The crystal structure of the Leishmania major surface proteinase leishmanolysin (gp63)

Structure

Volumn 6, Issue 8, 1998, Pages 1035-1046

  Schlagenhauf, Edith ^a,b   Etges, Robert ^a,c   Metcalf, Peter ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^b UNIVERSITY OF ZURICH   (Switzerland)

^c Inst F Biomedizinsche Forsch B   (Germany)

Author keywords

Crystal structure; Gp63; Leishmania; Leishmanolysin

Indexed keywords

ANIMALIA; INSECTA; LEISHMANIA MAJOR; MAMMALIA; PHLEBOTOMINAE; PROTOZOA;

EID: 0032529002     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(98)00104-X     Document Type: Article

References (45)

1. Desjeux, P. (1992). Human leishmaniases: epidemiology and public health aspects. World Health Stat Q. 45, 267-275.
2. WHO. (1990). Control of the leishmaniases: report of a WHO Expert Committee. WHO Technical Report Series 793.
3. Etges, R. (1992). Identification of a surface metalloproteinase on 13 species of Leishmania isolated from humans, Crithidia fasciculata, and Herpetomonas samuelpessoai. Acta Tropica 50, 205-217.
4. Russell, D.G. & Wilhelm, H. (1986). The involvement of the major surface glycoprotein (gp63) of Leishmania promastigotes in attachment to macrophages. J. Immunol. 136, 2613-2621.
5. Russell, D.G. (1987). The macrophage-attachment glycoprotein gp63 is the predominant C3-acceptor site on Leishmania mexicana promastigotes. Eur. J. Biochem. 164, 213-221.
6. Puentes, S.M., Dwyer, D.M., Bates, P.A. & Joiner, K.A. (1989). Binding and release of C3 from Leishmania donovani promastigotes during incubation in normal human serum. J. Immunol. 143, 3743-3749.
7. Connell, N.D., Medina-Acosta, E., McMaster, W.R., Bloom, B.R. & Russell, D.G. (1993). Effective immunization against cutaneous leishmaniasis with recombinant bacille Calmette-Guerin expressing the Leishmania surface proteinase gp63. Proc. Natl Acad. Sci. USA 90, 11473-11477.
8. Schneider, P., Ferguson, M.A.J., McConville, M.J., Mehlert, A., Homans, S.W. & Bordier, C. (1990). Structure of the glycosylphosphatidylinositol membrane anchor of the Leishmania major promastigote surface protease. J. Biol. Chem. 265, 16955-16964.
9. Etges, R., Bouvier, J. & Bordier, C. (1986). The major surface protein of Leishmania promastigotes is a protease. J. Biol. Chem. 261, 9098-9101.
10. El-Sayed, N.M. & Donelson, J.E. (1997). African trypanosomes have differentially expressed genes encoding homologues of the Leishmania GP63 surface protease. J. Biol. Chem. 272, 26742-26748.
11. McConville, M.J. & Ferguson, M.A. (1993). The structure, biosynthesis and function of glycosylated phosphatidylinositols in the parasitic protozoa and higher eukaryotes. Biochem. J. 294, 305-324.
12. Warburg, A. & Schlein, Y. (1986). The effect of post-bloodmeal nutrition of Phlebotomus papatasi on the transmission of Leishmania major. Am. J. Trop. Med. Hyg. 35, 926-930.
13. Schneider, P., Rosat, J.P., Bouvier, J., Louis, J. & Bordier, C. (1992). Leishmania major: differential regulation of the surface metalloprotease in amastigote and promastigote stages. Exp. Parasitol. 75, 196-206.
14. Ilg, T., Harbecke, D. & Overath, P. (1993). The lysosomal gp63-related protein in Leishmania mexicana amastigotes is a soluble metalloproteinase with an acidic pH optimum. FEBS Lett. 327, 103-107.
15. Schlagenhauf, E. (1995). X-Ray Crystallographic Studies of Leishmanolysin, the Major Surface Metalloproteinase from Leishmania major. PhD thesis, University of Heidelberg, Germany.
16. Bouvier, J., Schneider, P. & Etges, R. (1995). Leishmanolysin: surface metalloproteinase of Leishmania. Methods Enzymol. 248, 614-633.
17. Schlagenhauf, E., Etges, R. & Metcalf, P. (1995). Crystallization and preliminary X-ray diffraction studies of leishmanolysin, the major surface metalloproteinase from Leishmania major. Proteins 22, 55-66.
18. Freymann, D., Down, J., Carrington, I., Roditi, I., Turner, M. & Wiley, D. (1990). 2.9 A Resolution structure of the N-terminal domain of a variant surface glycoprotein from Trypanosoma brucei. J. Mol. Biol. 216, 141-160.
19. Blum, M.J., Down, J.A., Gurnett, A.M., Carrington, M., Turner, M.J. & Wiley, D.C. (1993). A structural motif in the variant surface glycoproteins of Trypanosoma brucei. Nature 362, 603-609.
20. Stöcker, W. & Bode, W. (1995). Structural features of a superfamily of zinc-endopeptidases: the metzincins. Curr. Opin. Struct. Biol. 5, 383-390.
21. Stöcker, W., et al., & Bode, W. (1995). The metzincins - topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases. Protein Sci. 4, 823-840.
22. Bode, W., Gomis-Rüth, F.X., Huber, R., Zwilling, R. & Stöcker, W. (1992). Structure of astacin and implications for activation of astacins and zinc-ligation of collagenases. Nature 358, 164-167.
23. Bode, W., Reinemer, P., Huber, R., Kleine, T., Schnierer, S. & Tschesche, H. (1994). The X-ray crystal structure of the catalytic domain of human neutrophil collagenase inhibited by a substrate analogue reveals the essentials for catalysis and specificity. EMBO J. 13, 1263-1269.
24. Gomis-Ruth, F., et al., & Bode, W. (1997). Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1. Nature 389, 77-81.
25. Sussman, J.L., et al., & Silman, I. (1991). Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Science 253, 872-879.
26. Streit, J.A., Donelson, J.E., Agey, M.W. & Wilson, M.E. (1996). Developmental changes in the expression of Leishmania chagasi gp63 and heat shock protein in a human macrophage cell line. Infect. Immun. 64, 1810-1818.
27. Button, L.L., Russell, D.G., Klein, H.L., Medina-Acosta, E., Karess, R.E. & McMaster, W.R. (1989). Genes encoding the major surface glycoprotein in Leishmania are tandemly linked at a single chromosomal locus and are constitutively transcribed. Mol. Biochem. Parasitol. 32, 271-284.
28. Victoir, K., Dujardin, J.C., de Doncker, S., Barker, D.C., Arevalo, J., Hamers, R. & Le Ray, D. (1995). Plasticity of gp63 gene organization in Leishmania (Viannia) braziliensis and Leishmania (Viannia) peruviana. Parasitology 111, 265-273.
29. Espinoza, J.R., et al., & Blackwell, J.M. (1995). Extensive polymorphism at the Gp63 locus in field isolates of Leishmania peruviana. Mol. Biochem. Parasitol. 72, 203-213.
30. Medina-Acosta, E., Karess, R.E. & Russell, D.G. (1993). Structurally distinct genes for the surface protease of Leishmania mexicana are developmentally regulated. Mol. Biochem. Parasitol. 57, 31-45.
31. Webb, J.R., Button, L.L. & McMaster, W.R. (1991). Heterogeneity of the genes encoding the major surface glycoprotein of Leishmania donovani. Mol. Biochem. Parasitol. 48, 173-184.
32. Steinkraus, H.B., Greer, J.M., Stephenson, D.C. & Langer, P.J. (1993). Sequence heterogeneity and polymorphic gene arrangements of the Leishmania guyanensis gp63 genes. Mol. Biochem. Parasitol. 62, 173-186.
33. Pace, N.R. (1997). A molecular view of microbial diversity and the biosphere. Science 276, 734-740.
34. Brittingham, A., Morrison, C.J., McMaster, W.R., McGwire, B.S., Chang, K.P. & Mosser, D.M. (1995). Role of the Leishmania surface protease gp63 in complement fixation, cell adhesion, and resistance to complement-mediated lysis. J. Immunol. 155, 3102-3111.
35. Collaborative Computational Project, No. 4. (1994). The CCP4 suite: programs for protein crystallography. Acta Cryst. D 50, 760-763.
36. Jones, T.A., Zou, J.-Y., Cowan, S.W. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst A 47, 110-119.
37. Bystroff, C., Baker, D., Fletterick, R.J. & Agard, D.A. (1993). PRISM: application to the solution of two protein structures. Acta Cryst. D 49, 440-448.
38. Brünger, A.T. (1992). X-PLOR, Version 3.1, a System for X-Ray Crystallography and NMR. Yale University Press, New Haven, CT.
39. Carson, M. (1991). Ribbons 2.0. J. Appl. Cryst. 24, 958-961.
40. Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950.
41. Nicholls, A. Sharp, K. & Honig, B. (1991). Protein folding and association: insights from the interfacial and thermodynamics properties of hydrocarbons. Proteins 11, 281-296.
42. Felsenstein, J. (1993). PHYLIP (phylogeny inference package). Cladistics 5, 164-166.
43. Thompson, J.D., Higgins, D.G. & Gibson, T.J. (1994). CLUSTALW: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680.
44. Grams, F., et al., & Bode, W. (1995). X-ray structures of human neutrophil collagenase complexed with peptide hydroxamate and peptide thiol inhibitors. Implications for substrate binding and rational drug design. Eur. J. Biochem. 228, 830-841.
45. Devereux, J. (1995). Wisconsin Package Version 9.0. Genetics Computer Group (GCG), Madison, WI.