castro D, Navas JI, Borrego JJ, (1999) Phagocytic and chemotactic responses of manila and carpet shell clam haemocytes against Vibrio tapetis, the causative agent of brown ring disease. Fish Shellfish Immunol 9: 543-555.
    • (1999) Fish Shellfish Immunol , vol.9 , pp. 543-555
    • López-Cortés, L.1    Castro, D.2    Navas, J.I.3    Borrego, J.J.4
  • 38
    • 0024486720 scopus 로고
    • Evidence for the involvement of opioid neuropeptides in the adherence and migration of immunocompetent invertebrate hemocytes
    • Stefano GB, Leung MK, Zhao X, Scharrer B, (1989) Evidence for the involvement of opioid neuropeptides in the adherence and migration of immunocompetent invertebrate hemocytes. Proc Natl Acad Sci USA 86: 626-630.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 626-630
    • Stefano, G.B.1    Leung, M.K.2    Zhao, X.3    Scharrer, B.4
  • 39
    • 0034908351 scopus 로고    scopus 로고
    • Platelet-derived growth factor and transforming growth factor- beta in invertebrate immune and neuroendocrine interactions: another sign of conservation in evolution
    • Ottaviani E, Franchini A, Kletsas D, (2001) Platelet-derived growth factor and transforming growth factor- beta in invertebrate immune and neuroendocrine interactions: another sign of conservation in evolution. Comp Biochem Physiol Part C Toxicol Pharmacol 129: 295-306.
    • (2001) Comp Biochem Physiol Part C Toxicol Pharmacol , vol.129 , pp. 295-306
    • Ottaviani, E.1    Franchini, A.2    Kletsas, D.3
  • 41
    • 0001274452 scopus 로고
    • Fish skin: An effective barrier to ice crystal propagation
    • Valerio PF, Kao MH, Fletcher GL, (1992) Fish skin: An effective barrier to ice crystal propagation. J Exp Biol 164: 135-151.
    • (1992) J Exp Biol , vol.164 , pp. 135-151
    • Valerio, P.F.1    Kao, M.H.2    Fletcher, G.L.3
  • 42
    • 61349124155 scopus 로고    scopus 로고
    • The immunogenicity of viral haemorragic septicaemia rhabdovirus (VHSV) DNA vaccines can depend on plasmid regulatory sequences
    • Chico V, Ortega-Villaizan M, Falcó A, Tafalla C, Pérez L, et al. (2009) The immunogenicity of viral haemorragic septicaemia rhabdovirus (VHSV) DNA vaccines can depend on plasmid regulatory sequences. Vaccine 27: 1938-1948.
    • (2009) Vaccine , vol.27 , pp. 1938-1948
    • Chico, V.1    Ortega-Villaizan, M.2    Falcó, A.3    Tafalla, C.4    Pérez, L.5
  • 43
    • 0017765562 scopus 로고
    • Isolement d'un rhabdovirus pathogène de la truite fario (Salmo trutta, L., 1766)
    • De Kinkelin P, Le Berre M, (1977) Isolement d'un rhabdovirus pathogène de la truite fario (Salmo trutta, L., 1766). C R Acad Sci Hebd Seances Acad Sci D 284: 101-104.
    • (1977) C R Acad Sci Hebd Seances Acad Sci D , vol.284 , pp. 101-104
    • de Kinkelin, P.1    Le Berre, M.2
  • 44
    • 84856327632 scopus 로고
    • Variabilidad del virus de la septicemia hemorragica viral de la trucha en España
    • Coll J, Basurco B, (1989) Variabilidad del virus de la septicemia hemorragica viral de la trucha en España. Med Vet 6: 425-430.
    • (1989) Med Vet , vol.6 , pp. 425-430
    • Coll, J.1    Basurco, B.2
  • 45
    • 32044454878 scopus 로고    scopus 로고
    • Interferon mediated antiviral activity against salmonid fish viruses in BF-2 and other cell lines
    • Saint-Jean SR, Pérez-Prieto SI, (2006) Interferon mediated antiviral activity against salmonid fish viruses in BF-2 and other cell lines. Vet Immunol Immunopathol 110: 1-10.
    • (2006) Vet Immunol Immunopathol , vol.110 , pp. 1-10
    • Saint-Jean, S.R.1    Pérez-Prieto, S.I.2
  • 46
    • 0029894714 scopus 로고    scopus 로고
    • Fast neutralization/immunoperoxidase assay for viral haemorrhagic septicaemia with anti-nucleoprotein monoclonal antibody
    • Lorenzo G, Estepa A, Coll JM, (1996) Fast neutralization/immunoperoxidase assay for viral haemorrhagic septicaemia with anti-nucleoprotein monoclonal antibody. J Virol Methods 58: 1-6.
    • (1996) J Virol Methods , vol.58 , pp. 1-6
    • Lorenzo, G.1    Estepa, A.2    Coll, J.M.3
  • 47
    • 18644374984 scopus 로고    scopus 로고
    • Salmonid viral haemorrhagic septicaemia virus: fusion-related enhancement of virus infectivity by peptides derived from viral glycoprotein G or a combinatorial library
    • Mas V, Pérez L, Encinar JA, Pastor MT, Rocha A, et al. (2002) Salmonid viral haemorrhagic septicaemia virus: fusion-related enhancement of virus infectivity by peptides derived from viral glycoprotein G or a combinatorial library. J Gen Virol 83: 2671-2681.
    • (2002) J Gen Virol , vol.83 , pp. 2671-2681
    • Mas, V.1    Pérez, L.2    Encinar, J.A.3    Pastor, M.T.4    Rocha, A.5
  • 48
    • 33745158157 scopus 로고
    • A simple method of estimating fifty per cent endpoints
    • Reed LJ, Muench H, (1938) A simple method of estimating fifty per cent endpoints. Am J Epidemiol 27: 493-497.
    • (1938) Am J Epidemiol , vol.27 , pp. 493-497
    • Reed, L.J.1    Muench, H.2
  • 49
    • 33749864877 scopus 로고    scopus 로고
    • Stable expression of bioactive recombinant pleurocidin in a fish cell line
    • Brocal I, Falcó A, Mas V, Rocha A, Pérez L, et al. (2006) Stable expression of bioactive recombinant pleurocidin in a fish cell line. Appl Microbiol Biotechnol 72: 1217-1228.
    • (2006) Appl Microbiol Biotechnol , vol.72 , pp. 1217-1228
    • Brocal, I.1    Falcó, A.2    Mas, V.3    Rocha, A.4    Pérez, L.5
  • 50
    • 34247471694 scopus 로고    scopus 로고
    • In vitro and in vivo differential expression of rainbow trout (Oncorhynchus mykiss) Mx isoforms in response to viral haemorrhagic septicaemia virus (VHSV) G gene, poly I:C and VHSV
    • Tafalla C, Chico V, Pérez L, Coll JM, Estepa A, (2007) In vitro and in vivo differential expression of rainbow trout (Oncorhynchus mykiss) Mx isoforms in response to viral haemorrhagic septicaemia virus (VHSV) G gene, poly I:C and VHSV. Fish Shellfish Immunol 23: 210-221.
    • (2007) Fish Shellfish Immunol , vol.23 , pp. 210-221
    • Tafalla, C.1    Chico, V.2    Pérez, L.3    Coll, J.M.4    Estepa, A.5
  • 51
    • 34848901649 scopus 로고    scopus 로고
    • Expression and antiviral activity of a [beta]-defensin-like peptide identified in the rainbow trout (Oncorhynchus mykiss) EST sequences
    • Falcó A, Chico V, Marroquí L, Pérez L, Coll JM, et al. (2008) Expression and antiviral activity of a [beta]-defensin-like peptide identified in the rainbow trout (Oncorhynchus mykiss) EST sequences. Mol Immunol 45: 757-765.
    • (2008) Mol Immunol , vol.45 , pp. 757-765
    • Falcó, A.1    Chico, V.2    Marroquí, L.3    Pérez, L.4    Coll, J.M.5
  • 52
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method
    • Livak KJ, Schmittgen TD, (2001) Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method. Methods 25: 402-408.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 53
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • Pfaffl MW, (2001) A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res 29: e45.
    • (2001) Nucleic Acids Res , vol.29
    • Pfaffl, M.W.1
  • 54
    • 32344451474 scopus 로고    scopus 로고
    • Rapid detection and quantitation of viral hemorrhagic septicemia virus in experimentally challenged rainbow trout by real-time RT-PCR
    • Chico V, Gómez N, Estepa A, Pérez L, (2006) Rapid detection and quantitation of viral hemorrhagic septicemia virus in experimentally challenged rainbow trout by real-time RT-PCR. J Virol Methods 132: 154-159.
    • (2006) J Virol Methods , vol.132 , pp. 154-159
    • Chico, V.1    Gómez, N.2    Estepa, A.3    Pérez, L.4
  • 55
    • 56349130560 scopus 로고    scopus 로고
    • Inhibitory effect of mycophenolic acid on the replication of infectious pancreatic necrosis virus and viral hemorrhagic septicemia virus
    • Marroquí L, Estepa A, Perez L, (2008) Inhibitory effect of mycophenolic acid on the replication of infectious pancreatic necrosis virus and viral hemorrhagic septicemia virus. Antiviral Res 80: 332-338.
    • (2008) Antiviral Res , vol.80 , pp. 332-338
    • Marroquí, L.1    Estepa, A.2    Perez, L.3
  • 56
    • 39149092684 scopus 로고    scopus 로고
    • Bath vaccination of rainbow trout (Oncorhynchus mykiss Walbaum) against Yersinia ruckeri: Effects of temperature on protection and gene expression
    • Raida MK, Buchmann K, (2008) Bath vaccination of rainbow trout (Oncorhynchus mykiss Walbaum) against Yersinia ruckeri: Effects of temperature on protection and gene expression. Vaccine 26: 1050-1062.
    • (2008) Vaccine , vol.26 , pp. 1050-1062
    • Raida, M.K.1    Buchmann, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.