Structure of a filamentous phosphoglycoprotein polymer: The secreted acid phosphatase of Leishmania mexicana

Journal of Molecular Biology

Volumn 282, Issue 1, 1998, Pages 137-148

  Stierhof, York Dieter ^a   Wiese, Martin ^a   Ilg, Thomas ^a   Overath, Peter ^a   Häner, Markus ^b   Aebi, Ueli ^b  

^a MAX PLANCK INST FÜR BIOLOGIE   (Germany)

^b UNIVERSITY OF BASEL   (Switzerland)

Author keywords

Electron microscopy; Filament structure; Mass determination; O glycosylation; Scanning transmission electron microscopy

Indexed keywords

ACID PHOSPHATASE; DIMER; GLYCOPROTEIN; MONOCLONAL ANTIBODY; PHOSPHOPROTEIN; PHOSPHOSERINE;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; LEISHMANIA MEXICANA; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN GLYCOSYLATION; PROTEIN STRUCTURE; SCANNING ELECTRON MICROSCOPY;

EID: 0032508579     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2012     Document Type: Article

References (35)

1. Alexander, J. & Russell, D. G. (1992). The interaction of Leishmania species with macrophages. Advan. Parasitol. 31, 175-254.
2. Balber, A. E. (1990). The pellicle and the membrane of the flagellum, flagellar adhesion zone and flagellar pocket: functionally discrete surface domains of the bloodstream form of African trypanosomes. Crit. Rev. Immunol. 10, 177-201.
3. Bates, B. P., Hermes, I. & Dwyer, D. M. (1990). Golgi-mediated posttranslational processing of secretory acid phosphatase by Leishmania donovani promastigotes. Mol. Biochem. Parasitol. 39, 247-256.
4. Brun, R. & Schönenberger, M. (1979). Cultivation and in vitro cloning of procyclic culture forms of Trypanosoma brucei in a semidefined medium. Acta Trop. 36, 289-292.
5. Engel, A., Eichner, R. & Aebi, U. (1985). Polymorphism of reconstituted human epidermal keratin filaments: determination of their mass-per-length and width by scanning transmission electron microscopy. J. Ultrastruct. Res. 90, 323-335.
6. Gottlieb, M. & Dwyer, D. M. (1982). Identification and partial characterization of an extracellular acid phosphatase activity of Leishmania donovani promastigotes. Mol. Cell. Biol. 2, 76-81.
7. Ilg, T., Stierhof, Y.-D., Etges, R., Adrian, M., Harbecke, D. & Overath, P. (1991). Secreted acid phosphatase of Leishmania mexicana: A filamentous phosphoglycoprotein polymer. Proc. Natl Acad. Sci. USA, 88, 8774-8778.
8. Ilg, T., Harbecke, D., Wiese, M. & Overath, P. (1993). Monoclonal antibodies to Leishmania secreted acid phosphatase and lipophosphoglycan. Partial characterization of private and public epitopes. Eur. J. Biochem. 217, 603-615.
9. Ilg, T., Overath, P., Ferguson, M. A. J., Rutherford, T., Campbell, D. G. & McConville, M. J. (1994a). O-and N-glycosylation of the Leishmania mexicana secreted acid phosphatase: characterization of a new class of phosphoserine linked glycans. J. Biol. Chem. 269, 24073-24081.
10. Ilg, T., Stierhof, Y.-D., Wiese, M., McConville, M. J. & Overath, P. (1994b). Characterization of phosphoglycan-containing secretory products of Leishmania. Parasitol. 108, 63-71.
11. Ilg, T., Stierhof, Y-D., McConville, M. J. & Overath, P. (1995). Purification, partial characterization and immunolocalization of a proteophosphoglycan secreted by Leishmania mexicana amastigotes. Eur. J. Cell Biol. 66, 205-215.
12. Ilg, T., Stierhof, Y.-D., Craik, D., Simpson, R., Handman, E. & Bacic, A. (1996). Purification and structural characterization of a filamentous, mucin-like proteo-phosphoglycan secreted by Leishmania parasites. J. Biol. Chem. 271, 21583-21596.
13. Ilg, T., Craik, D., Currie, G., Multhaup, G. & Bacic, A. (1998). Stage-specific proteophosphoglycan from Leishmania mexicana amastigotes. Structural characterization of novel mono-, di-, and tri-phosphorylated phosphodiester-linked oligosaccharides. J. Biol. Chem. 273, 13509-13523.
14. Jap, B. K., Zulauf, M., Scheybani, T., Hefti, A., Baumeister, W., Aebi, U. & Engel, A. (1992). 2D crystallization: from art to science. Ultramicroscopy, 46, 45-84.
15. Jentoft, N. (1990). Why are proteins O-glycosylated? Trends Biochem. Sci. 15, 291-294.
16. Lang, T., Warburg, A., Sacks, D. L., Croft, S. L., Lane, R. P. & Blackwell, J. M. (1991). Transmission and scanning EM-immunogold labeling of Leishmania major lipophosphoglycan in the sandfly Phlebotomus papatasi. Eur. J. Cell Biol. 55, 362-372.
17. LeBowitz, J. H., Coburn, C. M., McMahon-Pratt, D. & Beverley, S. M. (1990). Development of a stable Leishmania expression vector and application to the study of parasite surface antigen genes. Proc. Natl Acad. Sci. USA, 87, 9736-9740.
18. Lovelace, J. D. & Gottlieb, M. (1986). Comparison of extracellular acid phosphatase from various isolates of Leishmania. Am. J. Trop. Med. Hyg. 35, 1121-1128.
19. McConville, M. J. & Ferguson, M. A. J. (1993). The structure, biosynthesis and function of glycosylated phosphatidylinositols in the parasitic protozoa and higher eukaryotes. Biochem. J. 294, 305-324.
20. Mörgelin, M., Paulsson, M., Heinegard, D., Aebi, U. & Engel, J. (1995). Evidence of a defined spatial arrangement of hyaluronate in the central filament of cartilage proteoglycan aggregates. Biochem. J. 307, 595-601.
21. Müller, S., Goldie, K. N., Bürkli, R., Häring, R., Engel, A. & Reichelt, R. (1992). Factors influencing the precision of quantitative scanning transmission electron microscopy. Ultramicroscopy, 46, 317-334.
22. Overath, P., Stierhof, Y.-D. & Wiese, M. (1997). Endocytosis and secretion in trypanosomatid parasites -tumultuous traffic in a pocket. Trends Cell Biol. 7, 27-33.
23. Paulsson, M., Mörgelin, M., Wiedemann, H., Beardmore-Gray, M., Dunham, D., Hardingham, T., Heinegard, D., Timpl, R. & Engel, J. (1987). Extended and globular protein domains in cartilage proteoglycans. Biochem. J. 245, 763-772.
24. Peters, C., Stierhof, Y.-D. & Ilg, T. (1997). Proteophosphoglycan secreted by Leishmania mexicana amastigotes causes vacuole formation in macrophages. Infect. Immun. 65, 783-786.
25. Rosenberg, L., Hellmann, W. & Kleinschmidt, A. K. (1975). Electron microscopic studies of proteoglycan aggregates from bovine articular cartilage. J. Biol. Chem. 250, 1877-1883.
26. Shakarian, A. M., Ellis, S. L., Mallinson, D. J., Olafson, R. W. & Dwyer, D. M. (1997). Two tandemly arrayed genes encode the (histidine) secretory acid phosphatases of Leishmania donovani. Gene, 196, 127-137.
27. Stierhof, Y.-D., Ilg, T., Russell, D. G., Hohenberg, H. & Overath, P. (1994). Characterization of polymer release from the flagellar pocket of Leishmania mexicana promastigotes. J. Cell Biol. 125, 321-331.
28. Turco, S. J. & Descoteaux, A. (1992). The lipophosphoglycan of Leishmania parasites. Annu. Rev. Microbiol. 46, 65-94.
29. Tyler, J. M. & Branton, D. (1980). Rotary shadowing of extended molecules dried from glycerol. J. Ultrastruct. Res. 71, 95-102.
30. Walters, L. L., Modi, G. B., Tesh, R. B. & Burrage, T. (1987). Host-parasite relationship of Leishmania mexicana mexicana and Lutzomyia abonnecti (Diptera: Psychodidae). Am. J. Trop. Med. Hyg. 36, 294-314.
31. Webster, P. & Russell, D. G. (1993). The flagellar pocket of trypanosomatids. Parasitol. Today, 9, 201-206.
32. Wiedemann, H., Paulsson, M., Timpl, R., Engel, J. & Heinegard, D. (1984). Domain structure of cartilage proteoglycans revealed by rotary shadowing of intact and fragmented molecules. Biochem. J. 224, 331-333.
33. Wiese, M. (1998). A mitogen activated protein (MAP) kinase homologue of Leishmania mexicana is essential for parasite survival in the infected host. EMBO J. 17, 2619-2628.
34. Wiese, M., Ilg, T., Lottspeich, F. & Overath, P. (1995). Ser/Thr-rich repetitive motifs as targets for phosphoglycan modifications in Leishmania mexicana secreted acid phosphatase. EMBO J. 14, 1067-1074.
35. Wiese, M., Berger, O., Stierhof, Y.-D., Wolfram, M., Fuchs, M. & Overath, P. (1996). Gene cloning and cellular localization of a membrane-bound acid phosphatase of Leishmania mexicana. Mol. Biochem. Parasitol. 82, 153-165.