gp63 homologues in Trypanosoma cruzi: Surface antigens with metalloprotease activity and a possible role in host cell infection

Infection and Immunity

Volumn 71, Issue 10, 2003, Pages 5739-5749

  Cuevas, Ileana C ^a   Cazzulo, Juan J ^a   Sánchez, Daniel O ^a  

^a INSTITUTO DE INVESTIGACIONES BIOTECNOLÓGICAS   (Argentina)

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN; GLYCOPROTEIN GP 63; MEMBRANE ANTIGEN; MEMBRANE PROTEIN; METALLOPROTEINASE; PHOSPHATIDYLINOSITOL; PHOSPHOLIPASE C; UNCLASSIFIED DRUG;

AMASTIGOTE; ARTICLE; CHAGAS DISEASE; ENZYME ACTIVITY; HOST PARASITE INTERACTION; IMMUNOFLUORESCENCE; LEISHMANIA; LIFE CYCLE; NONHUMAN; NORTHERN BLOTTING; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROMASTIGOTE; PROTEIN FUNCTION; SEQUENCE HOMOLOGY; TRYPANOSOMA CRUZI; TRYPOMASTIGOTE; VERO CELL; WESTERN BLOTTING;

AMINO ACID SEQUENCE; ANIMALS; ANTIGENS, PROTOZOAN; ANTIGENS, SURFACE; BASE SEQUENCE; CERCOPITHECUS AETHIOPS; DNA, PROTOZOAN; GENES, PROTOZOAN; LEISHMANIA; METALLOENDOPEPTIDASES; MOLECULAR SEQUENCE DATA; PROTOZOAN PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SPECIES SPECIFICITY; TRYPANOSOMA CRUZI; VERO CELLS; VIRULENCE;

EID: 0141780967     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.71.10.5739-5749.2003     Document Type: Article

References (56)

1. Agüero, F., R. E. Verdún, A. C. C. Frasch, and D. O. Sánchez. 2000. A random sequencing approach for the analysis of the Trypanosoma cruzi genome: general structure, large gene and repetitive DNA families, and gene discovery. Genome Res. 10:1996-2005.
2. Bangs, J. D., D. A. Ransom, M. Nimick, G. Christie, and N. M. Hooper. 2001. In vitro cytocidal effects on Typanosoma brucei and inhibition of Leishmania major gp63 by peptidomimetic metalloprotease inhibitors. Mol. Biochem. Parasitol. 114:111-117.
3. Bonaldo, M. C., L. N. d'Escoffier, J. M. Salles, and S. Goldenberg. 1991. Characterization and expression of proteases during Trypanosoma cruzi metacyclogenesis. Exp. Parasitol. 73:44-51.
4. Bouvier, J., C. Bordier, H. Vogel, R. Reichelt, and R. Etges. 1989. Characterization of the promastigote surface protease of Leishmania as a membrane-bound zinc endopeptidase. Mol. Biochem. Parasitol. 37:235-245.
5. Bouvier, J., R. J. Etges, and C. Bordier. 1985. Identification and purification of membrane and soluble forms of the major surface protein of Leishmania promastigotes. J. Biol. Chem. 260:15504-15509.
6. Bouvier, J., P. Schneider, and R. Etges. 1995. Leishmanolysin: surface metalloproteinase of Leishmania. Methods Enzymol. 248:614-633.
7. Butler, M. J. 1998. Leishmanolysin, p. 1135-1140. In A. J. Barret, N. D. Rawlings, and J. F. Woessner (ed.), Handbook of proteolytic enzymes. Academic Press, San Diego, Calif.
8. Button, L. L., and W. R. McMaster. 1988. Molecular cloning of the major surface antigen of Leishmania. J. Exp. Med. 167:724-729.
9. Button, L. L., D. G. Russell, H. L. Klein, E. Medina-Acosta, R. E. Karess, and W. R. McMaster. 1989. Genes encoding the major surface glycoprotein in Leishmania are tandemly linked at a single chromosomal locus and are constitutively transcribed. Mol. Biochem. Parasitol. 32:271-283.
10. Camargo, E. P. 1964. Growth and differentiation in Trypanosoma cruzi. I. Origin of metacyclic trypanosomes in liquid media. Rev. Inst. Med. Trop. Sao Paulo 6:93-100.
11. Chang, C. S., and K. P. Chang. 1986. Monoclonal antibody affinity purification of a Leishmania membrane glycoprotein and its inhibition of Leishmania-macrophage binding. Proc. Natl. Acad. Sci. USA 83:100-104.
12. Chaudhuri, G., M. Chaudhuri, A. Pan, and K. P. Chang. 1989. Surface acid proteinase (gp63) of Leishmania mexicana. A metalloenzyme capable of protecting liposome-encapsulated proteins from phagolysosomal degradation by macrophages. J. Biol. Chem. 264:7483-7489.
13. D'Orsö, I., and A. C. Frasch. 2001. TcUBP-1, a developmentally regulated U-rich RNA-binding protein involved in selective mRNA destabilization in trypanosomes. J. Biol. Chem. 276:34801-34809.
14. Ellis, M., D. K. Sharma, J. D. Hilley, G. H. Coombs, and J. C. Mottram. 2002. Processing and trafficking of Leishmania mexicana gp63. Analysis using GP18 mutants deficient in glycosylphosphatidylinositol protein anchoring. J. Biol. Chem. 277:27968-27974.
15. El-Sayed, N. M., and J. E. Donelson. 1997. African trypanosomes have differentially expressed genes encoding homologues of the Leishmania gp63 surface protease. J. Biol. Chem. 272:26742-26748.
16. Espinoza, J. R., A. C. Skinner, C. R. Davies, A. Llanos-Cuentas, J. Arevalo, C. Dye, W. R. McMaster, J. W. Ajioka, and J. M. Blackwell. 1995. Extensive polymorphism at the Gp63 locus in field isolates of Leishmania peruviana. Mol. Biochem. Parasitol. 72:203-213.
17. Etges, R., J. Bouvier, and C. Bordier. 1986. The major surface protein of Leishmania promastigotes is a protease. J. Biol. Chem. 261:9098-9101.
18. Etges, R., J. Bouvier, and C. Bordier. 1986. The major surface protein of Leishmania promastigotes is anchored in the membrane by a myristic acid-labeled phospholipid. EMBO J. 5:597-601.
19. Etges, R. J., J. Bouvier, R. Hoffman, and C. Bordier. 1985. Evidence that the major surface proteins of three Leishmania species are structurally related. Mol. Biochem. Parasitol. 14:141-149.
20. Franke de Cazzulo, B. M., J. Martínez, M. J. North, G. H. Coombs, and J. J. Cazzulo. 1994. Effects of proteinase inhibitors on the growth and differentiation of Trypanosoma cruzi. FEMS Microbiol. Lett. 124:81-86.
21. Frasch, A. C. C. 2000. Functional diversity in the trans-sialidase and mucin families in Trypanosoma cruzi. Parasitol. Today 16:282-286.
22. Grandgenett, P. M., B. C. Coughlin, L. V. Kirchhoff, and J. E. Donelson. 2000. Differential expression of gp63 genes in Trypanosoma cruzi. Mol. Biochem. Parasitol. 110:409-415.
23. Greig, S., and F. Ashall. 1990. Electrophoretic detection of Trypanosoma cruzi peptidases. Mol. Biochem. Parasitol. 39:31-37.
24. Hanke, J., D. O. Sánchez, J. Henrihsson, L. Aslund, U. Pettersson, A. C. Frasch, and J. D. Hoheisel. 1996. Mapping the Trypanosoma cruzi genome: analyses of representative cosmid libraries. BioTechniques 21:686-688, 690-693.
25. Harlow, E., and D. Lane. 1999. Using antibodies: a laboratory manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
26. Inverso, J. A., E. Medina-Acosta, J. O'Connor, D. G. Russell, and G. A. Cross. 1993. Crithidia fasciculata contains a transcribed leishmanial surface proteinase (gp63) gene homologue. Mol. Biochem. Parasitol. 57:47-54.
27. Joshi, P. B., B. L. Kelly, S. Kamhawi, D. L. Sacks, and W. R. McMaster. 2002. Targeted gene deletion in Leishmania major identifies leishmanolysin (gp63) as a virulence factor. Mol. Biochem. Parasitol. 120:33-40.
28. LaCount, D. J., A. E. Gruszynsky, P. M. Grandgenett, J. D. Bangs, and J. E. Donelson. 2003. Expression and function of TbMSP (gp63) genes in African trypanosomes. J. Biol. Chem. 278:24658-24664.
29. Lowndes, C. M., M. C. Bonaldo, N. Thomaz, and S. Goldenberg. 1996. Heterogeneity of metalloprotease expression in Trypanosoma cruzi. Parasitology 112:393-399.
30. Macdonald, M. H., C. J. Morrison, and W. R. McMaster. 1995. Analysis of the active site and activation mechanism of the Leishmania surface metalloproteinase gp63. Biochim. Biophys. Acta 1253:199-207.
31. McGwire, B., and K. P. Chang. 1994. Genetic rescue of surface metalloproteinase (gp63) deficiency in Leishmania amazonensis variants increases their infection of macrophages at the early phase. Mol. Biochem. Parasitol. 66:345-347.
32. McGwire, B. S., and K. P. Chang. 1996. Posttranslational regulation of a Leishmania HEXXH metalloprotease (gp63). The effects of site-specific mutagenesis of catalytic, zinc binding, N-glycosylation, and glycosyl phosphatidylinositol addition sites on N-terminal end cleavage, intracellular stability, and extracellular exit. J. Biol. Chem. 271:7903-7909.
33. Medina-Acosta, E., R. E. Karess, and D. G. Russell. 1993. Structurally distinct genes for the surface protease of Leishmania mexicana are developmentally regulated. Mol. Biochem. Parasitol. 57:31-45.
34. Medina-Acosta, E., R. E. Karess, H. Schwartz, and D. G. Russell. 1989. The promastigote surface protease (gp63) of Leishmania is expressed but differentially processed and localized in the amastigote stage. Mol. Biochem. Parasitol. 37:263-273.
35. Mertz, L. M., and A. Rashtchian. 1994. Nucleotide imbalance and polymerase chain reaction: effects on DNA amplification and synthesis of high specific activity radiolabeled DNA probes. Anal. Biochem. 221:160-165.
36. Moran, P., and I. W. Caras. 1994. Requirements for glycosylphosphatidylinositol attachment are similar but not identical in mammalian cells and parasitic protozoa. J. Cell Biol. 125:333-343.
37. Neira, I., F. A. Silva, M. Cortez, and N. Yoshida. 2003. Involvement of Trypanosoma cruzi metacyclic trypomastigotes surface molecule gp82 in adhesion to gastric mucin and invasion of epithelial cells. Infect. Immun. 71:557-561.
38. Nielsen, H., J. Engelbrecht, S. Brunak, and G. von Heine. 1997. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Prot. Eng. 10:1-6.
39. Puentes, F., F. Guzman, V. Marin, C. Alonso, M. E. Patarroyo, and A. Moreno. 1999. Leishmania: fine mapping of the Leishmanolysin molecule's conserved core domains involved in binding and internalization. Exp. Parasitol. 93:7-22.
40. Ramamoorthy, R., J. E. Donelson, K. E. Paetz, M. Maybodi, S. C. Roberts, and M. E. Wilson. 1992. Three distinct RNAs for the surface protease gp63 are differentially expressed during development of Leishmania donovani chagasi promastigotes to an infectious form. J. Biol. Chem. 267:1888-1895.
41. Roberts, S. C., K. G. Swihart, M. W. Agey, R. Ramamoorthy, M. E. Wilson, and J. E. Donelson. 1993. Sequence diversity and organization of the msp gene family encoding gp63 of Leishmania chagasi. Mol. Biochem. Parasitol. 62:157-171.
42. 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.
43. Russell, D. G., and S. D. Wright. 1988. Complement receptor type 3 (CR3) binds to an Arg-Gly-Asp-containing region of the major surface glycoprotein, gp63, of Leishmania promastigotes. J. Exp. Med. 168:279-292.
44. Sambrook, J., and D. W. Russell. 2001. Molecular cloning: a laboratory manual, 3rd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
45. Schneider, P., and T. A. Glaser. 1993. Characterization of a surface metalloprotease from Herpetomonas samuelpessoai and comparison with Leishmania major promastigote surface protease. Mol. Biochem. Parasitol. 58:277-282.
46. Schneider, P., J. P. Rosat, J. Bouvier, J. Louis, and C. Bordier. 1992. Leishmania major: differential regulation of the surface metalloprotease in amastigote and promastigote stages. Exp. Parasitol. 75:196-206.
47. Seay, M. B., P. L. Heard, and G. Chaudhuri. 1996. Surface Zn-proteinase as a molecule for defense of Leishmania mexicana amazonensis promastigotes against cytolysis inside macrophage phagolysosomes. Infect. Immun. 64:5129-5137.
48. Soteriadou, K. P., M. S. Remoundos, M. C. Katsikas, A. K. Tzinia, V. Tsikaris, C. Sakarellos, and S. J. Tzartos. 1992. The Ser-Arg-Tyr-Asp region of the major surface glycoprotein of Leishmania mimics the Arg-Gly-Asp-Ser cell attachment region of fibronectin. J. Biol. Chem. 267:13980-13985.
49. Steinkraus, H. B., J. M. Greer, D. C. Stephenson, and P. J. Langer. 1993. Sequence heterogeneity and polymorphic gene arrangements of the Leishmania guyanensis gp63 genes. Mol. Biochem. Parasitol. 62:173-185.
50. Victoir, K., A. L. Banuls, J. Arevalo, A. Llanos-Cuentas, R. Hamers, S. Noel, S. De Doncker, D. Le Ray, M. Tibayrenc, and J. C. Dujardin. 1998. The gp63 gene locus, a target for genetic characterization of Leishmania belonging to subgenus Viannia. Parasitology 117:1-13.
51. Victoir, K., J. C. Dujardin, S. de Doncker, D. C. Barker, J. Arevalo, R. Hamers, and D. Le Ray. 1995. Plasticity of gp63 gene organization in Leishmania (Viannia) braziliensis and Leishmania (Viannia) peruviana. Parasitology 111:265-273.
52. Voth, B. R., B. L. Kelly, P. B. Joshi, A. C. Ivens, and W. R. McMaster. 1998. Differentially expressed Leishmania major gp63 genes encode cell surface leishmanolysin with distinct signals for glycosylphosphatidylinositol attachment. Mol. Biochem. Parasitol. 93:31-41.
53. Webb, J. R., L. L. Button, and W. R. McMaster. 1991. Heterogeneity of the genes encoding the major surface glycoprotein of Leishmania donovani. Mol. Biochem. Parasitol. 48:173-184.
54. Wilson, M. E., and K. K. Hardin. 1990. The major Leishmania donovani chagasi surface glycoprotein in tunicamycin-resistant promastigotes. J. Immunol. 144:4825-4834.
55. World Health Organization. 1997. Tropical disease research, progress 1995-1996. WHO Publications, Geneva, Switzerland.
56. Zingales, B., M. E. Pereira, R. P. Oliveira, K. A. Almeida, E. S. Umezawa, R. P. Souto, N. Vargas, M. I. Cano, J. F. da Silveira, N. S. Nehme, C. M. Morel, Z. Brener, and A. Macedo. 1997. Trypanosoma cruzi genome project: biological characteristics and molecular typing of clone CL Brener. Acta Trop. 68:159-173.