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Preferential activation of telomeric variant surface glycoprotein genes in Trypanosoma brucei
Molecular and Biochemical Parasitology, 1985During an infection, Trypanosoma brucei expresses diverse variant surface glycoprotein (VSG) genes in a quasi-sequential order. Numerous VSG genes have intrachromosomal locations but many are located adjacent to telomeres. We have tested whether telomeric VSG genes are preferentially activated compared to intrachromosomal VSG genes during an antigenic ...
R F, Aline +4 more
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Structure and variationwithin variant surface glycoproteins of Trypanosoma brucei
Annales de l'Institut Pasteur / Immunologie, 1985Variant surface glycoproteins of the African trypanosomes are members of a multigene family which show extraordinary amino sequence diversity. The extent of this diversity and the significance of homologies both in the amino acid sequence and in the post-translational modifications are discussed in the light of what is predicted for the structure of ...
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Purification of the membrane-form variant surface glycoprotein of Trypanosoma brucei
Journal of Chromatography A, 1990The membrane-form variant surface glycoprotein (mfVSG) is anchored in the plasma membrane of African trypanosomes by a diacylglycerol residue. On cell rupture the anchor is rapidly cleaved by an endogenous phospholipase C. A purification procedure is described which results in native mfVSG devoid of lipase activity.
D, Schell, P, Overath
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Expression of a minichromosomal variant surface glycoprotein gene in Trypanosoma brucei
Nature, 1985African trypanosomes contain numerous variant surface glycoprotein (VSG) genes, but express only one at a time. When different VSG genes are activated by gene duplicative or non-duplicative mechanisms, antigenic variation occurs. Although transcriptionally inactive VSG genes can have either an intra-chromosomal or a telomeric location, all expressed ...
V, Rothwell +4 more
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Degradation, Recycling, and Shedding of Trypanosoma brucei Variant Surface Glycoprotein
The Journal of Protozoology, 1990ABSTRACT. Trypanosoma brucei bloodstream forms express a densely packed surface coat consisting of identical variant surface glycoprotein (VSG) molecules. This surface coat is subject to antigenic variation by sequential expression of different VSG genes and thus enables the cells to escape the mammalian host's specific immune response.
A, Seyfang, D, Mecke, M, Duszenko
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Molecular and Biochemical Parasitology, 1986
Membrane-form variant surface glycoprotein of Trypanosoma brucei can be prepared in the presence of para-chloromercuriphenylsulphonic acid. The membrane-bound enzyme that usually cleaves a lipid from this glycoprotein, thus producing the soluble variant surface glycoprotein, is inhibited by a range of sulphydryl reagents. The effect of such inhibitors,
A. Gurnett, J. Ward, J. Raper, M. Turner
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Membrane-form variant surface glycoprotein of Trypanosoma brucei can be prepared in the presence of para-chloromercuriphenylsulphonic acid. The membrane-bound enzyme that usually cleaves a lipid from this glycoprotein, thus producing the soluble variant surface glycoprotein, is inhibited by a range of sulphydryl reagents. The effect of such inhibitors,
A. Gurnett, J. Ward, J. Raper, M. Turner
semanticscholar +3 more sources
Molecular and Biochemical Parasitology, 1981
Soluble surface coat glycoproteins were purified by concanavalin A affinity chromatography from variant populations of Trypanosoma rhodesiense (Wellcome strain). Each variant yielded a glycoprotein consisting of a single polypeptide chain. The apparent molecular weights of the different glycoproteins ranged from 58 000 to 67 000.
J G, Olenick, R W, Travis, S, Garson
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Soluble surface coat glycoproteins were purified by concanavalin A affinity chromatography from variant populations of Trypanosoma rhodesiense (Wellcome strain). Each variant yielded a glycoprotein consisting of a single polypeptide chain. The apparent molecular weights of the different glycoproteins ranged from 58 000 to 67 000.
J G, Olenick, R W, Travis, S, Garson
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Biochemistry, 1988
Secondary structure determinations have been carried out on two antigenically related variant surface glycoproteins (VSG's) from Trypanosoma brucei, WaTat 1.1 and WaTat 1.12. The two molecules, which bear highly homologous amino-terminal sequences, showed subtle differences in their circular dichroism (CD).
M. Clarke +3 more
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Secondary structure determinations have been carried out on two antigenically related variant surface glycoproteins (VSG's) from Trypanosoma brucei, WaTat 1.1 and WaTat 1.12. The two molecules, which bear highly homologous amino-terminal sequences, showed subtle differences in their circular dichroism (CD).
M. Clarke +3 more
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Isolation and cell-free synthesis of variant surface glycoproteins from Trypanosoma congolense.
Molecular and Biochemical Parasitology, 1985Two Trypanosoma congolense stocks, 1/148 FLY and TREU 921, were cloned in A/J strain mice immunosuppressed with cyclophosphamide. The cloned populations, AmNat 1.1 and AmNat 3.1, each characterized by a different variant antigen type, were checked for homogeneity by the indirect fluorescent antibody test using 6-day antisera developed in rabbits.
G. Cook, B. Honigberg, R. Zimmermann
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Biosynthesis and processing of a variant surface glycoprotein from Trypanosoma brucei brucei
Archives of Biochemistry and Biophysics, 1986Iowa trypanosome antigen type (IaTat) 1.2 variant surface glycoprotein (VSG) is synthesized in vitro as a Mr 54,000 preprotein that contains a 31-amino-acid signal peptide. Translation of mRNA in the presence of either dog pancreas or trypanosome microsomal membranes results in cotranslational cleavage of the signal peptide and addition of core ...
K A, Presper, E C, Heath
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