Subcellular localization of Trypanosoma cruzi glycoprotein Gp72

Journal of Cell Science

Volumn 109, Issue 13, 1996, Pages 2979-2988

  Haynes, Paul A ^a,c   Russell, David G ^b   Cross, George A M ^a  

^a ROCKEFELLER UNIVERSITY   (United States)

^b WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c UNIVERSITY OF WASHINGTON   (United States)

Author keywords

Epitope tag; Glycosylation; Surface glycoprotein 72; Trypanosoma cruzi

Indexed keywords

GLYCOPROTEIN;

ARTICLE; CELLULAR DISTRIBUTION; EPIMASTIGOTE; IMMUNOELECTRON MICROSCOPY; IMMUNOFLUORESCENCE; NONHUMAN; PRIORITY JOURNAL; PROTEIN LOCALIZATION; TRYPANOSOMA CRUZI;

AMINO ACID SEQUENCE; ANIMALS; CELL LINE; EPITOPES; FLUORESCENT ANTIBODY TECHNIQUE, INDIRECT; HUMANS; MEMBRANE GLYCOPROTEINS; MICROSCOPY, IMMUNOELECTRON; MOLECULAR SEQUENCE DATA; PHOSPHOPROTEINS; PROTOZOAN PROTEINS; RATS; RECOMBINANT FUSION PROTEINS; SEQUENCE TAGGED SITES; SUBCELLULAR FRACTIONS; TRYPANOSOMA CRUZI;

EID: 0030475877     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (37)

1. Andrews, N. W., Hong, K. S., Robbins, E. S. and Nussenzweig, V. (1987). Stage-specific surface antigens expressed during the morphogenesis of vertebrate forms of Trypanosoma cruzi. Exp. Parasitol. 64, 474-484.
2. Araya, J. E., Cano, M. I., Yoshida, N. and Franco da Silveira, J. (1994). Cloning and characterization of a gene for the stage-specific 82-kDa surface antigen of metacyclic trypomastigotes of Trypanosoma cruzi. Mol. Biochem. Parasitol. 65, 161-169.
3. Barry, J. D. (1979). Capping of variable surface antigen on Trypanosoma brucei and its immunological and biological significance. J. Cell Sci. 37, 287-302.
4. Bellofatto, V. and Cross, G. A. M. (1989). Expression of a bacterial gene in a trypanosomatid protozoan. Science 244, 1167-1169.
5. Bone, G. J. and Steinert, M. (1956). Isotopes incorporated in the nucleic acids of Trypanosoma mega. Nature 178, 308-309.
6. Brener, Z. (1973). Biology of Trypanosoma cruzi. Annu. Rev. Microbiol. 27, 347-382.
7. Cooper, R., Inverso, J. A., Espinosa, M., Nogueira, N. and Cross, G. A. M. (1991). Characterization of a candidate gene for GP72, an insect stage-specific antigen of Trypanosoma cruzi. Mol. Biochem. Parasitol. 49, 45-60.
8. Cooper, R., Ribeiro de Jesus, A. and Cross, G. A. M. (1993). Deletion of an immunodominant Trypanosoma cruzi surface glycoprotein disrupts flagellum-cell adhesion. J. Cell Biol. 122, 149-156.
9. Cotrim, P. C., Paranhos, G. S., Mortara, R. A., Wanderley, J., Rassi, A., Camargo, M. E. and Da Silveira, J. F. (1990). Expression in Escherichia coli of a dominant immunogen of Trypanosoma cruzi recognized by human chagasic sera. J. Clin. Microbiol. 28, 519-524.
10. Cross, G. A. M. and Takle, G. (1993). The surface trans-sialidase family of Trypanosoma cruzi. Annu. Rev. Microbiol. 46, 385-411.
11. De Lederkremer, R. M., Lima, C., Ramirez, M. I. and Casal, O. L. (1990). Structural features of the lipopeptidophosphoglycan from Trypanosoma cruzi common with the glycophosphatidylinositol anchors. Eur. J. Biochem. 192, 337-345.
12. Frommel, T. O. and Balber, A. E. (1987). Trypanosoma brucei brucei, T. brucei gambiense, and T. brucei rhodesiense: common glycoproteins and glycoprotein oligosaccharide heterogeneity identified by lectin affinity blotting and endoglycosidase H treatment. Exp. Parasitol. 63, 32-42.
13. Harth, G., Mills, A. A., Souto-Padron, T. and De Souza, W. (1992). Trypanosoma cruzi glycoprotein 72: immunological analysis and cellular localization. Mol. Cell. Biochem. 109, 25-36.
14. Haynes, P.A., Ferguson, M.A.J.F. and Cross, G.A.M. (1996). Structural characterization of novel oligosaccharides of cell surface glycoproteins of Trypanosoma cruzi. Glycobiology (in press).
15. Joiner, K., Hieny, S., Kirchhoff, L. V. and Sher, A. (1985). GP72, the 72 kilodalton glycoprotein, is the membrane acceptor site for complement factor C3 on Trypanosoma cruzi epimastigotes. J. Exp. Med. 161, 1196-1212.
16. Kelly, J. M., Ward, H. M., Miles, M. A. and Kendall, G. (1992). A shuttle vector which facilitates the expression of transfected genes in Trypanosoma cruzi and Leishmania. Nucl. Acids Res. 20, 3963-3969.
17. Kirchhoff, L. V., Hieny, S., Shiver, G. M., Snary, D. and Sher, A. (1984). Cryptic epitope explains the failure of a monoclonal antibody to bind to certain isolates of Trypanosoma cruzi. J. Immunol. 133, 2731-2735.
18. Kirchhoff, L. V. and Sher, A. (1985). Modifications of a 72kDa surface glycoprotein (GP-72) of Trypanosoma cruzi during development. Fed. Proc. 44, 1332.
19. Medina-Acosta, E. and Cross, G. (1993). Rapid isolation of DNA from trypanosomatid protozoa using a simple 'mini-prep' procedure. Mol. Biochem. Parasitol. 59, 327-330.
20. Nozaki, T. and Cross, G. A. M. (1994). Functional complementation of glycoprotein 72 in a Trypanosoma cruzi glycoprotein 72 null mutant. Mol. Biochem. Parasitol. 67, 91-102.
21. Nozaki, T. and Cross, G. A. M. (1995). Effects of 3′ untranslated and intergenic regions on gene expression in Trypanosoma cruzi. Mol. Biochem. Parasitol. 75, 55-67.
22. Pimenta, P., Saraiva, E. and Sacks, D. L. (1991). The comparative fine structure and surface glycoconjugate expression of three life stages of Leishmania major. Exp. Parasitol. 72, 191-204.
23. Previato, J. O., Jones, C., Xavier, M. T., Wait, R., Travassos, L. R., Parodi, A. J. and Mendonca-Previato, L. (1995). Structural characterization of the major glycosylphosphatidylinositol membrane-anchored glycoprotein from epimastigote forms of Trypanosoma cruzi Y-strain. J. Biol. Chem. 270, 7241-7250.
24. Ribeiro de Jesus, A., Cooper, R., Espinosa, M., Gomes, J. E. P. L., Garcia, E. S., Paul, S. and Cross, G. A. M. (1993). Gene deletion suggests a role for Trypanosoma cruzi surface glycoprotein GP72 in the insect and mammalian stages of the life cycle. J. Cell Sci. 106, 1023-1033.
25. Russell, D.G., Xu, S. and Chakraborty, P. (1992). Intracellular trafficking and the parasitophorous vacuole of Leishmania mexicana infected macrophages. J. Cell Sci. 103, 1193-1210.
26. Russell, D.G. (1994). Immunoelectron microscopy of endosomal trafficking in macrophages infected with microbial pathogens. In Microbes as Tools for Cell Biology, vol. 45 (ed. D.G. Russell), pp. 277-288. Academic Press, New York.
27. Schechter, M., Stevens, A. F., Luquetti, A. O., Snary, D., Allen, A. K. and Miles, M. A. (1986). Prevalence of antibodies to 72-kilodalton glycoprotein (GP72) in patients with Chagas' disease and further evidence of zymodeme-associated expression of GP72 carbohydrate epitopes. Infect. Immunol. 53, 547-566.
28. Schenkman, S., Ferguson, M. A. J., Heise, N., Cardoso de Almeida, M. L., Mortara, R. A. and Yoshida, N. (1993). Mucin-like glycoproteins linked to the membrane by glycosylphosphatidylinositol anchor are the major acceptors of sialic acid in a reaction catalyzed by trans-sialidase in metacyclic forms of Trypanosoma cruzi. Mol. Biochem. Parasitol. 59, 293-304.
29. Sher, A. and Snary, D. (1982). Specific inhibition of the morphogenesis of Trypanosoma cruzi by a monoclonal antibody. Nature 300, 639-640.
30. Snary, D., Ferguson, M. A. J., Scott, M. T. and Allen, A. K. (1981). Cell surface antigens of Trypanosoma cruzi: use of monoclonal antibodies to identify and isolate an epimastigote specific glycoprotein. Mol. Biochem. Parasitol. 3, 343-356.
31. Souto-Padron, T., Reyes, M. B., Leguizamon, S., Campetella, O. E., Frasch, A. C. C. and de Souza, W. (1989). Trypanosoma cruzi proteins which are antigenic during human infections are located in defined regions of the parasite. Eur. J. Cell Biol. 50, 272-278.
32. Takle, G. B., Young, A., Snary, D., Hudson, L. and Nicholls, S. C. (1989). Cloning and expression of a trypomastigote-specific 85-kilodalton surface antigen gene from Trypanosoma cruzi. Mol. Biochem. Parasitol. 37, 57-64.
33. Teixeira, S. M. R., Russell, D. G., Kirchhoff, L. V. and Donelson, J. E. (1994). A differentially expressed gene family encoding amastin, a surface protein of Trypanosoma cruzi amastigotes. J. Biol. Chem. 269, 20509-20516.
34. Tyers, M., Tokiwa, G. and Futcher, B. (1993). Comparison of the Saccharomyces cerevisiae G1 cyclins: Cln3 may be an upstream activator of Cln1, Cln2 and other cyclins. EMBO J. 12, 1955-1968.
35. Vickerman, K. (1969). On the surface coat and flagellar adhesion in trypanosomes. J. Cell Sci. 5, 163-194.
36. Von Heijne, G. (1986). A new method for predicting signal sequence cleavage sites. Nucl. Acids Res. 14, 4683-4690.
37. Woods, A., Baines, A. J. and Gull, K. (1989). Evidence for a Mr88 000 glycoprotein with a transmembrane association to a unique flagellum attachment region in Trypanosoma brucei. J. Cell Sci. 93, 501-508.