Immunological characterization and expression in Escherichia coli and Baculovirus systems of a Trypanosoma vivax antigen detected in the blood of infected animals
| dc.creator | Masake, R.A. | |
| dc.creator | Ole-MoiYoi, O.K. | |
| dc.creator | Urakawa, T. | |
| dc.creator | Hirumi, H. | |
| dc.creator | Majiwa, Phelix A.O. | |
| dc.creator | Wells, C.W. | |
| dc.creator | Minja, S.H. | |
| dc.creator | Makau, J.M. | |
| dc.creator | Nantulya, V.M. | |
| dc.date | 1995-12 | |
| dc.date | 2013-05-06T07:00:59Z | |
| dc.date | 2013-05-06T07:00:59Z | |
| dc.date.accessioned | 2026-06-27T16:41:38Z | |
| dc.description | A monoclonal antibody (MAb)Tv27 employed in an antigen-detection enzyme immunosorbent assay (Ag-ELISA) for diagnosis of Trypanosoma vivax infection was shown to react with a T. vivax-specific protein of an approximate molecular weight of 10 kDa. This protein is diffusely distributed throughout the cytosol and nucleus of metacyclic forms, bloodstream forms, and procyclic-like elongated trypomastigotes, but is not detectable in epimastigotes of T. vivax. The T. vivax-specific antigen prepared from parasite lysates appeared to be of lower molecular mass than the form expressed in either Escherichia coli or in baculovirus-infected silkworm insect cells. In the recombinant baculovirus-infected cells, the protein was expressed mostly as an 18-kDa peptide with less abundant forms of 13 and 12 kDa, while the protein expressed in E. coli was approximately 14 kDa. Both the low- and higher-molecular-weight proteins are recognized by the MAb Tv27 in Western blots and in Ag-ELISA. Although the crude preparations of the protein produced by the insect cells are labile when kept for more than 2 hr at 24°C, they retained reactivity at temperatures below 4°C for several weeks. The proteins expressed in both the insect cells and E. coli captured anti-T. vivax antibodies in sera prepared from trypanosome-infected animals. Since the recombinant protein expressed in the baculovirus-infected cells is available in large homogenous quantities, it would serve as a positive control in Ag-ELISA and is also usable for antibody detection assays. | |
| dc.identifier | https://hdl.handle.net/10568/28608 | |
| dc.identifier.uri | http://hdl.handle.net/123456789/130617 | |
| dc.language | en | |
| dc.publisher | Elsevier | |
| dc.rights | Limited Access | |
| dc.source | Experimental Parasitology;81: 536-545 | |
| dc.subject | trypanosomiasis | |
| dc.subject | trypanosoma vivax | |
| dc.subject | escherichia coli | |
| dc.subject | immunology | |
| dc.subject | disease control | |
| dc.subject | glossinidae | |
| dc.subject | antibodies | |
| dc.subject | animal diseases | |
| dc.subject | antigens | |
| dc.subject | monoclonal antibodies | |
| dc.title | Immunological characterization and expression in Escherichia coli and Baculovirus systems of a Trypanosoma vivax antigen detected in the blood of infected animals | |
| dc.type | Journal Article |
