The Ld Cht1 gene encodes the secretory chitinase of the human pathogen Leishmania donovani

Gene

Volumn 208, Issue 2, 1998, Pages 315-322

  Shakarian, Alison M ^a   Dwyer, Dennis M ^a  

^a Laboratory of Parasitic Diseases   (United States)

Author keywords

1,4 N acetylglucosaminohydrolase; Gene structure; Human parasite; Kinetoplastid; Leishmaniasis; Trypanosomatid

Indexed keywords

ANTISERUM; CHITINASE; SECRETORY PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; CELL GROWTH; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME RELEASE; ENZYME SUBSTRATE COMPLEX; GENE AMPLIFICATION; GENE ISOLATION; GENE STRUCTURE; GENETIC TRANSCRIPTION; IMMUNOPRECIPITATION; LEISHMANIA DONOVANI; NONHUMAN; OPEN READING FRAME; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; RNA TRANSLATION;

AMINO ACID SEQUENCE; ANIMALS; ANTIBODIES; BASE SEQUENCE; BINDING SITES; CHITINASE; CONSERVED SEQUENCE; GENES, PROTOZOAN; HUMANS; LEISHMANIA DONOVANI; MOLECULAR SEQUENCE DATA; OPEN READING FRAMES; PEPTIDE FRAGMENTS; POLYMERASE CHAIN REACTION; PROTEIN BIOSYNTHESIS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; TRANSCRIPTION, GENETIC;

EID: 0032570604     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(98)00011-0     Document Type: Article

References (28)

1. Arnold K., Gooday G. Chitinases in Trypanosomatidae: a cautionary note. Parasitol. Today. 8:1992;273.
2. Bates P.A., Hermes I., Dwyer D.M. Golgi-mediated post-translational processing of secretory acid phosphatase by Leishmania donovani promastigotes. Mol. Biochem. Parasitol. 39:1990;247-256.
3. de la Vega H., Specht C.A., Semino C.E., Robbins P.W., Eichinger D., Caplivski D., Ghosh S., Samuelson J. Cloning and expression of chitinases of Entamoebae. Mol. Biochem. Parasitol. 85:1997;139-147.
4. Devereaux J., Haeberli P., Smithies O. A comprehensive set of sequence analysis programs for the Convex. Nucleic Acids Res. 12:1984;387-395.
5. Doyle P.S., Dwyer D.M. Leishmania: immunochemical comparison of the secretory (extracellular) acid phosphatases from various species. Exp. Parasitol. 77:1993;435-444.
6. Flach J., Pilet P.E., Jolles P. What's new in chitinase research? Experientia. 48:1992;701-716.
7. Fuhrman J.A., Lane W.S., Smith R.F., Piessens W.F., Perler F.B. Transmission-blocking antibodies recognize microfilarial chitinase in brugian lymphatic filariasis. Proc. Natl. Acad. Sci. USA. 89:1992;1548-1552.
8. Fujii T., Miyashita K. Multiple domain structure in a chitinase gene (chiC) of Streptomyces lividans. J. Gen. Microbiol. 139:1993;677-686.
9. Gerber L.D., Kodukula K., Udenfriend S. Phosphatidylinositol glycan (PI-G) anchored membrane proteins. J. Biol. Chem. 17:1992;12166-12173.
10. Harpster M.H., Dunsmuir P. Nucleotide sequence of the chitinase B gene of Serratia marcescens QMB1466. Nucl. Acids Res. 17:1989;5395.
11. Heitz T., Segond S., Kauffmann S., Geoffroy P., Prasad V., Brunner F., Fritig B., Legrand M. Molecular characterization of a novel tobacco pathogenesis-related (PR) protein: a new plant chitinase/lysozyme. Mol. Gen. Genet. 245(2):1994;246-254.
12. Huber M., Cabib E., Miller L.H. Malaria parasite chitinase and penetration of the mosquito peritrophic membrane. Proc. Natl. Acad. Sci. USA. 88:1991;2807-2810.
13. Kramer K.J., Corpuz L., Choi H.K., Muthukrishnan S. Sequence of a cDNA and expression of the gene encoding epidermal and gut chitinases of Manduca sexta. Insect Biochem. Molec. Biol. 6:1993;691-710.
14. Kyte J., Doolittle R.F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:1982;105-132.
15. Langford C.K., Ullman B., Landfear S.M. Leishmania: codon utilization of nuclear genes. Exp. Parasitol. 74:1992;360-361.
16. Mantei, N. (1992) electronic file, available on the Internet via anonymous ftp from: ftp://bio.indiana.edu.molbiol.
17. McCarthy-Burke C., Bates P.A., Dwyer D.M. Leishmania donovani: use of two different, commercially available, chemically defined media for the continuous in vitro cultivation of promastigotes. Exp. Parasitol. 73:1991;385-387.
18. McCreath K.J., Gooday G.W. A rapid and sensitive microassay for determination of chitinolytic activity. J. Microbiol. Meth. 14:1992;229-237.
19. Pimenta P.F.P., Modi G.B., Pereira S.T., Shahabuddin M., Sacks D.L. A novel role for the peritrophic matrix in protecting Leishmania from the hydrolytic activities of the sand fly midgut. Parasitology. 115(4):1997;359-369.
20. Raghavan N., Freedman D.O., Fitzgerald P.C., Unnasch T.R., Ottesen E.A., Nutman T.B. Cloning and characterization of a potentially protective chitinase-like recombinant antigen from Wuchereria bancrofti. Infect. Immun. 62:1994;1901-1908.
21. Robbins P.W., Albright C., Benfield B. Cloning and expression of a Streptomyces plicatus chitinase (chitinase-63) in Escherichia coli. J. Biol. Chem. 263:1988;443-447.
22. Schlein Y., Jacobson R.L. Haemoglobin inhibits the development of infective promastigotes and chitinase secretion in Leishmania major cultures. Parasitology. 109:1994;23-28.
23. Schlein Y., Jacobson R.L., Shlomai J. Chitinase secreted by Leishmania functions in the sandfly vector. Proc. Roy. Soc. Lond. 245:1991;121-126.
24. Shahabuddin M., Kaslow D.C. Chitinase: a novel target for blocking parasite transmission? Parasitol. Today. 9:1993;252-255.
25. Shahabuddin M., Kaslow D.C. Plasmodium: parasite chitinase and its role in malaria transmission. Exp. Parasitol. 79:1994;85-88.
26. Shakarian A.M., Ellis S.L., Mallinson D.J., Olafson R.W., Dwyer D.M. Two tandemly arrayed genes encode the [histidine] secretory acid phosphatases of Leishmania donovani. Gene. 196:1997;127-137.
27. von Heijne G. Signal sequences. The limits of variation. J. Mol. Biol. 184:1985;99-105.
28. Watanabe T., Suzuki K., Oyanagi W., Ohnisi K., Tanaka H. Gene cloning of chitinase A1 from Bacillus circulans WL-12 revealed its evolutionary relationship to Serratia chitinase and to the type III homology units of fibronectin. J. Biol. Chem. 265:1990;15659-15665.