The identification, purification, and characterization of two invariant surface glycoproteins located beneath the surface coat barrier of bloodstream forms of Trypanosoma brucei.

作者: D.G. Jackson , H.J. Windle , H.P. Voorheis

DOI: 10.1016/S0021-9258(18)53066-0

关键词:

摘要: Two new polypeptides, termed ISG70 and ISG64, have been found in Trypanosoma brucei, using enzyme-catalyzed radioiodination techniques. Both are externally disposed integral membrane glycoproteins, containing N-linked carbohydrate chains. No structural homology was detected between ISG70, or the variant surface glycoprotein (VSG) when assessed by 1) comparative peptide mapping, 2) immunoprecipitation analysis, 3) lectin affinity chromatography. occurred 5.1 x 10(4) copies/cell has purified 880-fold from detergent extracts of plasma membranes a procedure that includes gel filtration, chromatography, preparative SDS-polyacrylamide electrophoresis. present only bloodstream forms specifically six different cloned variants Molteno Institute trypanosomal antigen type (MITat) serodeme T. brucei single International Laboratory for Research on Animal Diseases (ILTat) examined. Rabbits with chronic infections displayed circulating antibodies against ISG70. immunogenicity its invariant nature suggest it may be useful development an effective serodiagnostic test. Furthermore, stage-specific location combined implies function is strictly related to physiological role required parasite's residence mammalian host.

参考文章(66)
C A Auffret, M J Turner, Variant specific antigens of Trypanosoma brucei exist in solution as glycoprotein dimers Biochemical Journal. ,vol. 193, pp. 647- 650 ,(1981) , 10.1042/BJ1930647
David J. Anderson, Günter Blobel, Immunoprecipitation of Proteins from Cell-Free Translations Methods in Enzymology. ,vol. 96, pp. 111- 120 ,(1983) , 10.1016/S0076-6879(83)96012-3
R Bülow, Peter Overath, None, Purification and characterization of the membrane-form variant surface glycoprotein hydrolase of Trypanosoma brucei. Journal of Biological Chemistry. ,vol. 261, pp. 11918- 11923 ,(1986) , 10.1016/S0021-9258(18)67328-4
K Ziegelbauer, P Overath, Identification of invariant surface glycoproteins in the bloodstream stage of Trypanosoma brucei. Journal of Biological Chemistry. ,vol. 267, pp. 10791- 10796 ,(1992) , 10.1016/S0021-9258(19)50088-6
J A Fox, M Duszenko, M A Ferguson, M G Low, G A Cross, Purification and characterization of a novel glycan-phosphatidylinositol-specific phospholipase C from Trypanosoma brucei. Journal of Biological Chemistry. ,vol. 261, pp. 15767- 15771 ,(1986) , 10.1016/S0021-9258(18)66784-5
H P Voorheis, D J Bowles, G A Smith, Characteristics of the release of the surface coat protein from bloodstream forms of Trypanosoma brucei. Journal of Biological Chemistry. ,vol. 257, pp. 2300- 2304 ,(1982) , 10.1016/S0021-9258(18)34921-4
D Hereld, J L Krakow, J D Bangs, G W Hart, P T Englund, A phospholipase C from Trypanosoma brucei which selectively cleaves the glycolipid on the variant surface glycoprotein. Journal of Biological Chemistry. ,vol. 261, pp. 13813- 13819 ,(1986) , 10.1016/S0021-9258(18)67092-9
H S Penefsky, Reversible binding of Pi by beef heart mitochondrial adenosine triphosphatase. Journal of Biological Chemistry. ,vol. 252, pp. 2891- 2899 ,(1977) , 10.1016/S0021-9258(17)40446-7