Disease relevance of Tb11.02.1680

• The flagellar pocket of the bloodstream form of the African sleeping sickness parasite Trypanosoma brucei contains material that binds the beta-d-galactose-specific lectin ricin (Brickman, M. J., and Balber, A. E. (1990) J. Protozool. 37, 219-224) [1].

High impact information on Tb11.02.1680

• Since this lectin binds the surface glycoprotein EP-procyclin, we predicted that cells would lose affinity to conA if RNAi silenced genes affecting EP-procyclin expression or modification [2].
• Procyclic Trypanosoma brucei rhodesiense have a cell death mechanism which can be activated by an external signal, the lectin ConA, in vitro [3].
• Proteins from the endocytic pathway in bloodstream forms of Trypanosome brucei are modified by the addition of linear poly-N-acetyllactosamine side chains, which permits their isolation by tomato lectin affinity chromatography [4].
• ISG70 occurred in 5.1 x 10(4) copies/cell and has been purified 880-fold from detergent extracts of plasma membranes by a procedure that includes gel filtration, lectin affinity chromatography, and preparative SDS-polyacrylamide gel electrophoresis [5].
• The polyclonal lymphocyte activation was induced with variant antigen isolated by either ion exchange or lentil lectin column chromatography and by variant antigen isolated from antigenically dissimilar Trypanosoma brucei rhodesiense and Trypanosoma brucei brucei clones [6].

Biological context of Tb11.02.1680

• Radioactively labelled core-glycan prepared by dephosphorylation, deamination and reduction was analysed by high-pH anion-exchange chromatography, size-exclusion and lectin affinity chromatography [7].
• A model is proposed for susceptibility to trypanosome infection based on the generation of GlcNAc by RLO endochitinase activity in tsetse pupae inhibiting midgut lectin in teneral flies [8].
• The trypsinization protocol used did not remove major common glycoproteins detected on lectin blots of either life cycle form but removed greater than 95% of the variant specific glycoprotein and fragments derived from this protein of bloodstream forms [9].
• Lectin endocytosis assays revealed a block to postendosomal transport mediated by suppressing TbRAB11 [10].
• When parasites were trypsinized to remove the variant surface glycoprotein coat, new lectin binding sites were exposed, and specific binding of all three lectins increased significantly [11].

Anatomical context of Tb11.02.1680

• The lectin concanavalin A (ConA) bound to the outer surface of T. brucei in two discrete locations; one a narrow line close to the flagellum attachment zone on the cell body, the other at the distal tip of the flagellum itself [12].
• We purified Triton X-100-soluble ricin-binding glycoproteins by lectin affinity chromatography and immunized mice to generate hybridomas [13].
• The glucosyl lectin is specific for rabbit erythrocytes and is present in guts of fed G.m.morsitans and G.p.palpalis, titres of lectin activity do not increase substantially after the second bloodmeal [14].

Associations of Tb11.02.1680 with chemical compounds

• These structures, which also bind tomato lectin, are twice the size reported for the largest mammalian poly-N-acetyllactosamine N-linked glycans and also differ in their preponderance of -4GlcNAcbeta1-6Galbeta1- over -4GlcNacbeta1-3Galbeta1- interrepeat linkages [1].
• Multiple effects of the lectin-inhibitory sugars D-glucosamine and N-acetyl-glucosamine on tsetse-trypanosome interactions [15].
• A number of these carbohydrates (E.G., glucose, mannose, galactose and n-acetylgalactosamine) are, however, buried within the surface coat as evidenced by lectin binding to trypsinized parasites [16].

Analytical, diagnostic and therapeutic context of Tb11.02.1680

• Immunoprecipitation of the PSA-2 proteins with sera directed to lectin-binding proteins indicated that these polypeptides may be differentially glycosylated [17].
• No structural homology was detected between ISG70, ISG64, or the variant surface glycoprotein (VSG) when assessed by 1) comparative peptide mapping, 2) immunoprecipitation analysis, and 3) lectin affinity chromatography [5].

References