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Journal of Molecular Graphics and Modelling, 2021
Trypanosomes, which cause animal African trypanosomiasis, escape host immune responses by renewing their variable surface glycoprotein (VSG) coat. Chemotherapy is currently the only form of external intervention available.
Lucky Marufu, T. Coetzer
semanticscholar +1 more source
Trypanosomes, which cause animal African trypanosomiasis, escape host immune responses by renewing their variable surface glycoprotein (VSG) coat. Chemotherapy is currently the only form of external intervention available.
Lucky Marufu, T. Coetzer
semanticscholar +1 more source
A structural motif in the variant surface glycoproteins of Trypanosoma brucei
Nature, 1993The variable domain of the trypanosome variant surface glycoprotein (VSG) ILTat 1.24 has been shown by X-ray crystallography to resemble closely the structures of VSG MITat 1.2, despite their low sequence similarity. Specific structural features of these VSGs, including substitution of carbohydrate for an alpha-helix, can be found in other VSG ...
M. Blum +5 more
semanticscholar +3 more sources
Two variant surface glycoproteins of Trypanosoma brucei have a conserved C-terminus
Nature, 1981Gene duplication and transposition are known to be involved in the mechanism of antigenic variation in Trypanosoma brucei1–3. However, the structure of the antigens in question—the variant surface glycoproteins (VSGs)—is poorly defined. Limited sequencing data show extensive variation between the N-terminal amino acid sequences of different VSGs4,5 ...
G. Matthyssens +4 more
semanticscholar +3 more sources
Trypanosoma brucei: generation of specific antisera to recombinant variant surface glycoproteins.
Experimental Parasitology, 1999Abstract Hoek, M., Xu, H., and Cross, G. A. M. 1999.Trypanosoma brucei:Generation of specific antisera to recombinant variant surface glycoproteins.Experimental Parasitology91, 199–202.
M. Hoek, Hui Xu, George A. M. Cross
semanticscholar +3 more sources
Structural features affecting variant surface glycoprotein expression in Trypanosoma brucei
Molecular and Biochemical Parasitology, 2003The glycosylphosphatidylinositol (GPI)-anchored variant surface glycoprotein (VSG) of Trypanosoma brucei is the most abundant GPI-anchored protein expressed on any cell, and is an essential virulence factor. To determine what structural features affect efficient expression of VSG, we made a series of mutations in two VSGs.
Jun, Wang +2 more
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Solution properties of the variant surface glycoprotein of Trypanosoma brucei
Molecular and Biochemical Parasitology, 1986The solution properties of the membrane form and soluble form of variant surface glycoproteins from Trypanosoma brucei have been compared. Solution cross-linking studies established that both forms are dimers, although dissociation of membrane-form variant surface glycoprotein can be promoted by certain ionic and zwitterionic detergents.
A M, Gurnett, J, Raper, M J, Turner
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Molecular Immunology, 1987
The immunochemical structure of two variant surface glycoproteins (VSGs) from Trypanosoma brucei has been studied using monoclonal and polyclonal antibodies. These two VSGs, WaTat 1.1 and WaTat 1.12 have been shown to possess cross-reactive surface-exposed antigenic determinants [Barbet et al., Nature 300, 53-57 (1982)] and similar N-terminal amino ...
M. Clarke, A. Barbet, T. Pearson
semanticscholar +3 more sources
The immunochemical structure of two variant surface glycoproteins (VSGs) from Trypanosoma brucei has been studied using monoclonal and polyclonal antibodies. These two VSGs, WaTat 1.1 and WaTat 1.12 have been shown to possess cross-reactive surface-exposed antigenic determinants [Barbet et al., Nature 300, 53-57 (1982)] and similar N-terminal amino ...
M. Clarke, A. Barbet, T. Pearson
semanticscholar +3 more sources
The architecture of variant surface glycoprotein gene expression sites in Trypanosoma brucei
Molecular and Biochemical Parasitology, 2002Trypanosoma brucei evades the immune system by switching between Variant Surface Glycoprotein (VSG) genes. The active VSG gene is transcribed in one of approximately 20 telomeric expression sites (ESs). It has been postulated that ES polymorphism plays a role in host adaptation. To gain more insight into ES architecture, we have determined the complete
Matt Berriman +2 more
exaly +3 more sources
Trypanosoma brucei: Frequent loss of a telomeric variant surface glycoprotein gene
Experimental Parasitology, 1989We have observed the loss of an inactive telomeric variant surface glycoprotein (VSG) gene that is located on a minichromosome in Trypanosoma brucei. If this is due to gene conversion, it is the third "silent" gene conversion (i.e., one that does not produce an antigenic switch) detected in 19 antigenic switches of the IsTaR 1 serodeme.
R F, Aline, P J, Myler, K D, Stuart
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Molecular and Biochemical Parasitology, 1991
The AnTat 11.17 variant surface glycoprotein (VSG) is synthesized in both metacyclic and bloodstream forms of Trypanosoma gambiense. We have characterized the AnTat 11.17 gene, and analyzed its expression site (ES) in the bloodstream form by Southern and Northern blotting with probes from the Trypanosoma brucei AnTat 1.3A VSG ES, and by run-on ...
Etienne Pays
exaly +3 more sources
The AnTat 11.17 variant surface glycoprotein (VSG) is synthesized in both metacyclic and bloodstream forms of Trypanosoma gambiense. We have characterized the AnTat 11.17 gene, and analyzed its expression site (ES) in the bloodstream form by Southern and Northern blotting with probes from the Trypanosoma brucei AnTat 1.3A VSG ES, and by run-on ...
Etienne Pays
exaly +3 more sources