The membrane-anchoring systems of vertebrate acetylcholinesterase and variant surface glycoproteins of African trypanosomes share a common antigenic determinant |
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| Authors: | A Stieger M L Cardoso de Almeida M C Blatter U Brodbeck C Bordier |
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| Affiliation: | 1. Medizinisch-chemisches Institut der Universität Bern, Bühlstrasse 28, CH-3000 Bern 9, Switzerland;2. Molteno Institute, Medical Research Council, Biochemical Parasitology Unit, Downing Street, Cambridge CB2 SEE, England;3. Institut de Biochimie, Université de Lausanne, Chemin des Boveresses, CH-1066 Epalinges, Switzerland |
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| Abstract: | Amphiphilic detergent-soluble acetylcholinesterase (AChE) from Torpedo is converted to a hydrophilic form by digestion with phospholipase C from Trypanosoma brucei or from Bacillus cereus. This lipase digestion uncovers an immunological determinant which crossreacts with a complex carbohydrate structure present in the hydrophilic form of all variant surface glycoproteins (VSG) of T. brucei. This crossreacting determinant is also detected in human erythrocyte AChE after digestion with T. brucei lipase. From these results we conclude that the glycophospholipid anchors of protozoan VSG and of AChE of the two vertebrates share common structural features, suggesting that this novel type of membrane anchor has been conserved during evolution. |
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