RESUMO Rhipicephalus (Boophilus) microplus (Canestrini) é um dos parasitas que mais impactam a pecuária de países tropicais e subtropicais, incluindo o Brasil, com perdas em torno de US$ 3,24 bilhões por ano. Ocorrências de populações resistentes a diferentes classes de acaricidas e suas associações têm sido amplamente diagnosticadas em todo o Brasil. Para isso, bioensaios utilizando o teste de pacote larval (LPT) impregnado com cipermetrina e diazinon em diferentes concentrações foram realizados para caracterizar a resistência fenotípica (nível de resistência, RL), a resistência molecular (mutação no domínio III - S6 T2134A) e o metabolismo enzimático do diazinon e da cipermetrina em algumas populações de R. (Boophilus) microplus coletadas em diferentes regiões do estado de São Paulo. Dentre as 40 propriedades analisadas, 18 delas apresentaram fatores de resistência à cipermetrina, sendo RL I (53%) e RL II (47%). A mutação do domínio III T2134A foi encontrada pela primeira vez no Brasil, em sete fazendas. Larvas heterozigotas foram constatadas em seis delas, e larvas homozigotas resistentes em quatro. Nenhuma diferença (P>0,05) na atividade enzimática de α-esterase e β-esterase foi observada em testes com larvas vivas e mortas em uma concentração de cipermetrina de 409,6μg/cm2. Noventa por cento das propriedades apresentaram resistência ao agente ativo diazinon: RL I em 6%, RL II em 30% e RL III em 64%. Houve diferenças significativas (P<0,05) na atividade enzimática na concentração mais elevada (3,2μg/cm2) entre os grupos de larvas vivas e mortas.

ABSTRACT Rhipicephalus (Boophilus) microplus is one of the parasites that has an impact on livestock farming in Brazil. Bioassays using the larval packet test (LPT) impregnated with cypermethrin and diazinon at different concentrations were performed to characterize phenotypic resistance (resistance level, RL), molecular resistance (mutation in domain III - S6 T2134A) and enzymatic metabolism of diazinon and cypermethrin in some populations of R. microplus that were collected in different regions of the state of São Paulo. Among the 40 farms analyzed, 18 of them presented resistance factors for cypermethrin, with RL I (53%) and RL II (47%). Mutation of domain III T2134A was found for the first time in Brazil, on seven farms. Heterozygous larvae were found on six of them and resistant homozygous larvae on four. No differences (p>0.05) in enzymatic activity of α-esterase and β-esterase were found in tests with live and dead larvae at a cypermethrin concentration of 409.6μg/cm2. Ninety percent of the farms showed resistance to the active agent diazinon: RL I in 6%, RL II in 30% and RL III in 64%. There were significant differences (p<0.05) in enzymatic activity at the highest concentration (3.2μg/cm2).

Preference for specific protein substrates together with differential sensitivity to activators and inhibitors has allowed classification of serine/threonine protein phosphatases (PPs) into four major types designated types 1, 2A, 2B and 2C (PP1, PP2A, PP2B and PP2C, respectively). Comparison of sequences within their catalytic domains has indicated that PP1, PP2A and PP2B are members of the same gene family named PPP. On the other hand, the type 2C enzyme does not share sequence homology with the PPP members and thus represents another gene family, known as PPM. In this report we briefly summarize some of our studies about the role of serine/threonine phosphatases in growth and differentiation of three different eukaryotic models: Blastocladiella emersonii, Neurospora crassa and Dictyostelium discoideum. Our observations suggest that PP2C is the major phosphatase responsible for dephosphorylation of amidotransferase, an enzyme that controls cell wall synthesis during Blastocladiella emersonii zoospore germination. We also report the existence of a novel acid- and thermo-stable protein purified from Neurospora crassa mycelia, which specifically inhibits the PP1 activity of this fungus and mammals. Finally, we comment on our recent results demonstrating that Dictyostelium discoideum expresses a gene that codes for PP1, although this activity has never been demonstrated biochemically in this organism.