Serine Proteinase Inhibitors from Eggs and Larvae of Tick Boophilus microplus: Purification and Biochemical Characterization

Andreotti, Renato; Malavazi-Piza, Kelly C; Sasaki, Sergio D.; Torquato, Ricardo J.S.; Gomes, Alberto; Tanaka, Aparecida S.

doi:10.1023/a:1012242817869

Cited by 26 publications

(8 citation statements)

References 39 publications

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“…Our western blot results suggested that the calves that had been experimentally infected with ticks did not produce antibodies against serine proteinase inhibitors (in the range of 13-40 kDa). This result was in agreement with Andreotti et al (2001) and Pruett et al (2008). Lack of antibody induction against serine protease inhibitors in cattle during tick infestation may be due to the low amounts of these inhibitors introduced for immune response stimulation in the host.…”

Section: Discussionsupporting

confidence: 88%

“…Experimental challenges performed on animals previously immunized with tick larvae have shown that the animals acquired significant protective immunity against ticks, with reduction of the biological parameters that would favor ticks (ANDREOTTI et al, 2001;PREVOT et al, 2007).…”

Section: Discussionmentioning

confidence: 99%

“…Any new biochemical and physiological information about ticks may help in developing new vaccine. Tick larvae have been shown to be important sources of trypsin and chymotrypsin inhibitors (WILLADSEN; RIDING, 1979;MCKENNA, 1983;TANAKA et al, 1999;ANDREOTTI et al, 2001). There are reports suggesting that serine protease inhibitors may be candidates for use in vaccines and that such vaccines would be effective (MULENG et al, 2001;IMAMURA et al, 2005).The inhibitory activities of these proteins relating to blood clotting and inflammatory responses may facilitate ticks' blood sucking process.…”

Section: Reverse Zymographymentioning

confidence: 99%

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Assessment and partial purification of serine protease inhibitors from Rhipicephalus (Boophilus) annulatuslarvae

Nabian¹,

Taheri²,

Ranjbar³

et al. 2014

Rev. Bras. Parasitol. Vet.

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Ticks are rich sources of serine protease inhibitors, particularly those that prevent blood clotting and inflammatory responses during blood feeding. The tick Rhipicephalus (Boophlus) annulatus is an important ectoparasite of cattle. The aims of this study were to characterize and purify the serine protease inhibitors present in R. (B.) annulatus larval extract. The inhibitors were characterized by means of one and two-dimensional reverse zymography, and purified using affinity chromatography on a trypsin-Sepharose column. The analysis on one and two-dimensional reverse zymography of the larval extract showed trypsin inhibitory activity at between 13 and 40 kDa. Through non-reducing SDS-PAGE and reverse zymography for proteins purified by trypsin-Sepharose affinity chromatography, some protein bands with molecular weights between 13 and 34 kDa were detected. Western blotting showed that five protein bands at 48, 70, 110, 130 and 250 kDa reacted positively with immune serum, whereas there was no positive reaction in the range of 13-40 kDa. Serine protease inhibitors from R. (B.) annulatus have anti-trypsin activity similar to inhibitors belonging to several other hard tick species, thus suggesting that these proteins may be useful as targets in anti-tick vaccines.Keywords: Rhipicephalus (B.) annulatus, serine protease inhibitors, zymography. ResumoCarrapatos são uma rica fonte de inibidores da serina protease, particularmente aqueles que previnem coagulação e respostas inflamatórias durante a alimentação com sangue. O carrapato Rhipicephalus (B.) annulatus é um ectoparasita importante de bovinos. O objetivo deste estudo foi caracterizar e purificar os inibidores da serina protease presentes no extrato de larva do R. (B.) annulatus. Os inibidores foram caracterizados através de zimografia reversa uni e bidimensional e purificados com cromatografia de afinidade em uma coluna de sepharose-tripsina. A análise do extrato de larva pela zimografia reversa uni e bidimensional mostrou atividade inibitória de tripsina entre 13 e 40 kDa. Através de SDS-PAGE e zimografia reversa para proteínas purificadas pela cromatografia por sepharose-tripsina, algumas bandas de proteínas com pesos moleculares entre 13 e 34 kDa foram detectadas. Western blotting mostrou que cinco bandas de proteínas a 48, 70, 110, 130 e 250 kDa reagiram positivamente com o soro imune, enquanto não houve reação positiva nas bandas 13-40 kDa. Inibidores da serina protease do R. (B.) annulatus têm atividade antitripsina semelhante àquelas dos inibidores de outras espécies de carrapatos duros, sugerindo, assim, que essas proteínas podem ser úteis como alvo de vacinas contra carrapatos.Palavras-chave: Rhipicephalus (B.) annulatus, inibidores da serina protease, zimografia.

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Section: Discussionsupporting

confidence: 88%

Section: Discussionmentioning

confidence: 99%

Section: Reverse Zymographymentioning

confidence: 99%

See 1 more Smart Citation

Assessment and partial purification of serine protease inhibitors from Rhipicephalus (Boophilus) annulatuslarvae

Nabian¹,

Taheri²,

Ranjbar³

et al. 2014

Rev. Bras. Parasitol. Vet.

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“…microplus (Tanaka et al, 1999). However, differing concentrations and inhibitor specificity changes have been reported between egg and larval stages (Andreotti et al, 2001; Sasaki et al, 2004). Andreotti et al showed a 69.7 and 71.3% reduction in both engorged tick number and egg weight respectively when female ticks were fed on BmTIs-immunized cattle, confirming a crucial role for BmTIs in egg production and development (Andreotti et al, 2002).…”

Section: Role Of Serine Protease Inhibitors In Tick Biologymentioning

confidence: 99%

“…BmTI-6 , a Kunitz tSPI identified in ovaries, was also expressed in tick body fat and demonstrated specific inhibitory activity against trypsin and trypsin-like proteases, such as plasmin (Sasaki and Tanaka, 2008). As for other BmTIs, BmTI-6 is suspected to play a role in controlling endogenous proteases in the egg and larval stages (Andreotti et al, 2001; Sasaki et al, 2004). …”

Section: Role Of Serine Protease Inhibitors In Tick Biologymentioning

confidence: 99%

Serine Protease Inhibitors in Ticks: An Overview of Their Role in Tick Biology and Tick-Borne Pathogen Transmission

Blisnick

Foulon

Bonnet

2017

Front. Cell. Infect. Microbiol.

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New tick and tick-borne pathogen control approaches that are both environmentally sustainable and which provide broad protection are urgently needed. Their development, however, will rely on a greater understanding of tick biology, tick-pathogen, and tick-host interactions. The recent advances in new generation technologies to study genomes, transcriptomes, and proteomes has resulted in a plethora of tick biomacromolecular studies. Among these, many enzyme inhibitors have been described, notably serine protease inhibitors (SPIs), whose importance in various tick biological processes is only just beginning to be fully appreciated. Among the multiple active substances secreted during tick feeding, SPIs have been shown to be directly involved in regulation of inflammation, blood clotting, wound healing, vasoconstriction and the modulation of host defense mechanisms. In light of these activities, several SPIs were examined and were experimentally confirmed to facilitate tick pathogen transmission. In addition, to prevent coagulation of the ingested blood meal within the tick alimentary canal, SPIs are also involved in blood digestion and nutrient extraction from the meal. The presence of SPIs in tick hemocytes and their involvement in tick innate immune defenses have also been demonstrated, as well as their implication in hemolymph coagulation and egg development. Considering the involvement of SPIs in multiple crucial aspects of tick-host-pathogen interactions, as well as in various aspects of the tick parasitic lifestyle, these molecules represent highly suitable and attractive targets for the development of effective tick control strategies. Here we review the current knowledge regarding this class of inhibitors in tick biology and tick-borne pathogen transmission, and their potential as targets for future tick control trials.

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The effect of feeding on different hosts on the egg proteins in Haemaphysalis qinghaiensis tick

Li,

Cheng,

Liu

et al. 2024

Parasitol Res

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Serine Proteinase Inhibitors from Eggs and Larvae of Tick Boophilus microplus: Purification and Biochemical Characterization

Cited by 26 publications

References 39 publications

Assessment and partial purification of serine protease inhibitors from Rhipicephalus (Boophilus) annulatuslarvae

Assessment and partial purification of serine protease inhibitors from Rhipicephalus (Boophilus) annulatuslarvae

Serine Protease Inhibitors in Ticks: An Overview of Their Role in Tick Biology and Tick-Borne Pathogen Transmission

The effect of feeding on different hosts on the egg proteins in Haemaphysalis qinghaiensis tick

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