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Relevant bibliographies by topics / Class III β-tubulin

Academic literature on the topic 'Class III β-tubulin'

Author: Grafiati

Published: 11 March 2023

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Journal articles on the topic "Class III β-tubulin"

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Jouhilahti, Eeva-Mari, Sirkku Peltonen, and Juha Peltonen. "Class III β-Tubulin Is a Component of the Mitotic Spindle in Multiple Cell Types." Journal of Histochemistry & Cytochemistry 56, no. 12 (September 2, 2008): 1113–19. http://dx.doi.org/10.1369/jhc.2008.952002.

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The findings of this study show that Class III β-tubulin is a component of the mitotic spindle in multiple cell types. Class III β-tubulin has been widely used as a neuron-specific marker, but it has been detected also in association with breast and pancreatic cancers. In this study, we describe a novel finding of Class III β-tubulin in a subpopulation of cells in malignant peripheral nerve sheath tumor. The findings of this study also show that Class III β-tubulin is expressed by normal mesenchymal and epithelial cells (fibroblasts and keratinocytes), two transitional cell carcinoma cell lines, and neurofibroma Schwann cells, as shown by immunolabeling and Western transfer analysis using two different Tuj-1 antibodies that are specific for Class III β-tubulin. The corresponding mRNA was detected using RT-PCR and whole human genome microarrays. Both antibodies localized Class III β-tubulin to the mitotic spindle and showed a colocalization with α-tubulin. The immuno-reaction became visible in early prophase, and the most intense immunoreaction was detected during metaphase and anaphase when microtubules were connected to the kinetochores on chromosomes. Class III β-tubulin–specific immunoreaction lasted to the point when the midbody of cytokinesis became detectable.

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Reader, Jocelyn, Amy K. Harper, Teklu Legesse, Paul N. Staats, Olga Goloubeva, Gautam G. Rao, Amy Fulton, and Dana M. Roque. "EP4 and Class III β-Tubulin Expression in Uterine Smooth Muscle Tumors: Implications for Prognosis and Treatment." Cancers 11, no. 10 (October 18, 2019): 1590. http://dx.doi.org/10.3390/cancers11101590.

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The microtubule-stabilizing agent docetaxel in combination with gemcitabine represents one of the most effective regimens against the aggressive gynecologic tumor leiomyosarcoma (LMS). Upregulation of class III β-tubulin has previously been shown to confer taxane resistance in a variety of human cancers. Prostaglandin E2 receptor EP4 is linked to progression of a variety of human cancers and may represent a novel target for tumor inhibition in LMS. We evaluated the hypotheses that EP4 and class III β-tubulin have increased expression in LMS in comparison to normal myometrium or benign tumors and that expression of class III β-tubulin correlates with resistance to taxanes and poor clinical outcome. Gene expression was examined using TCGA data and correlated with clinicopathologic outcome which demonstrated that class III β-tubulin is more highly expressed in more aggressive sarcomas with EP4 being widely expressed in all subtypes of sarcoma. Immunohistochemistry for EP4 and class III β-tubulin was performed on patients with LMS, leiomyomatosis/STUMP, leiomyoma, and normal myometrium. Expression of EP4 and class III β-tubulin were characterized for cell lines SK-UT-1, SK-UT-1B, and PHM-41 and these cell lines were treated with docetaxel alone and in combination with EP4 inhibitors. In taxane-resistant cell lines that overexpress class III β-tubulin and EP4, treatment with EP4 inhibitor resulted in at least 2-fold sensitization to docetaxel. Expression of class III β-tubulin and EP4 in LMS may identify patients at risk of resistance to standard chemotherapies and candidates for augmentation of therapy through EP4 inhibition.

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Laferrière, Nicole B., and D. L. Brown. "Effects of taxol on the polymerization and posttranslational modification of class III β-tubulin in P19 embryonal carcinoma cells." Biochemistry and Cell Biology 73, no. 9-10 (September 1, 1995): 687–94. http://dx.doi.org/10.1139/o95-076.

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Undifferentiated P19 embryonal carcinoma cells and P19 cells induced to differentiate along a neuronal pathway by 10−6 M retinoic acid were treated with taxol to examine the effects of this microtubule-stabilizing drug on the subcellular sorting of class III β-tubulin and on neurite outgrowth. P19 cells were grown on cover slips and then treated with taxol at concentrations of 10−6 to 10−9 M for 24 h. The microtubule cytoskeleton was examined after double-immunofluorescence labelling with a monoclonal antibody to α-tubulin (YOL 1/34) and a monoclonal neuron-specific class III β-tubulin antibody (TuJ1). Treatment of undifferentiated P19 cells with concentrations of taxol greater than 4 × 10−8 M caused microtubule bundling and multiple aster formation and promoted polymerization of the low levels of class III β-tubulin found in these cells. In neurons, at 2 × 10−8 M taxol, bundling of microtubules at the base of the neurite was apparent. At taxol concentrations greater than 1 × 10−7 M, enhanced assembly of class III β-tubulin was apparent, although long neurites were not observed. Using isoelectric focusing followed by western blotting, we detected an additional isoform of class III β-tubulin after treatment with 10−6 M taxol. These results indicate taxol treatment alters the normal subcellular sorting of tubulin isotypes, promotes the polymerization and posttranslational modification of class III β-tubulin, and interferes with neurite outgrowth.Key words: tubulin, taxol, microtubule, posttranslational modification, neurite outgrowth.

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Linhartová, I., P. Dráber, E. Dráberová, and V. Viklický. "Immunological discrimination of β-tubulin isoforms in developing mouse brain. Post-translational modification of non-class-III β-tubulins." Biochemical Journal 288, no. 3 (December 15, 1992): 919–24. http://dx.doi.org/10.1042/bj2880919.

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Individual beta-tubulin isoforms in developing mouse brain were characterized using immunoblotting, after preceding high-resolution isoelectric focusing, with monoclonal antibodies against different structural regions of beta-tubulin. Some of the antibodies reacted with a limited number of tubulin isoforms in all stages of brain development and in HeLa cells. The epitope for the TU-14 antibody was located in the isotype-defining domain and was present on the beta-tubulin isotypes of classes I, II and IV, but absent on the neuron-specific class-III isotype. The data suggest that non-class-III beta-tubulins in mouse brain are substrates for developmentally regulated post-translational modifications and that beta-tubulins of non-neuronal cells are also post-translationally modified.

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Guo, Huiqin, Yu Zhao, Jiangyang Lu, and Zejian Li. "ERCC1, class III β-tubulin, p53, and RRM1-tailored selection of personalized chemotherapy for stage IV NSCLC patients: A prospective study." Journal of Clinical Oncology 30, no. 15_suppl (May 20, 2012): e18087-e18087. http://dx.doi.org/10.1200/jco.2012.30.15_suppl.e18087.

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e18087 Background: ERCC1, class III β-tubulin, p53, and RRM1 are predictive molecular biomarkers of platinum agents, taxel, vinorelbine and gemcitabine respectively in personalized therapies of NSCLC. Tailored therapy with several of these markers suggested patient benefit was reported previously. But there was no report about prospective study involving all of these biomarkers. Here we report a prospective study that patients were treated with the personalized therapy tailored by these 4 markers to assess this new therapy approach. Methods: From Feb. 2009 to Feb. 2011, in our single group at the thoracic surgical department of PUMC hospital, we identified 48 patients with previously untreated stage IV NSCLC, ECOG PS of 0-2, and at least 2 of the 4 low expression level markers were eligible. The expression level of ERCC1, class III β-tubulin, p53, and RRM1 was assayed by immunohistochemical (IHC) staining with the tissue samples obtained from bronchoscopy biopsy, percutaneous lung biopsy or operation. Patients with low ERCC1/low class III β-tubulin expression received cisplatin/taxel, patients with high ERCC1/low class III β-tubulin expression received gemcitabine(with low RRM1 level) or vinorelbine (with low p53 level)/taxel, patients with low ERCC1/high class III β-tubulin expression received cisplatin/gemcitabine(low RRM1) or vinorelbine (low p53), and patients with high ERCC1/high class IIIβ-tubulin expression received gemcitabine/vinorelbine. A follow-up CT was performed after every 2 cycles chemotherapy and every 3 months after chemotherapy. PFS and OS were estimated by the Kaplan-Meier method. Results: Follow-up period was 35 months till Jan. 2012. 16(33.3%) patients died within follow-up period, 32(66.7%) patients are still alive. The overall response(CR+PR) rate is 85.4% with 10CR, 31 PR, 5 SD and 2 PD. Median PFS is 14 months and median OS was 27 months. And 1-year OS was 88.3% Conclusions: Our study suggest ERCC1, class III β-tubulin, p53, and RRM1-tailored selection of personalized chemotherapy of NSCLC could dramatically raise response rate and improve survival over standard chemotherapy. It might be a promising treatment option in the future..

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Zhang, Shucai, Qi Li, Quan Zhang, Jinghui Wang, Haiqing Zhang, Zongde Zhang, Qunhui Wang, Xinjie Yang, Yanfei Gu, and Hui Zhang. "Expression of ERCC1 and Class III β-Tubulin in Resected Non-Small Cell Lung Cancer and its Correlation with Platinum-Based Adjuvant Chemotherapy." International Journal of Biological Markers 25, no. 3 (July 2010): 141–49. http://dx.doi.org/10.1177/172460081002500304.

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Objective To explore the relationship between the expression of excision repair cross-complementation group 1 (ERCC1) and class III β-tubulin and the clinical characteristics and overall survival of patients with non-small cell lung cancer (NSCLC). Methods Immunohistochemical analysis was used to determine the protein expression of ERCC1 and class III β-tubulin in 160 completely resected NSCLC primary tumor samples, 50 of which were paired with adjacent normal tissue samples and another 40 benign lung lesion tissue samples as controls. Clinical data at baseline, disease-free survival and overall survival were also collected. Univariate and multivariate Cox models were used to analyze the risk factors. Results In 160 tumor samples, the ERCC1 and class III β-tubulin positive rates obtained with immunohistochemistry were 46.9% and 49.4%, respectively. Both biomarkers had a higher positive rate in male patients. For patients who did not receive adjuvant chemotherapy, ERCC1 positivity was associated with longer survival (median survival time 73 vs 53 months, p=0.041), while in patients treated with platinum chemotherapy, ERCC1 positivity tended to be associated with poor survival (median survival time 41 vs 54 months, p=0.014). Class III β-tubulin positivity was also associated with poor survival (median survival time 38 vs 58 months, p<0.001), but had no influence on the survival of patients who did not receive adjuvant chemotherapy. Conclusions ERCC1 and class III β-tubulin could be important survival predictors for completely resected NSCLC patients treated with adjuvant chemotherapy. Further prospective studies need to be performed to test this hypothesis in Chinese patients.

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Mariani, Marisa, Roshan Karki, Manuela Spennato, Deep Pandya, Shiquan He, Mirko Andreoli, Paul Fiedler, and Cristiano Ferlini. "Class III β-tubulin in normal and cancer tissues." Gene 563, no. 2 (June 2015): 109–14. http://dx.doi.org/10.1016/j.gene.2015.03.061.

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Katsetos, Christos D., Mary M. Herman, and Sverre J. Mörk. "Class III β-tubulin in human development and cancer." Cell Motility and the Cytoskeleton 55, no. 2 (April 24, 2003): 77–96. http://dx.doi.org/10.1002/cm.10116.

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Alfano, Alan, Jin Xu, Xi Yang, Dhanraj Deshmukh, and Yun Qiu. "SRC Kinase-Mediated Tyrosine Phosphorylation of TUBB3 Regulates Its Stability and Mitotic Spindle Dynamics in Prostate Cancer Cells." Pharmaceutics 14, no. 5 (April 25, 2022): 932. http://dx.doi.org/10.3390/pharmaceutics14050932.

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Tubulin is an integral part of the cytoskeleton and plays a pivotal role in cellular signaling, maintenance, and division. β-tubulin is also the molecular target for taxane compounds such as docetaxel (DTX) and cabazitaxel (CTX), both first-line treatments for several solid cancers. Increased expression of Class III β-tubulin (TUBB3), a primarily neural isoform of β-tubulin, correlates with taxane resistance and poor prognosis. Although tyrosine kinase c-Src has been implicated to phosphorylate β-tubulins during both hematopoietic and neural differentiation, the mechanisms by which Src modulates tubulins functions are still poorly understood. Here, we report, for the first time, that TUBB3 is phosphorylated at Tyrosine 340 (Y340) by c-SRC in prostate cancer cells. We also showed that Y340 phosphorylation regulates TUBB3 protein stability and subcellular localization. Furthermore, we demonstrated that inhibition of SRC kinase activity compromises spindle stability in mitotic cells, at least partly due to the lack of TUBB3 Y340 phosphorylation. Given the importance of TUBB3 as a clinical biomarker of poor prognosis and drug resistance, characterization of TUBB3 posttranslational regulation could potentially serve as new biomarkers for disease recurrence and/or treatment failure.

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Alfano, Alan, Jin Xu, Xi Yang, Dhanraj Deshmukh, and Yun Qiu. "SRC Kinase-Mediated Tyrosine Phosphorylation of TUBB3 Regulates Its Stability and Mitotic Spindle Dynamics in Prostate Cancer Cells." Pharmaceutics 14, no. 5 (April 25, 2022): 932. http://dx.doi.org/10.3390/pharmaceutics14050932.

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Tubulin is an integral part of the cytoskeleton and plays a pivotal role in cellular signaling, maintenance, and division. β-tubulin is also the molecular target for taxane compounds such as docetaxel (DTX) and cabazitaxel (CTX), both first-line treatments for several solid cancers. Increased expression of Class III β-tubulin (TUBB3), a primarily neural isoform of β-tubulin, correlates with taxane resistance and poor prognosis. Although tyrosine kinase c-Src has been implicated to phosphorylate β-tubulins during both hematopoietic and neural differentiation, the mechanisms by which Src modulates tubulins functions are still poorly understood. Here, we report, for the first time, that TUBB3 is phosphorylated at Tyrosine 340 (Y340) by c-SRC in prostate cancer cells. We also showed that Y340 phosphorylation regulates TUBB3 protein stability and subcellular localization. Furthermore, we demonstrated that inhibition of SRC kinase activity compromises spindle stability in mitotic cells, at least partly due to the lack of TUBB3 Y340 phosphorylation. Given the importance of TUBB3 as a clinical biomarker of poor prognosis and drug resistance, characterization of TUBB3 posttranslational regulation could potentially serve as new biomarkers for disease recurrence and/or treatment failure.

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Dissertations / Theses on the topic "Class III β-tubulin"

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Ploussard, Guillaume. "Biomarqueurs émergents dans le cancer de prostate : à propos de la β-tubuline de classe III et du score urinaire PCA3." Phd thesis, Université Paris-Est, 2011. http://tel.archives-ouvertes.fr/tel-00920469.

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PEDICA, Federica. "Characterization of neoplastic and non-neoplastic microenvironment in liver, lung and bone marrow through the study of class III β-tubulin." Doctoral thesis, 2016. http://hdl.handle.net/11562/938311.

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La seguente tesi di Dottorato in Patologia Oncologica e Cellule Staminali è incentrata sullo studio di beta-tubulina classe III (tubb3), che è stata prevalentemente studiata in ambito oncologico nei tumori epiteliali come marcatore di resistenza alla terapia con taxani e di aggressività. Recentemente è stata poi descritta come marker dei periciti, cellule che indicano maturità della struttura vascolare in cui sono presenti, ma anche cellule particolari dotate di contrattilità e con una morfologia che richiama il miofibroblasto. L’osservazione di positività per tubb3 solo in rari casi di carcinoma epatocellulare, a differenza di molti altri carcinomi e la peculiare positività nel contesto dei vasi neoformati di questo tumore, ha suggerito di considerare tubb3 come un marker con superiori potenzialità rispetto a quanto descritto in letteratura. Per tale motivo abbiamo pensato di sviluppare 3 progetti paralleli su patologie diverse tra loro, sia in ambito non neoplastico (fibrosi polmonare idiopatica) che neoplastico (carcinoma epatocellulare e mielofibrosi primitiva idiopatica), accumunate dalla presenza di una popolazione cellulare fusata con aspetto simil-miofibroblastico. In particolare nella fibrosi polmonare idiopatica, tubb3 marca i miofibroblasti che fanno parte del focus fibroblastico, lesione patognomonica della malattia. Lo studio ha portato alla stesura di un articolo scientifico che è tutt’ora submitted. Nel carcinoma epatocellulare tubb3 si trova solo raramente nelle cellule neoplastiche, spesso al fronte di avanzamento del tumore e in circa 1/3 dei casi nei vasi peritumorali e peritumorali. La peculiarità di questi risultati ha portato allo sviluppo di un secondo studio su colture cellulari dinamiche in 3D con Bioreattore con lo scopo di capire come si comportassero i vasi tumorali in coltura una volta sottoposti al farmaco attualmente riconosciuto come unica terapia dall’FDA per il carcinoma epatocellulare avanzato, ovvero Sorafenib. Questo progetto è tutt’ora in fase di sviluppo con il gruppo di studio del Tumor Microenvironment dell’Ospedale San Raffaele di Milano, dove è presente il Bioreattore. Per quanto riguarda la mielofibrosi primitiva idiopatica, è lo stesso nome della malattia che ha suggerito di testare l’anticorpo e, visti i primi risultati incoraggianti, ci ha portato ad avviare una collaborazione con l’Ematologia del Policlinico GB Rossi allo scopo di capire se i pazienti che presentano una popolazione tubb3 nel contesto della biopsia midollare abbiano una biologia di malattia diversa e se questa eterogeneità abbia qualche correlazione con l’assetto mutazionale.
The following PhD thesis on Human Oncological Pathology and Stem Cell is focused on class III beta-tubulin (tubb3) that has been mainly investigated in oncological context for epithelial tumors as a marker of resistance to taxane and aggressiveness. Recently it has also been described as marker for pericytes, Recentemente è stata poi descritta come marker dei pericytes, which are cells indicating the maturity of vessels but have also contractility properties and morphologically recalls myofibroblasts. The presence of tubb3 in rare cases of hepatocellular carcinoma, differently compared to other carcinomas e the peculiar positivity in newly formed tumoral vessels, has suggested the possible wide potentiality of this marker compared to what has already been described in literature. For this reason we have decided to develop 3 projects in parallel on different diseases, both non-neoplastic (idiopathic pulmonary fibrosis) and neoplastic (hepatocellular carcinoma and primary myelofibrosis) conditions, that are in a way accumunated by the presence of a spindle population of cells resembling myofibroblasts. In pulmonary fibrosis, tubb3 identify the myofibroblasts forming fibroblastic foci, that are a pathognomonic lesion of the disease. This study has produced an original article that has been submitted. In Hepatocellular carcinoma, tubb3 is found only rarely in neoplastic cells, often at the front of edge of the tumor and in 1/3 of cases in peritumoral and intratumoral vessels. The peculiarity of these results has driven the idea of another study on dynamic 3D-cultures with Bioreactor, to investigate how tumoral vessels behave in dynamic cultures also when they are subjected to drug, such as Sorafenib. This study is on-going with the group of Tumor Microenvironment of ’Ospedale San Raffaele in Milano, where the Bioreactor is available. Concerning primary myelofibrosis, it was the name of the disease that suggested us to investigate this process with tubb3. Thank to the intial encouraging results, we have initiated a collaboration with the the Department of Haematology of Policlinico GB Rossi in Verona to understand id the patients that present a tubb3 positive population in the context of bone marrow biopsy have a different type of disease compared to other myelofibrosis and if this heterogeneity has some relation to mutational status.

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Conference papers on the topic "Class III β-tubulin"

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Mariani, Marisa, Marta De Donato, Lella Petrella, Enrica Martinelli, Gabriella Ferrandina, Gian Franco Zannoni, Giovanni Scambia, Shohreh Shahabi, and Cristiano Ferlini. "Abstract 4055: Class III β-tubulin and the cytoskeletal gateway of drug resistance in ovarian cancer." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-4055.

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Roque, Dana M., Danielle Meir-Levi, Gautam G. Rao, Paul Staats, Amy Fulton, and Jocelyn Reader. "Abstract 1179: EP4 receptor antagonism in paclitaxel-resistant ovarian clear cell carcinomas that overexpress class III β-tubulin." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-1179.

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Moon, Yongwha, Ja Seung Koo, Hyunju Han, Byeong-Woo Park, Seung Il Kim, Seho Park, Hyun Cheol Chung, Joo-Hang Kim, and Joo Hyuk Sohn. "Abstract C10: Class III β -tubulin predicts pathological response to neoadjuvant docetaxel-based chemotherapy in breast cancer patients." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics--Nov 12-16, 2011; San Francisco, CA. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1535-7163.targ-11-c10.

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Mariani, Marisa, Gian Franco Zannoni, Stefano Sioletic, Steven Sieber, Candice Martino, Enrica Martinelli, Claudio Coco, Giovanni Scambia, Shohreh Shahabi, and Cristiano Ferlini. "Abstract 4522: Androgen receptor is a main driver of aggressiveness in colorectal cancer through the class III β-tubulin pathway." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-4522.

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Sumitomo, Ryota, Tatsuya Hirai, Hiyoaki Murakami, Yosuke Otake, and Cheng-long Huang. "Abstract 4010: Adjuvant chemotherapy based on the intratumoral expressions of class III β tubulin and thymidylate synthase improved disease-free survival in patients with resected locally advanced non-small cell lung cancer." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-4010.

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Filho, Everton Chaves Correia, and Lia Camurça Costa. "RESISTÊNCIA DE HELMINTOS AOS BENZIMIDAZÓLICOS: UMAREVISÃO DE LITERATURA." In II Congresso Brasileiro de Parasitologia Humana On-line. Revista Multidisciplinar em Saúde, 2022. http://dx.doi.org/10.51161/conbrapah/32.

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Introdução: Em 2010, registrou-se cerca de 1 bilhão de casos de doenças causadas por helmintos no mundo. Diante disso, a Organização Mundial da Saúde (OMS) sugeriu a quimioprofilaxia periódica como tratamento preventivo de verminoses. A principal classe medicamentosa utilizada são os anti-helmínticos benzimidazólicos, que se mostraram eficazes no tratamento de verminoses, mas com potencial limitado em algunscasos. Logo, surgiu a hipótese de que uma exposição prolongada a tais drogas seria capaz de selecionar helmintos mais resistentes. Objetivos: 1) Compreender o mecanismo de ação dos benzimidazólicos; 2) Investigar a presença de resistência à medicação. Material e métodos: O presente estudo é uma revisão de literatura realizadamediante a busca pelos descritores “drugs resistance”, “helminths” e “benzimidazole”, na base de dados PubMed. Foram encontrados 439 artigos, dos quais 9, realizados entre os anos de 2010 a 2022, foram selecionados. Resultados: Estudos demonstram que benzimidazólicos agem na ligação à proteína β-tubulina, subunidade de microtúbulos, estruturas responsáveis pela homeostase celular. Dessa forma, estes sofrem encurtamento, resultando na morte celular do parasita. Todavia, após a descoberta de resistência à medicação em animais, questionou-se a presença de helmintos resistentes adrogas em humanos. Pesquisas feitas através de qPCR comprovaram a influência de fatores genéticos e ambientais na resistência parasitária. Com isso, foi identificado um polimorfismo de nucleotídeo único, nos códons 167, 198 e 200 do gene da β-tubulina, responsáveis por alterações celulares, impedindo a associação de benzimidazólicos ao sítio de ligação desta proteína. Ademais, o número de helmintos de vida livre, sensíveis à medicação, diminui a cada administração errônea de drogas, dosagens em curto período de tempo, e ao clima quente e seco, selecionando parasitas resistentes. Estudos brasileiros e australianos mostraram que A. lumbricoides, N. americanus e T. trichiura são os helmintos com maior prevalência de cepas resistentes. Entretanto, os benzimidazólicos conseguiram eliminar a maioria desses vermes. Conclusão: Comprovou se a existência de helmintos resistentes aos benzimidazólicos. Contudo, a prevalência dos mesmos ainda é baixa, sendo uma preocupação de saúde pública para os próximos anos, visto que o número de cepas resistentes aumenta com a administração errada de drogas e com mutações genéticas dos próprios parasitas.

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