Susceptibility of Phytomonas serpens to calpain inhibitors in vitro: interference on the proliferation, ultrastructure, cysteine peptidase expression and interaction with the invertebrate host

dc.creatorOliveira, Simone Santiago Carvalho de
dc.creatorGonçalves, Diego de Souza
dc.creatorGomes, Aline dos Santos Garcia
dc.creatorGonçalves, Inês Correa
dc.creatorSeabra, Sergio Henrique
dc.creatorMenna-Barreto, Rubem Figueiredo
dc.creatorLopes, Angela Hampshire de Carvalho Santos
dc.creatorLevy, Claudia Masini d'Avila
dc.creatorSantos, André Luis Souza dos
dc.creatorBranquinha, Marta Helena
dc.date2017-11-16T12:33:03Z
dc.date2017-11-16T12:33:03Z
dc.date2017
dc.date.accessioned2023-09-26T23:32:50Z
dc.date.available2023-09-26T23:32:50Z
dc.identifierOLIVEIRA, Simone Santiago Carvalho de; et al. Susceptibility of Phytomonas serpens to calpain inhibitors in vitro: interference on the proliferation, ultrastructure, cysteine peptidase expression and interaction with the invertebrate host. Mem Inst Oswaldo Cruz, v. 112, n.1, p. 31-43, Jan. 2017.
dc.identifier0074-0276
dc.identifierhttps://www.arca.fiocruz.br/handle/icict/23203
dc.identifier10.1590/0074-02760160270
dc.identifier1678-8060
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8891742
dc.descriptionA pleiotropic response to the calpain inhibitor MDL28170 was detected in the tomato parasite Phytomonas serpens. Ultrastructural studies revealed that MDL28170 caused mitochondrial swelling, shortening of flagellum and disruption of trans Golgi network. This effect was correlated to the inhibition in processing of cruzipain-like molecules, which presented an increase in expression paralleled by decreased proteolytic activity. Concomitantly, a calcium-dependent cysteine peptidase was detected in the parasite extract, the activity of which was repressed by pre-incubation of parasites with MDL28170. Flow cytometry and Western blotting analyses revealed the differential expression of calpain-like proteins (CALPs) in response to the pre-incubation of parasites with the MDL28170, and confocal fluorescence microscopy confirmed their surface location. The interaction of promastigotes with explanted salivary glands of the insect Oncopeltus fasciatus was reduced when parasites were pre-treated with MDL28170, which was correlated to reduced levels of surface cruzipain-like and gp63-like molecules. Treatment of parasites with anti-Drosophila melanogaster (Dm) calpain antibody also decreased the adhesion process. Additionally, parasites recovered from the interaction process presented higher levels of surface cruzipain-like and gp63-like molecules, with similar levels of CALPs cross-reactive to anti-Dm-calpain antibody. The results confirm the importance of exploring the use of calpain inhibitors in studying parasites' physiology.
dc.formatapplication/pdf
dc.languageeng
dc.publisherFundação Oswaldo Cruz. Instituto Oswaldo Cruz
dc.rightsopen access
dc.subjectPhytomonas serpens
dc.subjectParasitos
dc.subjectPhytomonas
dc.subjectcalpain-like proteins
dc.subjectcysteine peptidase
dc.subjectcruzipain
dc.subjectGp63
dc.subjectOncopeltus fasciatus
dc.titleSusceptibility of Phytomonas serpens to calpain inhibitors in vitro: interference on the proliferation, ultrastructure, cysteine peptidase expression and interaction with the invertebrate host
dc.typeArticle


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