The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.
Glycosyl-sn-1,2-dimyristylphosphatidylinositol is covalently linked to Trypanosoma brucei variant surface glycoprotein.
Open accessAbstract
The COOH terminus of the externally disposed variant surface glycoprotein (VSG) of the eukaryotic pathogenic protozoan Trypanosoma brucei strain 427 variant MITat 1.4 (117) is covalently linked to a novel phosphatidylinositol-containing glycolipid. This conclusion is supported by analysis of the products of nitrous acid deamination or Staphylococcus aureus phosphatidylinositol-specific phospholipase C treatment of purified membrane-form VSG. Lysis of trypanosomes is accompanied by release of soluble VSG, catalyzed by activation of an endogenous phospholipase C. The only apparent difference between membrane-form VSG and soluble VSG is the removal of sn-1,2-dimyristylglycerol. The COOH-terminal glycopeptide derived by Pronase digestion of soluble VSG was characterized by chemical modification and digestion with alkaline phosphatase. The results are consistent with the single non-N-acetylated glucosamine residue being the reducing terminus of the oligosaccharide and in a glycosidic linkage to a myo-inositol monophosphate that is probably myo-inositol 1,2-cyclic monophosphate. A partial structure for the VSG COOH-terminal moiety is presented. This structure represents a new type of eukaryotic post-translational protein modification and membrane anchor. We discuss the relevance of this structure to observations that have been made with other eukaryotic membrane proteins.
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Cites
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Inositol trisphosphate and diacylglycerol as second messengers
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The membrane form of variant surface glycoproteins of Trypanosoma brucei
de Almeida, M. L. C., & Turner, M. J. (1983) · Nature · doi:10.1038/302349a0 · Cited by 280
Ferguson, M. A., Haldar, K., & Cross, G. A. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)89166-9 · Cited by 268
Self-citationHenderson, L. E., Krutzsch, H. C., & Oroszlan, S. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.2.339 · Cited by 258
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Homans, S. W., Ferguson, M. A. J., Dwek, R. A., Rademacher, T. W., Anand, R., & Williams, A. F. (1988) · Nature · doi:10.1038/333269a0 · Cited by 444
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Self-citationSchofield, P. R., McFarland, K. C., Hayflick, J. S., Wilcox, J. N., Cho, T. M., Roy, S., Lee, N. M., Loh, H. H., & Seeburg, P. H. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb03402.x · Cited by 126
Hooper, N. M., Hryszko, J., & Turner, A. J. (1990) · Biochemical Journal · doi:10.1042/bj2670509 · Cited by 91
Targeting the GPI biosynthetic pathway
Yadav, U., & Khan, M. A. (2018) · Pathogens and Global Health · doi:10.1080/20477724.2018.1442764 · Cited by 55
Metadata
- Authors
- Ferguson, M. A., Low, M. G., & Cross, G. A.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1985-11
- Volume
- 260
- Issue
- 27
- Pages
- 14547-14555
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1528089915
- Cited by
- 422
- References
- 31
- FWCI
- 51.85
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Ferguson, M. A., Low, M. G., & Cross, G. A. (1985). Glycosyl-sn-1,2-dimyristylphosphatidylinositol is covalently linked to Trypanosoma brucei variant surface glycoprotein. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(17)38603-9
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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