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Volumn 126, Issue 2, 2003, Pages 201-208

Identification of excretory-secretory products of larval and adult Ostertagia ostertagi by immunoscreening of cDNA libraries

Author keywords

Candidate protective antigens; Excretory secretory products; Immunoscreening; Ostertagia ostertagi

Indexed keywords

ACTIN; COMPLEMENTARY DNA; HEAT SHOCK PROTEIN; KINESIN; OSTERTAGIA VACCINE; THIOREDOXIN PEROXIDASE; UNCLASSIFIED DRUG; VACCINE; VITELLOGENIN;

EID: 0037325351     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-6851(02)00274-8     Document Type: Article
Times cited : (52)

References (43)
  • 1
    • 0035850233 scopus 로고    scopus 로고
    • Treatment versus non-treatment of helminth infections in cattle: Defining the threshold
    • Vercruysse J., Claerebout E. Treatment versus non-treatment of helminth infections in cattle: defining the threshold. Vet. Parasitol. 98:2001;195-214.
    • (2001) Vet. Parasitol. , vol.98 , pp. 195-214
    • Vercruysse, J.1    Claerebout, E.2
  • 2
    • 0035935622 scopus 로고    scopus 로고
    • Vaccines against cysticercosis and hydatidosis
    • Lightowlers M.W., Gauci C.G. Vaccines against cysticercosis and hydatidosis. Vet. Parasitol. 101:2001;337-352.
    • (2001) Vet. Parasitol. , vol.101 , pp. 337-352
    • Lightowlers, M.W.1    Gauci, C.G.2
  • 3
    • 0027813118 scopus 로고
    • Partial characterization of proteolytic enzymes in different developmental stages of Ostertagia ostertagi
    • De Cock H., Knox D.P., Claerebout E., De Graaf D.C. Partial characterization of proteolytic enzymes in different developmental stages of Ostertagia ostertagi. J. Helminthol. 67:1993;271-278.
    • (1993) J. Helminthol. , vol.67 , pp. 271-278
    • De Cock, H.1    Knox, D.P.2    Claerebout, E.3    De Graaf, D.C.4
  • 4
    • 0034530983 scopus 로고    scopus 로고
    • Proteinases released in vitro by the parasitic stages of the bovine abomasal nematode Ostertagia ostertagi
    • Geldhof P., Claerebout E., Knox D.P., Agneessens J., Vercruysse J. Proteinases released in vitro by the parasitic stages of the bovine abomasal nematode Ostertagia ostertagi. Parasitology. 121:2000;639-647.
    • (2000) Parasitology , vol.121 , pp. 639-647
    • Geldhof, P.1    Claerebout, E.2    Knox, D.P.3    Agneessens, J.4    Vercruysse, J.5
  • 5
    • 0027332107 scopus 로고
    • Haemonchus contortus: Identification of proteases with diverse characteristics in adult worm excretory-secretory products
    • Karanu F.N., Rurangirwa F.R., McGuire T.C., Jasmer D.P. Haemonchus contortus: identification of proteases with diverse characteristics in adult worm excretory-secretory products. Exp. Parasitol. 77:1993;362-371.
    • (1993) Exp. Parasitol. , vol.77 , pp. 362-371
    • Karanu, F.N.1    Rurangirwa, F.R.2    McGuire, T.C.3    Jasmer, D.P.4
  • 6
    • 0031754465 scopus 로고    scopus 로고
    • Onchocerca volvulus: Microfilariae secrete elastinolytic and males nonelastinolytic matrix-degrading serine and metalloproteases
    • Haffner A., Guilavogui A.Z., Tischendorf F.W., Brattig N.W. Onchocerca volvulus: microfilariae secrete elastinolytic and males nonelastinolytic matrix-degrading serine and metalloproteases. Exp. Parasitol. 90:1998;26-33.
    • (1998) Exp. Parasitol. , vol.90 , pp. 26-33
    • Haffner, A.1    Guilavogui, A.Z.2    Tischendorf, F.W.3    Brattig, N.W.4
  • 7
    • 0035962925 scopus 로고    scopus 로고
    • Modulation of the host immune system by phosphorylcholine-containing glycoproteins secreted by parasitic filarial nematodes
    • Harnett W., Harnett M.M. Modulation of the host immune system by phosphorylcholine-containing glycoproteins secreted by parasitic filarial nematodes. Biochim. Biophys. Acta. 1539:2001;7-15.
    • (2001) Biochim. Biophys. Acta , vol.1539 , pp. 7-15
    • Harnett, W.1    Harnett, M.M.2
  • 8
    • 0035111288 scopus 로고    scopus 로고
    • Adaptive physiological processes in the host during gastrointestinal parasitism
    • Hoste H. Adaptive physiological processes in the host during gastrointestinal parasitism. Int. J. Parasitol. 31:2001;231-244.
    • (2001) Int. J. Parasitol. , vol.31 , pp. 231-244
    • Hoste, H.1
  • 9
    • 0002569166 scopus 로고
    • Immune response to nematodes
    • Cohen S, Warren KS, editors. Oxford: Blackwell Scientific Publications
    • Ogilvie BM, de Savigny D. Immune response to nematodes. In: Cohen S, Warren KS, editors. Immunology of parasitic infections. Oxford: Blackwell Scientific Publications; 1982. p. 715.
    • (1982) Immunology of Parasitic Infections , pp. 715
    • Ogilvie, B.M.1    De Savigny, D.2
  • 10
    • 0023915740 scopus 로고
    • Excretory-secretory products of helminth parasites: Effects on host immune responses
    • Lightowlers M.W., Rickard M.D. Excretory-secretory products of helminth parasites: effects on host immune responses. Parasitology. 96:1988;S123-S166.
    • (1988) Parasitology , vol.96 , pp. 123-S166
    • Lightowlers, M.W.1    Rickard, M.D.2
  • 11
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 13
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H., Engelbrecht J., Brunak S., von Heijne G. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10:1997;1-6.
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 14
    • 0032835839 scopus 로고    scopus 로고
    • Molecular cloning and characterization of gut-derived cysteine proteinases associated with a host protective extract from Haemonchus contortus
    • Skuce P.J., Redmond D.L., Liddell S., Stewart E.M., Newlands G.F., Smith W.D.et al. Molecular cloning and characterization of gut-derived cysteine proteinases associated with a host protective extract from Haemonchus contortus. Parasitology. 119:1999;405-412.
    • (1999) Parasitology , vol.119 , pp. 405-412
    • Skuce, P.J.1    Redmond, D.L.2    Liddell, S.3    Stewart, E.M.4    Newlands, G.F.5    Smith, W.D.6
  • 15
    • 0026681653 scopus 로고
    • XP2, a new member of the P-domain peptide family of potential growth factors, is synthesized in Xenopus laevis skin
    • Hauser F., Roeben C., Hoffmann W. xP2, a new member of the P-domain peptide family of potential growth factors, is synthesized in Xenopus laevis skin. J. Biol. Chem. 267:1992;14451-14455.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14451-14455
    • Hauser, F.1    Roeben, C.2    Hoffmann, W.3
  • 16
    • 0027959156 scopus 로고
    • Protein disulphide isomerase: Building bridges in protein folding
    • Freedman R.B., Hirst T.R., Tuite M.F. Protein disulphide isomerase: building bridges in protein folding. TIBS. 19:1994;331-336.
    • (1994) TIBS , vol.19 , pp. 331-336
    • Freedman, R.B.1    Hirst, T.R.2    Tuite, M.F.3
  • 17
    • 0031905860 scopus 로고    scopus 로고
    • An ERp60-like protein from the filarial parasite Dirofilaria immitis has both transglutaminase and protein disulfide isomerase activity
    • Chandrashekar R., Tsuji N., Morales T., Ozols V., Mehta K. An ERp60-like protein from the filarial parasite Dirofilaria immitis has both transglutaminase and protein disulfide isomerase activity. Proc. Natl. Acad. Sci. USA. 95:1998;531-536.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 531-536
    • Chandrashekar, R.1    Tsuji, N.2    Morales, T.3    Ozols, V.4    Mehta, K.5
  • 18
    • 0029092660 scopus 로고
    • Cloning and sequencing of an excretory/secretory antigen from Ostertagia ostertagi fourth-stage larvae containing multiple tandem repeats
    • de Graaf D.C., Peelman L.J., Claerebout E., Hilderson H., Schallig H.D., Vercruysse J. Cloning and sequencing of an excretory/secretory antigen from Ostertagia ostertagi fourth-stage larvae containing multiple tandem repeats. Mol. Biochem. Parasitol. 72:1995;239-241.
    • (1995) Mol. Biochem. Parasitol. , vol.72 , pp. 239-241
    • De Graaf, D.C.1    Peelman, L.J.2    Claerebout, E.3    Hilderson, H.4    Schallig, H.D.5    Vercruysse, J.6
  • 19
    • 0033955614 scopus 로고    scopus 로고
    • The ABA-1 allergen of Ascaris lumbricoides: Sequence polymorphism, stage and tissue-specific expression, lipid binding function, and protein biophysical properties
    • Xia Y., Spence H.J., Moore J., Heanly N., McDermott L., Cooper A.et al. The ABA-1 allergen of Ascaris lumbricoides: sequence polymorphism, stage and tissue-specific expression, lipid binding function, and protein biophysical properties. Parasitology. 120:2000;211-224.
    • (2000) Parasitology , vol.120 , pp. 211-224
    • Xia, Y.1    Spence, H.J.2    Moore, J.3    Heanly, N.4    McDermott, L.5    Cooper, A.6
  • 20
    • 0022749115 scopus 로고
    • Stage-specific secreted antigens of the parasitic larval stages of the nematode Ascaris
    • Kennedy M.W., Qureshi F. Stage-specific secreted antigens of the parasitic larval stages of the nematode Ascaris. Immunology. 58:1986;515-522.
    • (1986) Immunology , vol.58 , pp. 515-522
    • Kennedy, M.W.1    Qureshi, F.2
  • 21
    • 0033981221 scopus 로고    scopus 로고
    • The polyprotein lipid binding proteins of nematodes
    • Kennedy M.W. The polyprotein lipid binding proteins of nematodes. Biochim. Biophys. Acta. 1476:2000;149-164.
    • (2000) Biochim. Biophys. Acta , vol.1476 , pp. 149-164
    • Kennedy, M.W.1
  • 22
    • 0027183567 scopus 로고
    • Nemoglobins: Divergent nematode globins
    • Blaxter M.L. Nemoglobins: divergent nematode globins. Parasitol. Today. 9:1993;353-360.
    • (1993) Parasitol. Today , vol.9 , pp. 353-360
    • Blaxter, M.L.1
  • 23
    • 0029984954 scopus 로고    scopus 로고
    • Isolation, characterization and immunolocalization of a globin-like antigen from Ostertagia ostertagi adults
    • De Graaf D.C., Berghen P., Moens L., De Marez T.M., Raes S., Blaxter M.L.et al. Isolation, characterization and immunolocalization of a globin-like antigen from Ostertagia ostertagi adults. Parasitology. 133:1996;63-69.
    • (1996) Parasitology , vol.133 , pp. 63-69
    • De Graaf, D.C.1    Berghen, P.2    Moens, L.3    De Marez, T.M.4    Raes, S.5    Blaxter, M.L.6
  • 24
    • 0026512248 scopus 로고
    • The isolation characterization and cloning of a globin-like, host-protective antigen from the excretory-secretory products of Trichostrongylus colubriformis
    • Frenkel M.J., Dopheide T.A.A., Wagland B.M., Ward C.W. The isolation characterization and cloning of a globin-like, host-protective antigen from the excretory-secretory products of Trichostrongylus colubriformis. Mol. Biochem. Parasitol. 50:1992;27-36.
    • (1992) Mol. Biochem. Parasitol. , vol.50 , pp. 27-36
    • Frenkel, M.J.1    Dopheide, T.A.A.2    Wagland, B.M.3    Ward, C.W.4
  • 25
    • 0029989299 scopus 로고    scopus 로고
    • Cloning and characterization of Ancylostoma-secreted protein
    • Hawdon J.M., Jones B.F., Hoffman D.R., Hotez P.J. Cloning and characterization of Ancylostoma-secreted protein. J. Biol. Chem. 271:1996;6672-6678.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6672-6678
    • Hawdon, J.M.1    Jones, B.F.2    Hoffman, D.R.3    Hotez, P.J.4
  • 26
    • 0032934497 scopus 로고    scopus 로고
    • Ancylostoma secreted protein 2: Cloning and characterization of a second member of a family of nematode secreted proteins from Ancylostoma caninum
    • Hawdon J.M., Narasimhan S., Hotez P.J. Ancylostoma secreted protein 2: cloning and characterization of a second member of a family of nematode secreted proteins from Ancylostoma caninum. Mol. Biochem. Parasitol. 99:1999;149-165.
    • (1999) Mol. Biochem. Parasitol. , vol.99 , pp. 149-165
    • Hawdon, J.M.1    Narasimhan, S.2    Hotez, P.J.3
  • 27
    • 0030934540 scopus 로고    scopus 로고
    • Extensive sequence conservation among insect, nematode, and invertebrate vitellogenins reveals ancient common ancestry
    • Chen J., Sappington T.W., Raikhel A.S. Extensive sequence conservation among insect, nematode, and invertebrate vitellogenins reveals ancient common ancestry. J. Mol. Evol. 44:1997;440-451.
    • (1997) J. Mol. Evol. , vol.44 , pp. 440-451
    • Chen, J.1    Sappington, T.W.2    Raikhel, A.S.3
  • 28
    • 0029150195 scopus 로고
    • An abundant, trans-spliced mRNA from Toxocara canis infective larvae encodes a 26-kDa protein with homology to phosphatidylethanolamine-binding proteins
    • Gems D., Ferguson C.J., Robertson B.D., Nieves R., Page A.P., Blaxter M.L.et al. An abundant, trans-spliced mRNA from Toxocara canis infective larvae encodes a 26-kDa protein with homology to phosphatidylethanolamine-binding proteins. J. Biol. Chem. 270:1995;18517-18522.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18517-18522
    • Gems, D.1    Ferguson, C.J.2    Robertson, B.D.3    Nieves, R.4    Page, A.P.5    Blaxter, M.L.6
  • 29
    • 0029919506 scopus 로고    scopus 로고
    • An abundantly expressed mucin-like protein from Toxocara canis infective larvae: The precursor of the larval surface coat glycoproteins
    • Gems D., Maizels R.M. An abundantly expressed mucin-like protein from Toxocara canis infective larvae: the precursor of the larval surface coat glycoproteins. Proc. Natl. Acad. Sci. USA. 93:1996;1665-1670.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1665-1670
    • Gems, D.1    Maizels, R.M.2
  • 30
    • 0032509180 scopus 로고    scopus 로고
    • Caenorhabditis elegans is a nematode
    • Blaxter M.J. Caenorhabditis elegans is a nematode. Science. 282:1998;2041-2046.
    • (1998) Science , vol.282 , pp. 2041-2046
    • Blaxter, M.J.1
  • 31
    • 0034671646 scopus 로고    scopus 로고
    • A family of secreted mucins from the parasitic nematode Toxocara canis bears diverse mucin domains but shares similar flanking six-cysteine repeat motifs
    • Loukas A., Hintz M., Linder D., Mullin N.P., Parkinson J., Tetteh K.K.A. A family of secreted mucins from the parasitic nematode Toxocara canis bears diverse mucin domains but shares similar flanking six-cysteine repeat motifs. J. Biol. Chem. 275:2000;39600-39607.
    • (2000) J. Biol. Chem. , vol.275 , pp. 39600-39607
    • Loukas, A.1    Hintz, M.2    Linder, D.3    Mullin, N.P.4    Parkinson, J.5    Tetteh, K.K.A.6
  • 32
    • 0033952127 scopus 로고    scopus 로고
    • A survey of genes expressed in adults of the human hookworm, Necator americanus
    • Daub J., Loukas A., Pritchard D.I., Blaxter M. A survey of genes expressed in adults of the human hookworm, Necator americanus. Parasitology. 120:2000;171-184.
    • (2000) Parasitology , vol.120 , pp. 171-184
    • Daub, J.1    Loukas, A.2    Pritchard, D.I.3    Blaxter, M.4
  • 33
    • 0026483279 scopus 로고
    • Alpha-crystallin can function as a molecular chaperone
    • Horwitz J. Alpha-crystallin can function as a molecular chaperone. Proc. Natl. Acad. Sci. USA. 89:1992;10449-10453.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 34
    • 0027375653 scopus 로고
    • The expression of a small heat shock protein homologue is developmentally regulated in Nippostrongylus brasiliensis
    • Tweedie S., Grigg M.E., Ingram L., Selkirk M.E. The expression of a small heat shock protein homologue is developmentally regulated in Nippostrongylus brasiliensis. Mol. Biochem. Parasitol. 61:1993;149-153.
    • (1993) Mol. Biochem. Parasitol. , vol.61 , pp. 149-153
    • Tweedie, S.1    Grigg, M.E.2    Ingram, L.3    Selkirk, M.E.4
  • 35
    • 0031435939 scopus 로고    scopus 로고
    • Molecular cloning, expression and enzymatic activity of a thioredoxin peroxidase from Dirofilaria immitis
    • Klimowski L., Chandrashekar R., Tripp C.A. Molecular cloning, expression and enzymatic activity of a thioredoxin peroxidase from Dirofilaria immitis. Mol. Biochem. Parasitol. 90:1997;297-306.
    • (1997) Mol. Biochem. Parasitol. , vol.90 , pp. 297-306
    • Klimowski, L.1    Chandrashekar, R.2    Tripp, C.A.3
  • 36
    • 0032521486 scopus 로고    scopus 로고
    • Thioredoxin peroxidase from Onchocerca volvulus: A major hydrogen peroxide detoxifying enzyme in filarial parasites
    • Lu W., Egerton G.L., Bianco A.E., Williams S.A. Thioredoxin peroxidase from Onchocerca volvulus: a major hydrogen peroxide detoxifying enzyme in filarial parasites. Mol. Biochem. Parasitol. 91:1998;221-235.
    • (1998) Mol. Biochem. Parasitol. , vol.91 , pp. 221-235
    • Lu, W.1    Egerton, G.L.2    Bianco, A.E.3    Williams, S.A.4
  • 37
    • 0031826863 scopus 로고    scopus 로고
    • The peroxidoxin 2 protein of the human parasite Onchocerca volvulus: Recombinant expression, immunolocalization, and demonstration of homologous molecules in other species
    • Zipfel P.F., Schrum S., Bialonski A., Buttner D.W. The peroxidoxin 2 protein of the human parasite Onchocerca volvulus: recombinant expression, immunolocalization, and demonstration of homologous molecules in other species. Parasitol. Res. 84:1998;623-631.
    • (1998) Parasitol. Res. , vol.84 , pp. 623-631
    • Zipfel, P.F.1    Schrum, S.2    Bialonski, A.3    Buttner, D.W.4
  • 38
    • 0030792101 scopus 로고    scopus 로고
    • Cytochromes in the respiratory chain of helminth mitochondria
    • Kita K., Hirawake H., Takamiya S. Cytochromes in the respiratory chain of helminth mitochondria. Int. J. Parasitol. 27:1997;617-630.
    • (1997) Int. J. Parasitol. , vol.27 , pp. 617-630
    • Kita, K.1    Hirawake, H.2    Takamiya, S.3
  • 39
    • 0035001263 scopus 로고    scopus 로고
    • Protection against cutaneous leishmaniasis induced by recombinant antigens in murine and nonhuman primate models of the human disease
    • Campos-Neto A., Porrozzi R., Greeson K., Coler R.N., Webb J.R., Seiky Y.A.et al. Protection against cutaneous leishmaniasis induced by recombinant antigens in murine and nonhuman primate models of the human disease. Infect. Immun. 69:2001;4103-4108.
    • (2001) Infect. Immun. , vol.69 , pp. 4103-4108
    • Campos-Neto, A.1    Porrozzi, R.2    Greeson, K.3    Coler, R.N.4    Webb, J.R.5    Seiky, Y.A.6
  • 40
    • 0035935653 scopus 로고    scopus 로고
    • The contribution of molecular biology to the development of vaccines against nematode and trematode parasites of domestic ruminants
    • Knox D.P., Redmond D.L., Skuce P.J., Newlands G.F. The contribution of molecular biology to the development of vaccines against nematode and trematode parasites of domestic ruminants. Vet. Parasitol. 101:2001;311-335.
    • (2001) Vet. Parasitol. , vol.101 , pp. 311-335
    • Knox, D.P.1    Redmond, D.L.2    Skuce, P.J.3    Newlands, G.F.4
  • 41
    • 0029826617 scopus 로고    scopus 로고
    • Vaccination with alum-precipitated recombinant Ancylostoma-secreted protein 1 protects mice against challenge infections with infective hookworm (Ancylostoma caninum) larvae
    • Ghosh K., Hawdon J., Hotez P. Vaccination with alum-precipitated recombinant Ancylostoma-secreted protein 1 protects mice against challenge infections with infective hookworm (Ancylostoma caninum) larvae. J. Infect. Dis. 174:1996;1380-1383.
    • (1996) J. Infect. Dis. , vol.174 , pp. 1380-1383
    • Ghosh, K.1    Hawdon, J.2    Hotez, P.3
  • 42
    • 0033991240 scopus 로고    scopus 로고
    • Hookworm burden reductions in BALB/c mice vaccinated with recombinant Ancylostoma secreted proteins (ASPs) from Ancylostoma duodenale, Ancylostoma caninum and Necator americanus
    • Sen L., Ghosh K., Bin Z., Qiang S., Thompson M.G., Hawdon J.M.et al. Hookworm burden reductions in BALB/c mice vaccinated with recombinant Ancylostoma secreted proteins (ASPs) from Ancylostoma duodenale, Ancylostoma caninum and Necator americanus. Vaccine. 18:2000;1096-1102.
    • (2000) Vaccine , vol.18 , pp. 1096-1102
    • Sen, L.1    Ghosh, K.2    Bin, Z.3    Qiang, S.4    Thompson, M.G.5    Hawdon, J.M.6
  • 43
    • 0037292401 scopus 로고    scopus 로고
    • Protein disulphide isomerase of Ostertagia ostertagi - An excretory-secretory product of L4 and adult worms?
    • in press
    • Geldhof P, Vercauteren I, Knox D, De Maere V, Van Zeveren A, Berx G, et al. Protein disulphide isomerase of Ostertagia ostertagi - an excretory-secretory product of L4 and adult worms? Int J Parasitol (in press).
    • Int J Parasitol
    • Geldhof, P.1    Vercauteren, I.2    Knox, D.3    De Maere, V.4    Van Zeveren, A.5    Berx, G.6


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