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Trypanoplasma borreli cysteine proteinase activities support a conservation of function with respect to digestion of host proteins in common carp.
Dev Comp Immunol. 2008; 32(11):1348-61.DC

Abstract

Trypanoplasma borreli is an extracellular parasite that is transmitted by a leech vector and is naturally found in the blood of cyprinid fish. High parasitemia and associated severe anemia together with splenomegaly are typical of infection of common carp, Cyprinus carpio L. Papain-like cysteine proteinases expressed by trypanosome parasites contribute to the pathogenicity of trypanosomes, and are considered an important target for the development of new trypanocidal drugs. T. borreli is a member of the Parabodonida, sharing a common ancestor with the other Kinetoplastida. We demonstrate the presence of a cysteine proteinase expressed by T. borreli. Alignment of the sequence with other kinetoplastid cysteine proteinase sequences supports the phylogenetic hypotheses based on analyses of ribosomal RNA genes. We expressed the T. borreli cysteine proteinase in Escherichia coli, refolded the purified protein into a biologically active proteinase and showed it has cathepsin L-like activity. Addition of the (non)active proteinase to in vitro-derived carp head kidney-derived macrophages did not significantly modulate macrophage activity. Immunization of carp with the recombinant proteinase did induce a very high increase in proteinase-specific antibodies but only slightly lowered parasitemia. Digestion of host hemoglobin and immunoglobulin by the cysteine proteinase likely contribute to the pathogenicity of T. borreli. The possibility that digestion by the cysteine proteinase of host transferrin could contribute to an innate activation profile of macrophages in vivo is discussed. Our findings suggest a conservation of function with respect to cysteine proteinase activity in the Parabodonida in support of the hypotheses on the phylogeny of the Kinetoplastida.

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Authors+Show Affiliations

Ruszczyk A
Cell Biology and Immunology Group, Wageningen Institute of Animal Sciences, Wageningen University, P.O. Box 338, 6700 AH Wageningen, The Netherlands.
Forlenza M
No affiliation info available
Joerink M
No affiliation info available
Ribeiro CM
No affiliation info available
Jurecka P
No affiliation info available
Wiegertjes GF
No affiliation info available

MeSH

Amino Acid SequenceAnimalsCarpsCloning, MolecularCysteine EndopeptidasesFish DiseasesGene Expression RegulationKinetoplastidaMacrophagesMolecular Sequence DataPhylogenyRecombinant ProteinsSequence AlignmentSequence Homology, Amino Acid

Pub Type(s)

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

Language

eng

PubMed ID

18571233

Citation

Ruszczyk, Aleksandra, et al. "Trypanoplasma Borreli Cysteine Proteinase Activities Support a Conservation of Function With Respect to Digestion of Host Proteins in Common Carp." Developmental and Comparative Immunology, vol. 32, no. 11, 2008, pp. 1348-61.
Ruszczyk A, Forlenza M, Joerink M, et al. Trypanoplasma borreli cysteine proteinase activities support a conservation of function with respect to digestion of host proteins in common carp. Dev Comp Immunol. 2008;32(11):1348-61.
Ruszczyk, A., Forlenza, M., Joerink, M., Ribeiro, C. M., Jurecka, P., & Wiegertjes, G. F. (2008). Trypanoplasma borreli cysteine proteinase activities support a conservation of function with respect to digestion of host proteins in common carp. Developmental and Comparative Immunology, 32(11), 1348-61. https://doi.org/10.1016/j.dci.2008.05.002
Ruszczyk A, et al. Trypanoplasma Borreli Cysteine Proteinase Activities Support a Conservation of Function With Respect to Digestion of Host Proteins in Common Carp. Dev Comp Immunol. 2008;32(11):1348-61. PubMed PMID: 18571233.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Trypanoplasma borreli cysteine proteinase activities support a conservation of function with respect to digestion of host proteins in common carp. AU - Ruszczyk,Aleksandra, AU - Forlenza,Maria, AU - Joerink,Maaike, AU - Ribeiro,Carla M S, AU - Jurecka,Patrycja, AU - Wiegertjes,Geert F, Y1 - 2008/06/02/ PY - 2007/07/18/received PY - 2008/04/17/revised PY - 2008/05/05/accepted PY - 2008/6/24/pubmed PY - 2008/10/18/medline PY - 2008/6/24/entrez SP - 1348 EP - 61 JF - Developmental and comparative immunology JO - Dev Comp Immunol VL - 32 IS - 11 N2 - Trypanoplasma borreli is an extracellular parasite that is transmitted by a leech vector and is naturally found in the blood of cyprinid fish. High parasitemia and associated severe anemia together with splenomegaly are typical of infection of common carp, Cyprinus carpio L. Papain-like cysteine proteinases expressed by trypanosome parasites contribute to the pathogenicity of trypanosomes, and are considered an important target for the development of new trypanocidal drugs. T. borreli is a member of the Parabodonida, sharing a common ancestor with the other Kinetoplastida. We demonstrate the presence of a cysteine proteinase expressed by T. borreli. Alignment of the sequence with other kinetoplastid cysteine proteinase sequences supports the phylogenetic hypotheses based on analyses of ribosomal RNA genes. We expressed the T. borreli cysteine proteinase in Escherichia coli, refolded the purified protein into a biologically active proteinase and showed it has cathepsin L-like activity. Addition of the (non)active proteinase to in vitro-derived carp head kidney-derived macrophages did not significantly modulate macrophage activity. Immunization of carp with the recombinant proteinase did induce a very high increase in proteinase-specific antibodies but only slightly lowered parasitemia. Digestion of host hemoglobin and immunoglobulin by the cysteine proteinase likely contribute to the pathogenicity of T. borreli. The possibility that digestion by the cysteine proteinase of host transferrin could contribute to an innate activation profile of macrophages in vivo is discussed. Our findings suggest a conservation of function with respect to cysteine proteinase activity in the Parabodonida in support of the hypotheses on the phylogeny of the Kinetoplastida. SN - 0145-305X UR - https://www.unboundmedicine.com/medline/citation/18571233/Trypanoplasma_borreli_cysteine_proteinase_activities_support_a_conservation_of_function_with_respect_to_digestion_of_host_proteins_in_common_carp_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0145-305X(08)00104-3 DB - PRIME DP - Unbound Medicine ER -