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Molecular cloning and functional characterisation of a cathepsin L-like proteinase from the fish kinetoplastid parasite Trypanosoma carassii.
Fish Shellfish Immunol. 2008 Feb; 24(2):205-14.FS

Abstract

Trypanosoma carassii is a fish kinetoplastid parasite that belongs to the family Trypanosomatida. In the present study we cloned a cathepsin L-like proteinase from T. carassii. The nucleotide sequence of 1371bp translated into a preproprotein of 456 amino acids. The preproprotein contained the oxyanion hole (Gln), the active triad formed by Cys, His and Asn and the conserved ERFNIN-like, GNFD and GCNGG motifs, characteristic for cathepsin L proteinases. Phylogenetic analysis showed that the T. carassii cysteine proteinase clustered with other cathepsin L-like proteinases from the Trypanosomatida. We produced a recombinant T. carassii cysteine proteinase in Escherichia coli and demonstrated that it has cathepsin L activity. Immunization of common carp (Cyprinus carpio L.) with the recombinant protein induced a very high increase in proteinase-specific antibodies but only slightly lowered parasitaemia. Our findings suggest that the T. carassii cysteine proteinase is highly conserved within the Trypanosomatida with respect to structure and activity but is not a major protective antigen in carp.

Authors+Show Affiliations

Ruszczyk A
Cell Biology and Immunology Group, Wageningen Institute of Animal Sciences, Wageningen University, Wageningen, The Netherlands.
Forlenza M
No affiliation info available
Savelkoul HF
No affiliation info available
Wiegertjes GF
No affiliation info available

MeSH

Amino Acid SequenceAnimalsAntibodies, ProtozoanCarpsCathepsin LCathepsinsCloning, MolecularCysteine EndopeptidasesDNA, ComplementaryDNA, KinetoplastEscherichia coliFish DiseasesMolecular Sequence DataPhylogenyProtozoan ProteinsRecombinant ProteinsSequence AlignmentTime FactorsTrypanosomaTrypanosomiasisVaccination

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

18162408

Citation

Ruszczyk, Aleksandra, et al. "Molecular Cloning and Functional Characterisation of a Cathepsin L-like Proteinase From the Fish Kinetoplastid Parasite Trypanosoma Carassii." Fish & Shellfish Immunology, vol. 24, no. 2, 2008, pp. 205-14.
Ruszczyk A, Forlenza M, Savelkoul HF, et al. Molecular cloning and functional characterisation of a cathepsin L-like proteinase from the fish kinetoplastid parasite Trypanosoma carassii. Fish Shellfish Immunol. 2008;24(2):205-14.
Ruszczyk, A., Forlenza, M., Savelkoul, H. F., & Wiegertjes, G. F. (2008). Molecular cloning and functional characterisation of a cathepsin L-like proteinase from the fish kinetoplastid parasite Trypanosoma carassii. Fish & Shellfish Immunology, 24(2), 205-14.
Ruszczyk A, et al. Molecular Cloning and Functional Characterisation of a Cathepsin L-like Proteinase From the Fish Kinetoplastid Parasite Trypanosoma Carassii. Fish Shellfish Immunol. 2008;24(2):205-14. PubMed PMID: 18162408.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Molecular cloning and functional characterisation of a cathepsin L-like proteinase from the fish kinetoplastid parasite Trypanosoma carassii. AU - Ruszczyk,Aleksandra, AU - Forlenza,Maria, AU - Savelkoul,Huub F J, AU - Wiegertjes,Geert F, Y1 - 2007/11/21/ PY - 2007/07/26/received PY - 2007/10/19/revised PY - 2007/10/26/accepted PY - 2007/12/29/pubmed PY - 2008/11/5/medline PY - 2007/12/29/entrez SP - 205 EP - 14 JF - Fish & shellfish immunology JO - Fish Shellfish Immunol VL - 24 IS - 2 N2 - Trypanosoma carassii is a fish kinetoplastid parasite that belongs to the family Trypanosomatida. In the present study we cloned a cathepsin L-like proteinase from T. carassii. The nucleotide sequence of 1371bp translated into a preproprotein of 456 amino acids. The preproprotein contained the oxyanion hole (Gln), the active triad formed by Cys, His and Asn and the conserved ERFNIN-like, GNFD and GCNGG motifs, characteristic for cathepsin L proteinases. Phylogenetic analysis showed that the T. carassii cysteine proteinase clustered with other cathepsin L-like proteinases from the Trypanosomatida. We produced a recombinant T. carassii cysteine proteinase in Escherichia coli and demonstrated that it has cathepsin L activity. Immunization of common carp (Cyprinus carpio L.) with the recombinant protein induced a very high increase in proteinase-specific antibodies but only slightly lowered parasitaemia. Our findings suggest that the T. carassii cysteine proteinase is highly conserved within the Trypanosomatida with respect to structure and activity but is not a major protective antigen in carp. SN - 1050-4648 UR - https://www.unboundmedicine.com/medline/citation/18162408/Molecular_cloning_and_functional_characterisation_of_a_cathepsin_L_like_proteinase_from_the_fish_kinetoplastid_parasite_Trypanosoma_carassii_ DB - PRIME DP - Unbound Medicine ER -