Recombinant and native TviCATL from Trypanosoma vivax: Enzymatic characterisation and evaluation as a diagnostic target for animal African trypanosomosis

Lauren E.A. Eyssen, Perina Vather, Laurelle Jackson, Phindile Ximba, Nicolas Biteau, Théo Baltz, Alain Boulangé, Philippe Büscher, Theresa H.T. Coetzer

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)

Abstract

African animal trypanosomosis (nagana) is caused by tsetse-transmitted protozoan parasites. Their cysteine proteases are potential chemotherapeutic and diagnostic targets. The N-glycosylated catalytic domain of Trypanosoma vivax cathepsin L-like cysteine protease, rTviCATL cat , was recombinantly expressed and purified from culture supernatants while native TviCATL was purified from T. vivax Y486 parasite lysates. Typical of Clan CA, family C 1 proteases, TviCATL activity is sensitive to E-64 and cystatin and substrate specificity is defined by the S 2 pocket. Leucine was preferred in P 2 and basic and non-bulky, hydrophobic residues accepted in P 1 and P 3 respectively. Reversible aldehyde inhibitors, antipain, chymostatin and leupeptin, with Arg in P 1 and irreversible peptidyl chloromethylketone inhibitors with hydrophobic residues in P 2 inhibited TviCATL activity. TviCATL digested host proteins: bovine haemoglobin, serum albumin, fibrinogen and denatured collagen (gelatine) over a wide pH range, including neutral to slightly acidic pH. The recombinant catalytic domain of TviCATL showed promise as a diagnostic target for detecting T. vivax infection in cattle in an indirect antibody detection ELISA.

Original languageEnglish
Pages (from-to)50-54
Number of pages5
JournalMolecular and Biochemical Parasitology
Volume223
DOIs
Publication statusPublished - Jul 2018
Externally publishedYes

Keywords

  • Cathepsin L-like peptidase
  • Diagnostic target
  • Nagana
  • Trypanosoma vivax
  • TviCATL

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