Cloning and characterization of a 150 kDa microsphere antigen of Theileria parva that is immunologically cross-reactive with the polymorphic immunodominant molecule (PIM)

To identify the genes encoding novel immunodominant antigens of Theileria parvo a ?gt11 library of piroplasm genomic DNA was immunoscreened with bovine recovery serum and a gene encoding a 150 kDa antigen (p150) was identified. The predicted polypeptide contains an N-terminal secretory signal sequen...

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Autores principales: Skilton, Robert A., Bishop, Richard P., Wells, C.W., Spooner, P.R., Gobright, E.I., Nkonge, C., Musoke, A.J., Macklin, M.D., Iams, K.P.
Formato: Journal Article
Lenguaje:Inglés
Publicado: Cambridge University Press 1998
Materias:
Acceso en línea:https://hdl.handle.net/10568/35337
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author Skilton, Robert A.
Bishop, Richard P.
Wells, C.W.
Spooner, P.R.
Gobright, E.I.
Nkonge, C.
Musoke, A.J.
Macklin, M.D.
Iams, K.P.
author_browse Bishop, Richard P.
Gobright, E.I.
Iams, K.P.
Macklin, M.D.
Musoke, A.J.
Nkonge, C.
Skilton, Robert A.
Spooner, P.R.
Wells, C.W.
author_facet Skilton, Robert A.
Bishop, Richard P.
Wells, C.W.
Spooner, P.R.
Gobright, E.I.
Nkonge, C.
Musoke, A.J.
Macklin, M.D.
Iams, K.P.
author_sort Skilton, Robert A.
collection Repository of Agricultural Research Outputs (CGSpace)
description To identify the genes encoding novel immunodominant antigens of Theileria parvo a ?gt11 library of piroplasm genomic DNA was immunoscreened with bovine recovery serum and a gene encoding a 150 kDa antigen (p150) was identified. The predicted polypeptide contains an N-terminal secretory signal sequence and a proline-rich region of repeated amino acid motifs. The repeat region is polymorphic between stocks of T. parva in both copy number and sequence, and analysis of the repeat region from 10 stocks of T. parva revealed 5 p150 variants. A monoclonal antibody (mAb) against the T. parva polymorphic immunodominant molecule (PIM) cross-reacted with the recombinant p150. The p150 has sequence homology with a PIM peptide sequence containing the anti-PIM mAb epitope. Immunoelectron microscopy demonstrated that the p150 antigen, like PIM, is located in the microspheres of the sporozoites and is exocytosed following sporozoite invasion of the host lymphocyte. By immunoelectron microscopy p150 was subsequently transiently detectable on the sporozoite surface and in the lymphocyte cytosol. Immunoblotting showed that p150 is also expressed by the schizont stage, but at much lower levels compared to the sporozoite. These results suggest a major role for p150 in the early events of host-sporozoite interaction.
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spelling CGSpace353372024-11-15T08:52:49Z Cloning and characterization of a 150 kDa microsphere antigen of Theileria parva that is immunologically cross-reactive with the polymorphic immunodominant molecule (PIM) Skilton, Robert A. Bishop, Richard P. Wells, C.W. Spooner, P.R. Gobright, E.I. Nkonge, C. Musoke, A.J. Macklin, M.D. Iams, K.P. vaccines animal diseases livestock To identify the genes encoding novel immunodominant antigens of Theileria parvo a ?gt11 library of piroplasm genomic DNA was immunoscreened with bovine recovery serum and a gene encoding a 150 kDa antigen (p150) was identified. The predicted polypeptide contains an N-terminal secretory signal sequence and a proline-rich region of repeated amino acid motifs. The repeat region is polymorphic between stocks of T. parva in both copy number and sequence, and analysis of the repeat region from 10 stocks of T. parva revealed 5 p150 variants. A monoclonal antibody (mAb) against the T. parva polymorphic immunodominant molecule (PIM) cross-reacted with the recombinant p150. The p150 has sequence homology with a PIM peptide sequence containing the anti-PIM mAb epitope. Immunoelectron microscopy demonstrated that the p150 antigen, like PIM, is located in the microspheres of the sporozoites and is exocytosed following sporozoite invasion of the host lymphocyte. By immunoelectron microscopy p150 was subsequently transiently detectable on the sporozoite surface and in the lymphocyte cytosol. Immunoblotting showed that p150 is also expressed by the schizont stage, but at much lower levels compared to the sporozoite. These results suggest a major role for p150 in the early events of host-sporozoite interaction. 1998-10 2014-04-14T10:56:02Z 2014-04-14T10:56:02Z Journal Article https://hdl.handle.net/10568/35337 en Limited Access Cambridge University Press Skilton, R.A., Bishop, R.P., Wells, C.W., Spooner, P.R., Gobright, E., Nkonge, C., Musoke, A.J., Macklin, M. and Iams, K.P. 1998. Cloning and characterization of a 150 kDa microsphere antigen of Theileria parva that is immunologically cross-reactive with the polymorphic immunodominant molecule (PIM). Parasitology 117(4): 321-330.
spellingShingle vaccines
animal diseases
livestock
Skilton, Robert A.
Bishop, Richard P.
Wells, C.W.
Spooner, P.R.
Gobright, E.I.
Nkonge, C.
Musoke, A.J.
Macklin, M.D.
Iams, K.P.
Cloning and characterization of a 150 kDa microsphere antigen of Theileria parva that is immunologically cross-reactive with the polymorphic immunodominant molecule (PIM)
title Cloning and characterization of a 150 kDa microsphere antigen of Theileria parva that is immunologically cross-reactive with the polymorphic immunodominant molecule (PIM)
title_full Cloning and characterization of a 150 kDa microsphere antigen of Theileria parva that is immunologically cross-reactive with the polymorphic immunodominant molecule (PIM)
title_fullStr Cloning and characterization of a 150 kDa microsphere antigen of Theileria parva that is immunologically cross-reactive with the polymorphic immunodominant molecule (PIM)
title_full_unstemmed Cloning and characterization of a 150 kDa microsphere antigen of Theileria parva that is immunologically cross-reactive with the polymorphic immunodominant molecule (PIM)
title_short Cloning and characterization of a 150 kDa microsphere antigen of Theileria parva that is immunologically cross-reactive with the polymorphic immunodominant molecule (PIM)
title_sort cloning and characterization of a 150 kda microsphere antigen of theileria parva that is immunologically cross reactive with the polymorphic immunodominant molecule pim
topic vaccines
animal diseases
livestock
url https://hdl.handle.net/10568/35337
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