Schein E, 1985. Equine babesiosis. Ristic M, ed. Babesiosis of Domestic Animals and Man. Boca Raton, FL: CRC Press, 197–208.
Dubremetz JF, Garcia-Reguet N, Conseil V, Fourmaux MN, 1998. Apical organelles and host-cell invasion by Apicomplexa. Int J Parasitol 28 :1007–1013.
Blackman MJ, Bannister LH, 2001. Apical organelles of Apicomplexa: biology and isolation by subcellular fractionation. Mol Biochem Parasitol 117 :11–25.
Preiser P, Kaviratne M, Khan S, Bannister L, Jarra W, 2000. The apical organelles of malaria merozoites: host cell selection, invasion, host immunity and immune evasion. Microbes Infect 2 :1461–1477.
Lindquist S, 1986. The heat shock response. Annu Rev Biochem 55 :1151–1191.
Schlesinger MJ, 1990. Heat shock proteins. J Biol Chem 265 :12111–12114.
Gething MJ, Sambrook J, 1992. Protein folding in the cell. Nature 355 :33–45.
Hartl FU, Martin J, Neupert W, 1992. Protein folding in the cell: the role of molecular chaperones Hsp70 and Hsp60. Annu Rev Biophys Biomol Struct 21 :293–322.
Craig EA, Gambill BD, Nelson RJ, 1993. Heat shock proteins: molecular chaperones of protein biogenesis. Microbiol Rev 57 :402–414.
Haas IG, Wabl M, 1983. Immunoglobulin heavy chain binding protein. Nature 306 :387–389.
Gething MJ, 1999. Role and regulation of the ER chaperone BiP. Semin Cell Dev Biol 10 :465–472.
Avarazed A, Igarashi I, Kanemaru K, Hirumi K, Omata Y, Saito A, Oyamada T, Nagasawa H, Toyoda Y, Suzuki N, 1997. Improved in vitro cultivation of Babesia caballi. J Vet Med Sci 59 :479–481.
Ikadai H, Martin MD, Nagasawa H, Fujisaki K, Suzuki N, Mikami T, Kudo N, Oyamada T, Igarashi I, 2001. Analysis of a growth-promoting factor for Babesia caballi cultivation. J Parasitol 87 :1484–1486.
Ikadai H, Tamaki Y, Xuan X, Igarashi I, Kawai S, Nagasawa H, Fujisaki K, Toyoda Y, Suzuki N, Mikami T, 1999. Inhibitory effect of monoclonal antibodies on the growth of Babesia caballi. Int J Parasitol 29 :1785–1791.
Ikadai H, Xuan X, Igarashi I, Tanaka S, Kanemaru T, Nagasawa H, Fujisaki K, Suzuki N, Mikami T, 1999. Cloning and expression of a 48-kilodalton Babesia caballi merozoite rhoptry protein and potential use of the recombinant antigen in an enzyme-linked immunosorbent assay. J Clin Microbiol 37 :3475–3480.
Hager KM, Striepen B, Tilney LG, Roos DS, 1999. The nuclear envelope serves as an intermediary between the ER and Golgi complex in the intracellular parasite Toxoplasma gondii. J Cell Sci 112 :2631–2638.
Dunn PP, Bumstead JM, Tomley FM, 1996. Primary structure of a BiP homologue in Eimeria spp. Parasitol Res 82 :566–568.
Kappes B, Suetterlin BW, Hofer-Warbinek R, Humar R, Franklin RM, 1993. Two major phosphoproteins of Plasmodium falciparum are heat shock proteins. Mol Biochem Parasitol 59 :83–94.
Bangs JD, Uyetake L, Brickman MJ, Balber AE, Boothroyd JC, 1993. Molecular cloning and cellular localization of a BiP homologue in Trypanosoma brucei. Divergent ER retention signals in a lower eukaryote. J Cell Sci 105 :1101–1113.
Nicholson RC, Williams DB, Moran LA, 1990. An essential member of the HSP70 gene family of Saccharomyces cerevisiae is homologous to immunoglobulin heavy chain binding protein. Proc Natl Acad Sci USA 87 :1159–1163.
Munro S, Pelham HR, 1986. An Hsp70-like protein in the ER: identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein. Cell 46 :291–300.
von Heijne G, 1986. A new method for predicting signal sequence cleavage sites. Nucleic Acids Res 14 :4683–4690.
Freedman RB, Hirst TR, Tuite MF, 1994. Protein disulfide isomerase: building bridges in protein folding. Trends Biochem Sci 19 :331–336.
Pelham HRB, 1989. Control of protein exit from the endoplasmic reticulum. Annu Rev Cell Biol 5 :1–23.
Pelham HRB, 1989. Heat shock and the sorting of luminal ER proteins. EMBO J 8 :3171–3176.
Kumar N, Zheng H, 1992. Nucleotide sequence of a Plasmodiun falciparum stress protein with similarity to mammalian. Mol Biochem Parasitol 56 :353–356.
Sambrook J, Fritsch EF, Maniatis T, 1989. Molecular Cloning: A Laboratory Manual. Second edition. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
Bangs JD, Brouch EM, Ransom DM, Roggy JL, 1996. A soluble secretory reporter system in Trypanosoma brucei. Studies on endoplasmic reticulum targeting. J Biol Chem 271 :18387–18393.
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A composite 2,206 nucleotide DNA sequence encoding a putative immunoglobulin-binding protein (BiP) was constructed from a sequence obtained from Babesia caballi cDNA library clones. The 1,962 nucleotide open reading frame predicts a 72 kD protein with extensive homology with BiPs from Apicomplexa parasites. The BiP gene had a predicted N-terminal signal sequence of 18 amino acids and a C-terminal tetrapeptide sequence (Ser-Asp-Glu-Leu) for signaling in the endoplasmic reticulum lumen. The recombinant protein expressed in baculovirus showed an apparent mass of 72 kD, which is identical to that of the native B. caballi protein. Monoclonal antibodies (MAbs) against B. caballi BiP reacted strongly with extracellular merozoites, but not in early intraerythrocytic stage. Detailed observation showed that the reaction of MAbs against pear-shaped forms was markedly irregular, with either no reaction, or reaction with one or two brightly fluorescent pear-shaped forms (two parasites) of B. caballi.
Schein E, 1985. Equine babesiosis. Ristic M, ed. Babesiosis of Domestic Animals and Man. Boca Raton, FL: CRC Press, 197–208.
Dubremetz JF, Garcia-Reguet N, Conseil V, Fourmaux MN, 1998. Apical organelles and host-cell invasion by Apicomplexa. Int J Parasitol 28 :1007–1013.
Blackman MJ, Bannister LH, 2001. Apical organelles of Apicomplexa: biology and isolation by subcellular fractionation. Mol Biochem Parasitol 117 :11–25.
Preiser P, Kaviratne M, Khan S, Bannister L, Jarra W, 2000. The apical organelles of malaria merozoites: host cell selection, invasion, host immunity and immune evasion. Microbes Infect 2 :1461–1477.
Lindquist S, 1986. The heat shock response. Annu Rev Biochem 55 :1151–1191.
Schlesinger MJ, 1990. Heat shock proteins. J Biol Chem 265 :12111–12114.
Gething MJ, Sambrook J, 1992. Protein folding in the cell. Nature 355 :33–45.
Hartl FU, Martin J, Neupert W, 1992. Protein folding in the cell: the role of molecular chaperones Hsp70 and Hsp60. Annu Rev Biophys Biomol Struct 21 :293–322.
Craig EA, Gambill BD, Nelson RJ, 1993. Heat shock proteins: molecular chaperones of protein biogenesis. Microbiol Rev 57 :402–414.
Haas IG, Wabl M, 1983. Immunoglobulin heavy chain binding protein. Nature 306 :387–389.
Gething MJ, 1999. Role and regulation of the ER chaperone BiP. Semin Cell Dev Biol 10 :465–472.
Avarazed A, Igarashi I, Kanemaru K, Hirumi K, Omata Y, Saito A, Oyamada T, Nagasawa H, Toyoda Y, Suzuki N, 1997. Improved in vitro cultivation of Babesia caballi. J Vet Med Sci 59 :479–481.
Ikadai H, Martin MD, Nagasawa H, Fujisaki K, Suzuki N, Mikami T, Kudo N, Oyamada T, Igarashi I, 2001. Analysis of a growth-promoting factor for Babesia caballi cultivation. J Parasitol 87 :1484–1486.
Ikadai H, Tamaki Y, Xuan X, Igarashi I, Kawai S, Nagasawa H, Fujisaki K, Toyoda Y, Suzuki N, Mikami T, 1999. Inhibitory effect of monoclonal antibodies on the growth of Babesia caballi. Int J Parasitol 29 :1785–1791.
Ikadai H, Xuan X, Igarashi I, Tanaka S, Kanemaru T, Nagasawa H, Fujisaki K, Suzuki N, Mikami T, 1999. Cloning and expression of a 48-kilodalton Babesia caballi merozoite rhoptry protein and potential use of the recombinant antigen in an enzyme-linked immunosorbent assay. J Clin Microbiol 37 :3475–3480.
Hager KM, Striepen B, Tilney LG, Roos DS, 1999. The nuclear envelope serves as an intermediary between the ER and Golgi complex in the intracellular parasite Toxoplasma gondii. J Cell Sci 112 :2631–2638.
Dunn PP, Bumstead JM, Tomley FM, 1996. Primary structure of a BiP homologue in Eimeria spp. Parasitol Res 82 :566–568.
Kappes B, Suetterlin BW, Hofer-Warbinek R, Humar R, Franklin RM, 1993. Two major phosphoproteins of Plasmodium falciparum are heat shock proteins. Mol Biochem Parasitol 59 :83–94.
Bangs JD, Uyetake L, Brickman MJ, Balber AE, Boothroyd JC, 1993. Molecular cloning and cellular localization of a BiP homologue in Trypanosoma brucei. Divergent ER retention signals in a lower eukaryote. J Cell Sci 105 :1101–1113.
Nicholson RC, Williams DB, Moran LA, 1990. An essential member of the HSP70 gene family of Saccharomyces cerevisiae is homologous to immunoglobulin heavy chain binding protein. Proc Natl Acad Sci USA 87 :1159–1163.
Munro S, Pelham HR, 1986. An Hsp70-like protein in the ER: identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein. Cell 46 :291–300.
von Heijne G, 1986. A new method for predicting signal sequence cleavage sites. Nucleic Acids Res 14 :4683–4690.
Freedman RB, Hirst TR, Tuite MF, 1994. Protein disulfide isomerase: building bridges in protein folding. Trends Biochem Sci 19 :331–336.
Pelham HRB, 1989. Control of protein exit from the endoplasmic reticulum. Annu Rev Cell Biol 5 :1–23.
Pelham HRB, 1989. Heat shock and the sorting of luminal ER proteins. EMBO J 8 :3171–3176.
Kumar N, Zheng H, 1992. Nucleotide sequence of a Plasmodiun falciparum stress protein with similarity to mammalian. Mol Biochem Parasitol 56 :353–356.
Sambrook J, Fritsch EF, Maniatis T, 1989. Molecular Cloning: A Laboratory Manual. Second edition. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
Bangs JD, Brouch EM, Ransom DM, Roggy JL, 1996. A soluble secretory reporter system in Trypanosoma brucei. Studies on endoplasmic reticulum targeting. J Biol Chem 271 :18387–18393.
Past two years | Past Year | Past 30 Days | |
---|---|---|---|
Abstract Views | 98 | 79 | 6 |
Full Text Views | 238 | 2 | 0 |
PDF Downloads | 35 | 2 | 0 |