A <i>Boophilus microplus</i> vitellin-degrading cysteine endopeptidase

Seixas, Adriana; Santos, Patricia C. Dos; Velloso, Fernando F.; Vaz, Itabajara da Silva; Masuda, Aoi; Horn, Fabiana; Termignoni, Carlos

doi:10.1017/s0031182002002731

Cited by 55 publications

(56 citation statements)

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“…Previous studies demonstrated the presence of acidic peptidase activity in R. microplus gut, ovary, egg and larva (Renard et al 2002;Seixas et al 2003;Estrela Fig. 2.…”

Section: Discussionmentioning

confidence: 91%

“…The cathepsin-L-like protease from the tick Ornithodoros moubata plays a role in the digestion of vitellin (Vt), the major reserve protein in arthropod eggs, providing nutrients during embryogenesis (Fagotto, 1990). In R. microplus, 2 cysteine endopeptidases involved in Vt hydrolysis have been studied: vitellin-degrading cysteine endopeptidase (VTDCE; Seixas et al 2003) and Riphicephalus microplus larval cysteine endopeptidase (RmLCE; Estrela et al 2007). VTDCE was previously purified from R. microplus eggs by a purification protocol in which an autolysis step to hydrolyse Vt is crucial (Seixas et al 2003).…”

Section: Introductionmentioning

confidence: 99%

“…In R. microplus, 2 cysteine endopeptidases involved in Vt hydrolysis have been studied: vitellin-degrading cysteine endopeptidase (VTDCE; Seixas et al 2003) and Riphicephalus microplus larval cysteine endopeptidase (RmLCE; Estrela et al 2007). VTDCE was previously purified from R. microplus eggs by a purification protocol in which an autolysis step to hydrolyse Vt is crucial (Seixas et al 2003). Contrarily to VTDCE, the larval cysteine endopeptidase RmLCE elutes from an anionic resin free of Vt. BmCL1, another cysteine endopeptidase from R. microplus, was localized in probable secretory cells of the gut and may be involved in haemoglobin degradation (Renard et al 2000(Renard et al , 2002.…”

Section: Introductionmentioning

confidence: 99%

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Localization and function ofRhipicephalus (Boophilus) microplusvitellin-degrading cysteine endopeptidase

et al. 2010

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S U M M A R YThe tick Rhipicephalus (Boophilus) microplus is an important parasite of cattle in many areas of the tropics. Characterization of molecules involved in mechanisms such as vitellogenesis and embryo development may contribute to a better understanding of this parasite's physiology. The vitellin-degrading cysteine endopeptidase (VTDCE) is the most active enzyme involved in vitellin hydrolysis in R. microplus eggs. Here we show an association between VTDCE and vitellin in an additional site, apart from the active site. Our data also demonstrate cysteine endopeptidase activity in different tissues such as ovary, gut, fat body, salivary gland and female haemolymph, where it is controlled by a physiological inhibitor. In R. microplus female gut, VTDCE is localized in areas of protein synthesis and trafficking with the underlying haemolymph. VTDCE is also localized in the ovary basal region, in vesicle membranes of ovary pedicel cells and in oocyte cytosol. These results suggest that VTDCE plays a role in vitellin digestion during tick development.

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“…Previous studies demonstrated the presence of acidic peptidase activity in R. microplus gut, ovary, egg and larva (Renard et al 2002;Seixas et al 2003;Estrela Fig. 2.…”

Section: Discussionmentioning

confidence: 91%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Localization and function ofRhipicephalus (Boophilus) microplusvitellin-degrading cysteine endopeptidase

et al. 2010

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“…During attaching mammalian hosts the temperature of the circumstance is around 35°C, but after dropping off, it is depending on the ambient temperature. Recently, broad temperature activity profiles were also shown with cysteine endopeptidase purified from eggs of the hard tick B. microplus [15]. Broad preference of HlSP for temperature might be related to behavioral features of the hard ticks.…”

Section: Discussionmentioning

confidence: 95%

Enzymatic Characterization of a Cubilin-Related Serine Proteinase from the Hard Tick Haemaphysalis longicornis

et al. 2004

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ABSTRACT. In the present study, we performed enzymatic characterization of Haemaphysalis longicornis serine proteinase (HlSP) with a view to shed light on the mechanisms of blood digestion in the hard ticks. Escherichia coli-expressed recombinant HlSP (rHlSP) was shown to potently hydrolyze the synthetic substrates Bz-(DL)-Arg-pNA, Z-Ala-Ala-Leu-pNA and Suc-Ala-Ala-Ala-pNA and yielded an activity of 31.5, 88.2 and 18.3 µmol/min/mg protein, respectively at an optimum temperature of 25°C. However, the enzyme showed little activity to hydrolyze the substratese Suc-Arg-Pro-Phe-His-Leu-Leu-Val-Tyr-MCA and Pyr-Phe-Leu-pNA. The optimum pH for the enzyme was shown to be 4.0 to 5.0. Several inhibitors such as antipain, leupeptin and phenylmethylsulfonyl fluoride (PMSF), specific for serine proteinase were shown to inhibit enzyme activity by 20-82%, while E-64 (specific for cysteine proteinases) and pepstatinA (specific for aspartic proteinases) had shown only little inhibitory effects on it. This is the first report on enzymatic characterization of a functional serine proteinase from the hard ticks. KEY WORDS: enzyme activity, Haemaphysalis longicornis, serine proteinase.J. Vet. Med. Sci. 66(10): 1195-1198, 2004 Ticks and tick-borne diseases are of extreme importance throughout the world and the associated economic losses are immense. Reliance on acaricides for tick control has led to serious problems which include development of resistance to acaricides that created control problems [5], and increased the threat to the wide-spread occurrence of the pathogens associated with ticks. In addition, chemical residues in animal products, and the effects of such chemicals on the environment, must be considered when new acaricides are developed.Proteolytic enzymes may represent interesting target molecules for drug design because of its involvement in the mediation of a wide range of cellular processes such as protein metabolism and the processing of precursor proteins in the living organisms [11]. In haematophagous ticks, blood digestion in the midgut is thought to be the most essential process because it is the source of energy as well as the most critical interface between the ticks and the pathogens that transmitted by ticks. Studies have reported that aspartic and cysteine proteinases exert proteolytic role, in the midguts [8,13] of the hard tick Boophilus microplus.The hard tick Haemaphysalis longicornis is distributed in a vast area of Eurasia, including Japan [6], where it transmits a wide range of pathogens, including viruses, rickettsia and protozoan parasites, causing important human and animal diseases [17]. In particular, H. longicornis serves as a vector of Theileria orientalis, which is the most economically important protozoan infectious disease of cattle in Asia [6]. In contrast to the extensive reports on proteinase activities in haematophagous insects, very little is known about these activities in the hard tick H. longicornis despite of its high vector potentiality.Recently, we cloned and partially characteri...

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“…The tick energetic metabolism has been investigated in the different embryogenesis phases. An interesting observation is that all proteases already characterized are proteinases that require an acidic pH to become activated (LOGULLO et al, 1998;SEIXAS et al, 2003;POHL et al, 2008). Indeed, it has been observed that eggs of R.…”

Section: Tick Heme-binding Aspartic Proteinase -Thapmentioning

confidence: 99%

New approaches toward anti-Rhipicephalus (Boophilus) microplus tick vaccine

Parizi¹,

Pohl²,

Masuda³

et al. 2009

RBPV

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The tick Rhipicephalus (Boophilus) microplus (formerly Boophilus microplus) is the major ectoparasite affecting livestock in America, Asia, Africa, and Oceania. Conventional tick control is based on the use of acaricides but immunization of bovines with tick gut proteins induces only a partial protective immune response. Based on this information, distinct research groups have explored the possibility of protecting the animals by inducing an immune response against other tick proteins. However, the antigens so far described do not induce the necessary protection for suppressing the use of acaricides. Currently, several groups are engaged in identifying new tick proteins to be used as targets for the development of new vaccines. This approach focuses on the enhancement of the immunogenicity of antigens already tested by incorporating new adjuvants or formulations and by searching for new antigens. This paper reviews the work done by Brazilian researchers to develop a vaccine against this tick.Keywords: Boophilus microplus, Rhipicephalus microplus, vaccine, tick, control. ResumoO carrapato Rhipicephalus (Boophilus) microplus (anteriormente Boophilus microplus) é o principal ectoparasita que afeta bovinos na América, Ásia, África e Oceania e o seu controle é tradicionalmente realizado através do uso de acaricidas. Experimentos de imunização com proteínas do carrapato mostram que a resposta imune desenvolvida pelos bovinos vacinados protege, em parte, os animais do parasitismo. Baseado nessas observações, vários grupos de pesquisa exploram a possibilidade de proteger os animais pela indução de uma resposta imune contra proteínas do carrapato. Entretanto, os antígenos já caracterizados não asseguram o grau de proteção necessário para suprimir o uso de acaricidas. Portanto, esses grupos de pesquisa estão engajados na tentativa de identificar novas proteínas que possam ser utilizadas para o desenvolvimento de novas vacinas, as quais possam induzir maior imunogenicidade de que os antígenos já testados, através do uso de novas formulações e/ou pela incorporação de adjuvantes. O presente artigo apresenta uma revisão da literatura sobre os resultados obtidos por pesquisadores brasileiros no desenvolvimento de vacinas contra o carrapato.

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A Boophilus microplus vitellin-degrading cysteine endopeptidase

Cited by 55 publications

References 24 publications

Localization and function ofRhipicephalus (Boophilus) microplusvitellin-degrading cysteine endopeptidase

Localization and function ofRhipicephalus (Boophilus) microplusvitellin-degrading cysteine endopeptidase

Enzymatic Characterization of a Cubilin-Related Serine Proteinase from the Hard Tick Haemaphysalis longicornis

New approaches toward anti-Rhipicephalus (Boophilus) microplus tick vaccine

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