{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,10]],"date-time":"2026-10-10T14:58:05Z","timestamp":1791644285431,"version":"4.3.4"},"reference-count":94,"publisher":"MDPI AG","issue":"4","license":[{"start":{"date-parts":[[2025,3,31]],"date-time":"2025-03-31T00:00:00Z","timestamp":1743379200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Pontificia Universidad Cat\u00f3lica del Ecuador"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Pathogens"],"abstract":"<jats:p>The protozoan parasite Trypanosoma cruzi, causative agent of Chagas disease, affects millions of people in endemic Latin American countries and beyond. In Latin America, Chagas disease is an important cause of death and disability, for which vaccines are lacking and improved treatment options are required. Additionally, the factors governing the development of a variety of clinical manifestations during Chagas disease, ranging from complete lack of symptoms to severe irreversible chronic organ damage (mainly cardiac or digestive), remain largely unknown. Much remains to be learned regarding the biology of T. cruzi in order to enhance our understanding of these lines of inquiry. In this context, proteomic methods have been leveraged to investigate different parasite strains, life-cycle forms, subcellular compartments, macromolecular complexes, signaling events and secreted molecules. The factors driving morphological transformation during the life cycle, the composition and functions of the parasite\u2019s organelles and secreted molecules as well as the determinants of pathogenicity have been explored via proteomic methods, yielding insights into the fundamental processes behind the parasite biology and informing drug design and vaccine development. Importantly, the correlation between the wide genetic and phenotypic variability displayed by T. cruzi has been examined through proteomic methods as well. Here, we review the literature on T. cruzi proteomics and discuss it in the light of its limitations and in the context of the parasite\u2019s genetic diversity.<\/jats:p>","DOI":"10.3390\/pathogens14040337","type":"journal-article","created":{"date-parts":[[2025,4,1]],"date-time":"2025-04-01T11:17:57Z","timestamp":1743506277000},"page":"337","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":9,"title":["An Overview of Trypanosoma cruzi Biology Through the Lens of Proteomics: A Review"],"prefix":"10.3390","volume":"14","author":[{"given":"Jenny","family":"Telleria","sequence":"first","affiliation":[{"name":"Institut de Recherche Pour le D\u00e9veloppement (IRD), UMR Intertryp IRD-CIRAD, 34398 Montpellier, Cedex 5, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jaime A.","family":"Costales","sequence":"additional","affiliation":[{"name":"Centro de Investigaci\u00f3n Para la Salud en Am\u00e9rica Latina, Pontificia Universidad Cat\u00f3lica del Ecuador, Quito 170525, Ecuador"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2025,3,31]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Lidani, K.C.F., Andrade, F.A., Bavia, L., Damasceno, F.S., Beltrame, M.H., Messias-Reason, I.J., and Sandri, T.L. (2019). Chagas Disease: From Discovery to a Worldwide Health Problem. Front. Public Health, 7.","DOI":"10.3389\/fpubh.2019.00166"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1590\/0074-0276140362","article-title":"The main sceneries of Chagas disease transmission. The vectors, blood and oral transmissions\u2014A comprehensive review","volume":"110","author":"Coura","year":"2014","journal-title":"Mem. Inst. Oswaldo Cruz"},{"key":"ref_3","first-page":"384","article-title":"Gu\u00edas cl\u00ednicas de la enfermedad de Chagas 2006: Parte VI. Tratamiento antiparasitario de la enfermedad de Chagas","volume":"25","author":"Apt","year":"2008","journal-title":"Rev. Chil. Infectol."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1016\/j.actatropica.2014.01.002","article-title":"Toxic and therapeutic effects of Nifurtimox and Benznidazol on Trypanosoma cruzi ex vivo infection of human placental chorionic villi explants","volume":"132","author":"Rojo","year":"2014","journal-title":"Acta Trop."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"601","DOI":"10.1016\/j.cbpa.2006.03.004","article-title":"Mode of action of natural and synthetic drugs against Trypanosoma cruzi and their interaction with the mammalian host","volume":"146","author":"Maya","year":"2007","journal-title":"Comp. Biochem. Physiol. A Mol. Integr. Physiol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"4896","DOI":"10.1128\/AAC.00537-10","article-title":"Tolerance of Benznidazole in Treatment of Chagas\u2019 Disease in Adults","volume":"54","author":"Pinazo","year":"2010","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"1224","DOI":"10.1016\/S0300-8932(09)73074-X","article-title":"The Impact of Socioeconomic Conditions on Chronic Chagas Disease Progression","volume":"62","author":"Viotti","year":"2009","journal-title":"Rev. Esp. Cardiol. Engl. Ed."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"2357","DOI":"10.1021\/pr700659m","article-title":"Proteomic Analysis of Trypanosoma cruzi Resistance to Benznidazole","volume":"7","author":"Andrade","year":"2008","journal-title":"J. Proteome Res."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"404","DOI":"10.1126\/science.1112181","article-title":"Comparative Genomics of Trypanosomatid Parasitic Protozoa","volume":"309","year":"2005","journal-title":"Science"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"D344","DOI":"10.1093\/nar\/gkh049","article-title":"TcruziDB: An integrated Trypanosoma cruzi genome resource","volume":"32","author":"Luchtan","year":"2004","journal-title":"Nucleic Acids Res."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1016\/0169-4758(95)80081-6","article-title":"Mechanisms of stage-regulated gene expression in kinetoplastida","volume":"11","author":"Graham","year":"1995","journal-title":"Parasitol. Today"},{"key":"ref_12","doi-asserted-by":"crossref","unstructured":"Callejas-Hern\u00e1ndez, F., Gutierrez-Nogues, \u00c1., Rastrojo, A., Giron\u00e8s, N., and Fresno, M. (2019). Analysis of mRNA processing at whole transcriptome level, transcriptomic profile and genome sequence refinement of Trypanosoma cruzi. Sci. Rep., 9.","DOI":"10.1038\/s41598-019-53924-6"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"813","DOI":"10.1039\/d0mt00030b","article-title":"Comparative high-throughput analysis of the Trypanosoma cruzi response to organometallic compounds","volume":"12","author":"Mosquillo","year":"2020","journal-title":"Metallomics"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"881","DOI":"10.1016\/j.ijpara.2004.05.002","article-title":"Proteome analysis of the causative agent of Chagas disease: Trypanosoma cruzi","volume":"34","author":"Arrambide","year":"2004","journal-title":"Int. J. Parasitol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1016\/0166-6851(86)90085-X","article-title":"Stage-specific surface antigens of metacyclic trypomastigotes of Trypanosoma cruzi identified by monoclonal antibodies","volume":"18","author":"Teixeira","year":"1986","journal-title":"Mol. Biochem. Parasitol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"3530","DOI":"10.1021\/pr401120y","article-title":"Cell Surface Proteome Analysis of Human-Hosted Trypanosoma cruzi Life Stages","volume":"13","author":"Queiroz","year":"2014","journal-title":"J. Proteome Res."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1017\/S0031182000065264","article-title":"The induction of Trypanosoma cruzi trypomastigote to amastigote transformation by low pH","volume":"110","author":"Tomlinson","year":"1995","journal-title":"Parasitology"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1007\/s00203-008-0439-6","article-title":"Proteomic map of Trypanosoma cruzi CL Brener: The reference strain of the genome project","volume":"191","author":"Chapeaurouge","year":"2009","journal-title":"Arch. Microbiol."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"3642","DOI":"10.1021\/pr800887u","article-title":"Proteomic Analysis of Detergent-Solubilized Membrane Proteins from Insect-Developmental Forms of Trypanosoma cruzi","volume":"8","author":"Cordero","year":"2009","journal-title":"J. Proteome Res."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1126\/science.1110289","article-title":"The Trypanosoma cruzi Proteome","volume":"309","author":"Atwood","year":"2005","journal-title":"Science"},{"key":"ref_21","doi-asserted-by":"crossref","unstructured":"Avila, C.C., Mule, S.N., Rosa-Fernandes, L., Viner, R., Baris\u00f3n, M.J., Costa-Martins, A.G., De Oliveira, G.S., Teixeira, M.M.G., Marinho, C.R.F., and Silber, A.M. (2018). Proteome-Wide Analysis of Trypanosoma cruzi Exponential and Stationary Growth Phases Reveals a Subcellular Compartment-Specific Regulation. Genes, 9.","DOI":"10.3390\/genes9080413"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"e00302-17","DOI":"10.1128\/IAI.00302-17","article-title":"Inhibition of Host Cell Lysosome Spreading by Trypanosoma cruzi Metacyclic Stage-Specific Surface Molecule gp90 Downregulates Parasite Invasion","volume":"85","author":"Rodrigues","year":"2017","journal-title":"Infect. Immun."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"2694","DOI":"10.1002\/pmic.201200078","article-title":"Quantitative proteomics of Trypanosoma cruzi during metacyclogenesis","volume":"12","author":"Marchini","year":"2012","journal-title":"Proteomics"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"1422","DOI":"10.1002\/jms.1267","article-title":"Proteomic analysis of metacyclic trypomastigotes undergoing Trypanosoma cruzi metacyclogenesis","volume":"42","author":"Arrambide","year":"2007","journal-title":"J. Mass Spectrom. JMS"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"712","DOI":"10.1111\/mmi.13653","article-title":"Recently differentiated epimastigotes from Trypanosoma cruzi are infective to the mammalian host","volume":"104","author":"Kessler","year":"2017","journal-title":"Mol. Microbiol."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"1066","DOI":"10.2174\/0929866522666150915122120","article-title":"Comparative Two-Dimensional Gel Electrophoresis of Trypanosoma cruzi Mammalian-Stage Forms in an Alkaline pH Range","volume":"22","author":"Queiroz","year":"2015","journal-title":"Protein Pept. Lett."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1186\/1477-5956-6-24","article-title":"Trypanosoma cruzi alkaline 2-DE: Optimization and application to comparative proteome analysis of flagellate life stages","volume":"6","author":"Charneau","year":"2008","journal-title":"Proteome Sci."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1052","DOI":"10.1002\/pmic.200300637","article-title":"Proteomic analysis of the human pathogen Trypanosoma cruzi","volume":"4","author":"Paba","year":"2004","journal-title":"Proteomics"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"2735","DOI":"10.1002\/pmic.200700940","article-title":"Proteomics in Trypanosoma cruzi\u2014Localization of novel proteins to various organelles","volume":"8","author":"Ferella","year":"2008","journal-title":"Proteomics"},{"key":"ref_30","doi-asserted-by":"crossref","unstructured":"Ulrich, P.N., Jimenez, V., Park, M., Martins, V.P., Atwood, J., Moles, K., Collins, D., Rohloff, P., Tarleton, R., and Moreno, S.N.J. (2011). Identification of Contractile Vacuole Proteins in Trypanosoma cruzi. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0018013"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"e00088-23","DOI":"10.1128\/msphere.00088-23","article-title":"Proximity-Dependent Biotinylation and Identification of Flagellar Proteins in Trypanosoma cruzi","volume":"8","author":"Won","year":"2023","journal-title":"mSphere"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1016\/j.bbrc.2009.02.095","article-title":"Proteomic analysis of the Trypanosoma cruzi ribosomal proteins","volume":"382","author":"Ayub","year":"2009","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"1782","DOI":"10.1002\/pmic.200800730","article-title":"Subcellular proteomics of Trypanosoma cruzi reservosomes","volume":"9","author":"Nakayasu","year":"2009","journal-title":"Proteomics"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1016\/j.exppara.2007.04.013","article-title":"A contractile vacuole complex is involved in osmoregulation in Trypanosoma cruzi","volume":"118","author":"Rohloff","year":"2008","journal-title":"Exp. Parasitol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1016\/S0022-1910(00)00170-0","article-title":"Ionic composition of the rectal contents and excreta of the reduviid bug Triatoma infestans","volume":"47","author":"Kollien","year":"2001","journal-title":"J. Insect Physiol."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"3255","DOI":"10.1021\/pr400110h","article-title":"Comprehensive Proteomic Analysis of Trypanosoma cruzi Epimastigote Cell Surface Proteins by Two Complementary Methods","volume":"12","author":"Queiroz","year":"2013","journal-title":"J. Proteome Res."},{"key":"ref_37","doi-asserted-by":"crossref","unstructured":"Santos J\u00fanior, A.d.C.M.d., Kalume, D.E., Camargo, R., G\u00f3mez-Mendoza, D.P., Correa, J.R., Charneau, S., Sousa, M.V.d., Lima, B.D.d., and Ricart, C.A.O. (2015). Unveiling the Trypanosoma cruzi Nuclear Proteome. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0138667"},{"key":"ref_38","doi-asserted-by":"crossref","unstructured":"Qui\u00f1ones, W., Acosta, H., Gon\u00e7alves, C.S., Motta, M.C.M., Gualdr\u00f3n-L\u00f3pez, M., and Michels, P.A.M. (2020). Structure, Properties, and Function of Glycosomes in Trypanosoma cruzi. Front. Cell. Infect. Microbiol., 10.","DOI":"10.3389\/fcimb.2020.00025"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1016\/j.molbiopara.2019.02.008","article-title":"Proteomic analysis of glycosomes from Trypanosoma cruzi epimastigotes","volume":"229","author":"Acosta","year":"2019","journal-title":"Mol. Biochem. Parasitol."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"103822","DOI":"10.1016\/j.jprot.2020.103822","article-title":"Proteomic analysis of Trypanosoma cruzi spliceosome complex","volume":"223","author":"Barbosa","year":"2020","journal-title":"J. Proteom."},{"key":"ref_41","doi-asserted-by":"crossref","unstructured":"Ballesteros-Rodea, G., Santill\u00e1n, M., Mart\u00ednez-Calvillo, S., and Manning-Cela, R. (2012). Flagellar Motility of Trypanosoma cruzi Epimastigotes. J. Biomed. Biotechnol., 2012.","DOI":"10.1155\/2012\/520380"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"e03556-22","DOI":"10.1128\/mbio.03556-22","article-title":"The Intracellular Amastigote of Trypanosoma cruzi Maintains an Actively Beating Flagellum","volume":"14","author":"Won","year":"2023","journal-title":"mBio"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1073\/pnas.83.1.115","article-title":"Natural populations of Trypanosoma cruzi, the agent of Chagas disease, have a complex multiclonal structure","volume":"83","author":"Tibayrenc","year":"1986","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_44","doi-asserted-by":"crossref","unstructured":"Tibayrenc, M., and Ayala, F.J. (2020). Genomics and High-Resolution Typing Confirm Predominant Clonal Evolution Down to a Microevolutionary Scale in Trypanosoma cruzi. Pathogens, 9.","DOI":"10.3390\/pathogens9050356"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1016\/j.actatropica.2015.05.006","article-title":"The population genetics of Trypanosoma cruzi revisited in the light of the predominant clonal evolution model","volume":"151","author":"Tibayrenc","year":"2015","journal-title":"Acta Trop."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"E3305","DOI":"10.1073\/pnas.1212452109","article-title":"Reproductive clonality of pathogens: A perspective on pathogenic viruses, bacteria, fungi, and parasitic protozoa","volume":"109","author":"Tibayrenc","year":"2012","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1016\/j.meegid.2011.12.009","article-title":"The revised Trypanosoma cruzi subspecific nomenclature: Rationale, epidemiological relevance and research applications","volume":"12","author":"Zingales","year":"2012","journal-title":"Infect. Genet. Evol."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"1051","DOI":"10.1590\/S0074-02762009000700021","article-title":"A new consensus for Trypanosoma cruzi intraspecific nomenclature: Second revision meeting recommends TcI to TcVI","volume":"104","author":"Zingales","year":"2009","journal-title":"Mem. Inst. Oswaldo Cruz"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1016\/j.pt.2012.01.006","article-title":"The evolution of Trypanosoma cruzi: The \u2018bat seeding\u2019 hypothesis","volume":"28","author":"Hamilton","year":"2012","journal-title":"Trends Parasitol."},{"key":"ref_50","doi-asserted-by":"crossref","unstructured":"Brossas, J.-Y., Gulin, J.E.N., Bisio, M.M.C., Chapelle, M., Marinach-Patrice, C., Bordessoules, M., Palazon Ruiz, G., Vion, J., Paris, L., and Altcheh, J. (2017). Secretome analysis of Trypanosoma cruzi by proteomics studies. PLoS ONE, 12.","DOI":"10.1371\/journal.pone.0185504"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"1842","DOI":"10.1128\/IAI.00193-16","article-title":"TcI Isolates of Trypanosoma cruzi Exploit the Antioxidant Network for Enhanced Intracellular Survival in Macrophages and Virulence in Mice","volume":"84","author":"Zago","year":"2016","journal-title":"Infect. Immun."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1186\/s13071-018-3181-1","article-title":"Differential expression of proteins in genetically distinct Trypanosoma cruzi samples (TcI and TcII DTUs) isolated from chronic Chagas disease cardiac patients","volume":"11","year":"2018","journal-title":"Parasit. Vectors"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"540","DOI":"10.1016\/j.exppara.2010.06.005","article-title":"Proteomic analysis of two Trypanosoma cruzi zymodeme 3 strains","volume":"126","author":"Kikuchi","year":"2010","journal-title":"Exp. Parasitol."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"20411","DOI":"10.1073\/pnas.1015496107","article-title":"Phylogenetic character mapping of proteomic diversity shows high correlation with subspecific phylogenetic diversity in Trypanosoma cruzi","volume":"107","author":"Telleria","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_55","doi-asserted-by":"crossref","unstructured":"Machin, A., Telleria, J., Brizard, J.-P., Demettre, E., S\u00e9veno, M., Ayala, F.J., and Tibayrenc, M. (2014). Trypanosoma cruzi: Gene Expression Surveyed by Proteomic Analysis Reveals Interaction between Different Genotypes in Mixed In Vitro Cultures. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0095442"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"1673","DOI":"10.1016\/j.jprot.2011.05.001","article-title":"Differential expression of Trypanosoma cruzi I associated with clinical forms of Chagas disease: Overexpression of oxidative stress proteins in acute patient isolate","volume":"74","author":"Solari","year":"2011","journal-title":"J. Proteom."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"104041","DOI":"10.1016\/j.meegid.2019.104041","article-title":"Comparative proteomic analysis of trypomastigotes from Trypanosoma cruzi strains with different pathogenicity","volume":"76","author":"Fresno","year":"2019","journal-title":"Infect. Genet. Evol."},{"key":"ref_58","doi-asserted-by":"crossref","unstructured":"De Souza, W. (2019). Role of Proteomics in the Study of Trypanosoma cruzi Biology. Biology of Trypanosoma cruzi, IntechOpen.","DOI":"10.5772\/intechopen.80373"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"883","DOI":"10.1021\/pr300947g","article-title":"Proteomic Analysis of Trypanosoma cruzi Secretome: Characterization of Two Populations of Extracellular Vesicles and Soluble Proteins","volume":"12","author":"Rodrigues","year":"2013","journal-title":"J. Proteome Res."},{"key":"ref_60","doi-asserted-by":"crossref","unstructured":"Mandacaru, S.C., Queiroz, R.M.L., Alborghetti, M.R., De Oliveira, L.S., De Lima, C.M.R., Bastos, I.M.D., Santana, J.M., Roepstorff, P., Ricart, C.A.O., and Charneau, S. (2019). Exoproteome profiling of Trypanosoma cruzi during amastigogenesis early stages. PLoS ONE, 14.","DOI":"10.1371\/journal.pone.0225386"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"744","DOI":"10.1128\/JCM.01649-16","article-title":"Characterization and Diagnostic Application of Trypanosoma cruzi Trypomastigote Excreted-Secreted Antigens Shed in Extracellular Vesicles Released from Infected Mammalian Cells","volume":"55","author":"Ndao","year":"2017","journal-title":"J. Clin. Microbiol."},{"key":"ref_62","doi-asserted-by":"crossref","unstructured":"Retana Moreira, L., Prescilla-Ledezma, A., Cornet-Gomez, A., Linares, F., J\u00f3dar-Reyes, A.B., Fernandez, J., Ibarrola Vannucci, A.K., De Pablos, L.M., and Osuna, A. (2021). Biophysical and Biochemical Comparison of Extracellular Vesicles Produced by Infective and Non-Infective Stages of Trypanosoma cruzi. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22105183"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"1463779","DOI":"10.1080\/20013078.2018.1463779","article-title":"Proteomic analysis reveals different composition of extracellular vesicles released by two Trypanosoma cruzi strains associated with their distinct interaction with host cells","volume":"7","author":"Ribeiro","year":"2018","journal-title":"J. Extracell. Vesicles"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"1846","DOI":"10.3201\/eid2608.191042","article-title":"Plasma-Derived Extracellular Vesicles as Potential Biomarkers in Heart Transplant Patient with Chronic Chagas Disease","volume":"26","author":"Mendes","year":"2020","journal-title":"Emerg. Infect. Dis."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1038\/cr.2011.22","article-title":"Regulation of chromatin by histone modifications","volume":"21","author":"Bannister","year":"2011","journal-title":"Cell Res."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"2039","DOI":"10.1021\/acs.jproteome.6b00208","article-title":"Chromatin Proteomics Reveals Variable Histone Modifications during the Life Cycle of Trypanosoma cruzi","volume":"15","author":"Nunes","year":"2016","journal-title":"J. Proteome Res."},{"key":"ref_67","doi-asserted-by":"crossref","unstructured":"Magalh\u00e3es, R.D.M., Mattos, E.C., Rozanski, A., Galante, P.A.F., Palmisano, G., Cruz, A.K., Colli, W., Camargo, A.A., and Alves, M.J.M. (2020). Global changes in nitration levels and DNA binding profile of Trypanosoma cruzi histones induced by incubation with host extracellular matrix. PLoS Negl. Trop. Dis., 14.","DOI":"10.1371\/journal.pntd.0008262"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"104020","DOI":"10.1016\/j.jprot.2020.104020","article-title":"Proteome-wide modulation of S-nitrosylation in Trypanosoma cruzi trypomastigotes upon interaction with the host extracellular matrix","volume":"231","author":"Mule","year":"2021","journal-title":"J. Proteom."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"374","DOI":"10.1021\/acs.jproteome.7b00603","article-title":"Comparative Proteomic Analysis of Lysine Acetylation in Trypanosomes","volume":"17","author":"Moretti","year":"2018","journal-title":"J. Proteome Res."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"2200230","DOI":"10.1002\/pmic.202200230","article-title":"Non-histone protein methylation in Trypanosoma cruzi epimastigotes","volume":"23","author":"Lucena","year":"2023","journal-title":"Proteomics"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1017\/S0031182018001828","article-title":"Trichostatin A induces Trypanosoma cruzi histone and tubulin acetylation: Effects on cell division and microtubule cytoskeleton remodelling","volume":"146","author":"Zuma","year":"2019","journal-title":"Parasitology"},{"key":"ref_72","doi-asserted-by":"crossref","unstructured":"Pereira, M., Soares, C., Canuto, G.A.B., Tavares, M.F.M., Colli, W., and Alves, M.J.M. (2015). Down Regulation of NO Signaling in Trypanosoma cruzi upon Parasite-Extracellular Matrix Interaction: Changes in Protein Modification by Nitrosylation and Nitration. PLoS Negl. Trop. Dis., 9.","DOI":"10.1371\/journal.pntd.0003683"},{"key":"ref_73","doi-asserted-by":"crossref","unstructured":"Parsons, M., Worthey, E.A., Ward, P.N., and Mottram, J.C. (2005). Comparative analysis of the kinomes of three pathogenic trypanosomatids: Leishmania major, Trypanosoma brucei and Trypanosoma cruzi. BMC Genom., 6.","DOI":"10.1186\/1471-2164-6-127"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"3489","DOI":"10.1002\/pmic.200800874","article-title":"Phosphoproteomic analysis of the human pathogen Trypanosoma cruzi at the epimastigote stage","volume":"9","author":"Nakayasu","year":"2009","journal-title":"Proteomics"},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"927","DOI":"10.1007\/s12192-019-01018-7","article-title":"Quantitative phosphoproteome and proteome analyses emphasize the influence of phosphorylation events during the nutritional stress of Trypanosoma cruzi: The initial moments of in vitro metacyclogenesis","volume":"24","author":"Lucena","year":"2019","journal-title":"Cell Stress Chaperones"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"182","DOI":"10.1016\/j.jprot.2016.05.034","article-title":"Comprehensive glycoprofiling of the epimastigote and trypomastigote stages of Trypanosoma cruzi","volume":"151","author":"Alves","year":"2017","journal-title":"J. Proteom."},{"key":"ref_77","doi-asserted-by":"crossref","unstructured":"Torres-Guti\u00e9rrez, E., P\u00e9rez-Cervera, Y., Camoin, L., Zenteno, E., Aquino-Gil, M.O., Lefebvre, T., Cabrera-Bravo, M., Reynoso-Ducoing, O., Bucio-Torres, M.I., and Salazar-Schettino, P.M. (2019). Identification of O-Glcnacylated Proteins in Trypanosoma cruzi. Front. Endocrinol., 10.","DOI":"10.3389\/fendo.2019.00199"},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"M110.007369","DOI":"10.1074\/mcp.M110.007369","article-title":"SUMOylation Pathway in Trypanosoma cruzi: Functional Characterization and Proteomic Analysis of Target Proteins","volume":"10","author":"Bayona","year":"2011","journal-title":"Mol. Cell. Proteom."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"649","DOI":"10.1590\/S0001-37652007000400007","article-title":"The pentose phosphate pathway in Trypanosoma cruzi: A potential target for the chemotherapy of Chagas disease","volume":"79","author":"Maugeri","year":"2007","journal-title":"An. Acad. Bras. Ci\u00eanc."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.jsb.2004.12.005","article-title":"Crystal structure of the tryparedoxin peroxidase from the human parasite","volume":"150","author":"Pineyro","year":"2005","journal-title":"J. Struct. Biol."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"61","DOI":"10.4155\/fmc-2016-0180","article-title":"Polyamine-Trypanothione Pathway: An Update","volume":"9","author":"Ilari","year":"2017","journal-title":"Future Med. Chem."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"1683","DOI":"10.1016\/j.jprot.2011.04.006","article-title":"Molecular characterization and interactome analysis of Trypanosoma cruzi Tryparedoxin 1","volume":"74","author":"Portela","year":"2011","journal-title":"J. Proteom."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1016\/j.jprot.2015.03.001","article-title":"Molecular characterization and interactome analysis of Trypanosoma cruzi tryparedoxin II","volume":"120","author":"Arias","year":"2015","journal-title":"J. Proteom."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.bbapap.2015.10.005","article-title":"Trypanosoma cruzi mitochondrial tryparedoxin peroxidase is located throughout the cell and its pull down provides one step towards the understanding of its mechanism of action","volume":"1864","author":"Peloso","year":"2016","journal-title":"Biochim. Biophys. Acta BBA-Proteins Proteom."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1074\/mcp.M116.061200","article-title":"Quantitative Proteomic Analysis of Replicative and Nonreplicative Forms Reveals Important Insights into Chromatin Biology of Trypanosoma cruzi","volume":"16","author":"Calderano","year":"2017","journal-title":"Mol. Cell. Proteom."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"1159","DOI":"10.1128\/EC.00113-10","article-title":"The Pre-mRNA Splicing Machinery of Trypanosomes: Complex or Simplified?","volume":"9","year":"2010","journal-title":"Eukaryot. Cell"},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1016\/j.gene.2009.12.009","article-title":"Proteomic analysis reveals the dynamic association of proteins with translated mRNAs in Trypanosoma cruzi","volume":"452","author":"Alves","year":"2010","journal-title":"Gene"},{"key":"ref_88","first-page":"1106","article-title":"Assessing the partners of the RBP9-mRNP complex in Trypanosoma cruzi using shotgun proteomics and RNA-seq","volume":"15","author":"Wippel","year":"2018","journal-title":"RNA Biol."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"986","DOI":"10.1111\/mmi.14672","article-title":"Affinity-based proteomics reveals novel targets of inositol pyrophosphate (5-IP7)-dependent phosphorylation and binding in Trypanosoma cruzi replicative stages","volume":"115","author":"Mantilla","year":"2021","journal-title":"Mol. Microbiol."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/j.exppara.2014.03.013","article-title":"Trypanosoma cruzi chemical proteomics using immobilized benznidazole","volume":"140","author":"Trochine","year":"2014","journal-title":"Exp. Parasitol."},{"key":"ref_91","doi-asserted-by":"crossref","unstructured":"Azeredo, C.M., Saraiva, M.F., De Oliveira, M.R., Barbosa, G., De Almeida, M.V., De Souza, M.V.N., and Soares, M.J. (2020). The terpenic diamine GIB24 inhibits the growth of Trypanosoma cruzi epimastigotes and intracellular amastigotes, with proteomic analysis of drug-resistant epimastigotes. Chem. Biol. Interact., 330.","DOI":"10.1016\/j.cbi.2020.109165"},{"key":"ref_92","doi-asserted-by":"crossref","unstructured":"Brunoro, G.V.F., Fa\u00e7a, V.M., Caminha, M.A., Ferreira, A.T.d.S., Trugilho, M., de Moura, K.C.G., Perales, J., Valente, R.H., and Menna-Barreto, R.F.S. (2016). Differential Gel Electrophoresis (DIGE) Evaluation of Naphthoimidazoles Mode of Action: A Study in Trypanosoma cruzi Bloodstream Trypomastigotes. PLoS Negl. Trop. Dis., 10.","DOI":"10.1371\/journal.pntd.0004951"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"2306","DOI":"10.1016\/j.jprot.2010.07.002","article-title":"A proteomic analysis of the mechanism of action of naphthoimidazoles in Trypanosoma cruzi epimastigotes in vitro","volume":"73","author":"Beghini","year":"2010","journal-title":"J. Proteom."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"208","DOI":"10.1016\/j.bjid.2018.02.009","article-title":"Trypanosoma cruzi: Analysis of two different strains after piplartine treatment","volume":"22","author":"Vieira","year":"2018","journal-title":"Braz. J. Infect. Dis."}],"container-title":["Pathogens"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2076-0817\/14\/4\/337\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,9]],"date-time":"2025-10-09T17:07:01Z","timestamp":1760029621000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2076-0817\/14\/4\/337"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,3,31]]},"references-count":94,"journal-issue":{"issue":"4","published-online":{"date-parts":[[2025,4]]}},"alternative-id":["pathogens14040337"],"URL":"https:\/\/doi.org\/10.3390\/pathogens14040337","relation":{},"ISSN":["2076-0817"],"issn-type":[{"value":"2076-0817","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,3,31]]}}}