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Kinetics, Subcellular Localization, and Contribution to Parasite Virulence of a Trypanosoma Cruzi Hybrid Type a Heme Peroxidase (Tcapx-Ccp)

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Kinetics, Subcellular Localization, and Contribution to Parasite Virulence of a Trypanosoma Cruzi Hybrid Type a Heme Peroxidase (Tcapx-Ccp) Kinetics, subcellular localization, and contribution to parasite virulence of a Trypanosoma cruzi hybrid type A heme peroxidase (TcAPx-CcP) Martín Hugoa,b,1,2, Alejandra Martíneza,b,1, Madia Trujilloa,b, Damián Estradaa,b, Mauricio Mastrogiovannia,b, Edlaine Linaresc, Ohara Augustoc, Federico Issogliod, Ari Zeidad, Darío A. Estrínd, Harry F. G. Heijnene, Lucía Piacenzaa,b,3, and Rafael Radia,b,3 aDepartamento de Bioquímica, Facultad de Medicina, Universidad de la República, Montevideo 11800, Uruguay; bCenter for Free Radical and Biomedical Research, Universidad de la República, Montevideo 11800, Uruguay; cDepartamento de Bioquímica, Instituto de Química, Universidade de São Paulo, 05508-000, Sao Paulo, Brazil; dDepartamento de Química Inorgánica, Analítica y Química-Física and Instituto de Química Física de Materiales, Medio Ambiente y Energía (INQUIMAE), Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, C1428EHA Buenos Aires, Argentina; and eDepartment of Clinical Chemistry and Hematology, Cell Microscopy Core, University Medical Center, 3584CX Utrecht, The Netherlands Contributed by Rafael Radi, November 10, 2016 (sent for review September 30, 2016; reviewed by Anibal Vercesi and Shane R. Wilkinson) The Trypanosoma cruzi ascorbate peroxidase is, by sequence analy- which the trypanosomatid-specific thiol trypanothione ([T(SH)2], sis, a hybrid type A member of class I heme peroxidases [TcAPx-cyto- N1,N8-bisglutathionylspermidine) plays a central role in the fun- chrome c peroxidase (CcP)], suggesting both ascorbate (Asc) and neling of reducing equivalents to the different peroxidase antioxi- cytochrome c (Cc) peroxidase activity. Here, we show that the enzyme dant systems (10). Two typical 2-Cys peroxiredoxins are located in k = × 7 −1· −1 reacts fast with H2O2 ( 2.9 10 M s ) and catalytically decom- the cytosol (CPX) and in the mitochondrial matrix (MPX), re- poses H2O2 using Cc as the reducing substrate with higher efficiency spectively, and efficiently scavenge H O ,peroxynitrite,andsmall- k K = × 5 × 4 −1· −1 2 2 than Asc ( cat/ m 2.1 10 versus 3.5 10 M s , respectively). chain organic hydroperoxides (11–13). Two glutathione-dependent Visible-absorption spectra of purified recombinant TcAPx-CcP after peroxidases are located at the endoplasmic reticulum (ER) and in H2O2 reaction denote the formation of a compound I-like product, characteristic of the generation of a tryptophanyl radical-cation the cytosol, and seem to be important in the metabolization of lipid- (Trp233•+). Mutation of Trp233 to phenylalanine (W233F) completely derived hydroperoxides (14). Finally, a plant-like related heme abolishes the Cc-dependent peroxidase activity. In addition to peroxidase located at the ER displays ascorbate (Asc)-dependent •+ Trp233 ,aCys222-derived radical was identified by electron paramag- peroxidase activity (APx) (15). T. cruzi netic resonance spin trapping, immunospin trapping, and MS analysis Because the antioxidant defense systems are distinct from its mammalian host, the trypanosomal activities are suitable afterequimolarH2O2 addition, supporting an alternative electron targets for specific rationale pharmacological inhibition. During its transfer (ET) pathway from the heme. Molecular dynamics studies T. cruzi revealed that ET between Trp233 and Cys222 is possible and likely to life cycle, undergoes various morphological and biochemical participate in the catalytic cycle. Recognizing the ability of TcAPx-CcP changes. One of the most complex transformations occurs during to use alternative reducing substrates, we searched for its subcellular localization in the infective parasite stages (intracellular amastigotes Significance and extracellular trypomastigotes). TcAPx-CcP was found closely as- sociated with mitochondrial membranes and, most interestingly, Trypanosoma cruzi, the causative agent of Chagas disease, af- with the outer leaflet of the plasma membrane, suggesting a role fects 8–10 million people in Latin America. Parasite antioxidant at the host–parasite interface. TcAPx-CcP overexpressers were signif- systems are essential for parasite survival and infectivity in the icantly more infective to macrophages and cardiomyocytes, as well vertebrate host. Herein, we characterized the enzymic properties, as in the mouse model of Chagas disease, supporting the involve- subcellular localization, and contribution to parasite virulence of a ment of TcAPx-CcP in pathogen virulence as part of the parasite T. cruzi hybrid type A member of class I heme peroxidases. The antioxidant armamentarium. enzyme reacts fast with hydrogen peroxide and utilizes both ferrocytochrome c and ascorbate as reducing substrates [T. cruzi Trypanosoma cruzi | heme peroxidase | oxidants | virulence | kinetics ascorbate peroxidase (TcAPx)-cytochrome c peroxidase (CcP)]. A unique subcellular distribution of TcAPx-CcP in the infective he protozoan parasite Trypanosoma cruzi is the causative stages suggests a role during parasite–host interactions. Infection agent of Chagas disease (CD; also known as American try- of macrophages and cardiomyocytes, as well as in mice, con- T Tc panosomiasis). Up to 10 million people across Latin America are firmed the involvement of APx-CcP in pathogen virulence as infected with this protozoan parasite, a distribution range that is part of the parasite antioxidant armamentarium. expanding driven by migration of infected insects and hosts, with CD Author contributions: M.H., A.M., M.T., L.P., and R.R. designed research; M.H., A.M., now emerging as a public health problem at nonendemic sites (1, 2). D.E., M.M., E.L., O.A., F.I., A.Z., D.A.E., H.F.G.H., and L.P. performed research; M.H., T. cruzi strains are heterogeneous, exhibiting a high degree of bio- A.M., M.T., D.E., M.M., O.A., F.I., A.Z., D.A.E., H.F.G.H., L.P., and R.R. analyzed data; chemical and genetic variability. Such differences are believed, at and L.P. and R.R. wrote the paper. least in part, to be responsible for disease outcome, which ranges Reviewers: A.V., Universidade de Campinas; and S.R.W., Queen Mary University of London. from being asymptomatic during the course of infection to fatal severe cardiac and digestive complications (3). It has been shown The authors declare no conflict of interest. 1 that the parasite antioxidant systems are essential for parasite M.H. and A.M. contributed equally to this work. 2 survival and establishment of the infection in the vertebrate host Present address: Department of Molecular Toxicology, German Institute of Human Nu- trition Potsdam-Rehbruecke (DIfE), 14558 Nuthetal, Germany. (4–7).Incontrasttomosteukaryotes,T. cruzi lacks catalase and 3To whom correspondence may be addressed. Email: [email protected] or lpiacenza@ selenium-dependent glutathione peroxidases, which are enzymes fmed.edu.uy. capable of rapidly metabolizing high levels of H2O2 (8, 9). Instead, This article contains supporting information online at www.pnas.org/lookup/suppl/doi:10. it expresses an array of complex enzyme-mediated mechanisms in 1073/pnas.1618611114/-/DCSupplemental. E1326–E1335 | PNAS | Published online February 8, 2017 www.pnas.org/cgi/doi/10.1073/pnas.1618611114 Downloaded by guest on September 26, 2021 metacyclogenesis, the process where a noninfective and replicative 1 2 PNAS PLUS insect-derived epimastigote cell transforms to a highly infectious, A TcAPx-CcP nonreplicative, metacyclic trypomastigote. During this process, it has been shown that T. cruzi up-regulates several antioxidant en- B C zymes to preadapt to the hostile environment of the vertebrate host (5, 16, 17). Enzymes known to be up-regulated during this differ- 935 065 065 0.02 entiation process include peroxiredoxins, [T(SH)2]synthase(5),Fe- 0.04 containing superoxide dismutases, and APx (16). 0.01 T. cruzi ascorbate peroxidase (TcAPx)wasfirstreportedtore- 0.02 duce H2O2 catalytically in the presence of Asc as the reducing 0.00 0.00 substrate (APx activity), but with a catalytic efficiency several fold 500 550 600 650 500 550 600 650 lower than plant APx (18, 19). Its overexpression confers parasite resistance toward exogenously added H2O2 toxicity (13, 15, 20). Recent studies have shown that T. cruzi lacking TcAPx is still ca- pable of infecting cultured mammalian cells, albeit at a reduced D E level, and can still establish an infection in the mouse model of CD 0.50 0.48 (20). Although the enzyme does not seem to be essential for par- 0.49 asite infectivity, its enhanced expression may represent an addi- 0.47 0.48 tional skill for the parasite to deal with host-derived oxidant toxicity 0.47 both in the acute and chronic stages of the disease (6, 21). nm) (409 bance 0.46 r TcAPx shares significant homology (62% identity and 86% simi- 0.46 Absorbance 414 nm Absorbance Leishmania major Lm Abso 0.45 larity) with its peroxidase ( P) counterpart (18). 0.45 0.02 0.04 0.06 0.08 0.10 Absorbance (414 nm) Both parasite enzymes are related to the class I heme-peroxidase group Absorbance (409 nm) 0.02 0.04 0.06 0.08 0.10 TimeTime (s) of antioxidant enzymes that includes catalase-peroxidase (katG), Timetime (s) (s) APx, cytochrome c peroxidase (CcP), and the hybrid type (A and B) peroxidases (22). Phylogenetic studies have classified the T. cruzi and Fig. 1. Spectroscopic analysis of TcAPx-CcP compound I and compound Leishmania enzymes as members of the hybrid type A, subfamily A1, I-like intermediates. (A) SDS/PAGE of purified, recombinant TcAPx-CcP (1) heme peroxidases (23), with other sequences in this group displaying and its W233F mutant (2) visualized following Coomassie blue staining. both Asc- and cytochrome c (Cc)-dependent peroxidase activities Absorption spectra of TcAPx-CcP (2 μM) (B) and the W233F mutant (C) be- μ (22, 24). Based on this fact, we have renamed TcAPx as TcAPx-CcP. fore (solid line) and after (dashed line) equimolar H2O2 addition (2 M). These hybrid type A peroxidases represent a real turning point in the (Inset) Spectra from 500 to 650 nm. Arrows indicate the Soret peak of the evolution of ancient bifunctional catalase-peroxidase toward mono- resting enzyme and after H2O2 reaction.
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