Characterization of cathepsin B proteinase (AcCP-2) in eggs and larvae stages of hookworm Ancylostoma caninum

Yang, Yurong; Qin, Weiwen; Hua, Wei; Ying, Jianxi; Jing, Zhen

doi:10.1016/j.exppara.2011.08.018

Cited by 10 publications

(5 citation statements)

References 35 publications

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“…In addition, like embryonic development, proteolysis is an essential metabolic process required for protein processing. The cysteine proteases that are present in the embryonic and larval stages of parasites suggest that these proteases may function in ways related not only to the development of parasitism and nutrition digestion but also to the embryonic and larval development (HASHMI et al, 2002;YANG et al, 2011). Therefore, protease inhibition may be another strategy to control parasites.…”

Section: Introductionmentioning

confidence: 99%

Lectin, hemolysin and protease inhibitors in seed fractions with ovicidal activity against Haemonchus contortus

Salles

Braga

Nascimento³

et al. 2014

Rev. Bras. Parasitol. Vet.

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Bioactive molecules of plant species are promising alternatives for the chemical control of gastrointestinal nematodes in ruminants. Extracts of native and exotic seed species from Brazil's semi-arid region were tested in vitro in an egg hatch assay and the bioactivity of their proteins was investigated. Each seed species was subjected to three extractions with three types of solvents. All the seeds showed ovicidal activity, which varied according to the solvents. Higher ovicidal activity was found in the molecule fractions of low molecular weight (<12 kDa) for Albizia lebbeck, Ipomoea asarifolia, Jatropha curcas, Libidibia ferrea, Moringa oleifera and Ricinus communis (P<0.05, Bonferroni test). The two fractions of Crotalaria spectabilis showed the same ovicidal activity (P>0.05, Bonferroni test). Hemagglutinating activity was detected in the fractions of C. spectabilis and M. oleifera fractions, hemolysin activity in the A. lebbeck and M. oleifera fractions, serine protease inhibitory activity in the A. lebbeck, I. asarifolia, J. curcas, M. oleifera and R. communis fractions, cysteine protease inhibitor activity in the M. oleifera fraction, and no protein activity in the L. ferrea fraction. The results of this work reveal new plant species with a potential for use in controlling nematode parasites in goats, thus opening a new field of research involving plant protein molecules with ovicidal properties.Keywords: Goats, nematodes, egg hatch assay, lectin, protease inhibitors, hemolysin. ResumoMoléculas bioativas de espécies vegetais são alternativas promissoras ao controle químico dos nematoides gastrintestinais em ruminantes. Extratos de sementes de espécies nativas e exóticas do Semiárido Brasileiro foram testados in vitro em ensaio de eclosão de ovos e investigada a natureza proteica da bioatividade. Três extrações com três solventes foram feitas para cada semente estudada. Todas as sementes apresentaram atividade ovicida, variando com o solvente utilizado. Maior taxa de inibição da eclosão concentrou-se nas frações de moléculas de baixa massa molecular (<12 kDa) para Albizia lebbeck, Ipomoea asarifolia, Jatropha curcas, Libidibia ferrea, Moringa oleifera e Ricinus communis (P<0,05, teste de Bonferroni). Crotalaria spectabilis mostrou atividade nas duas frações, sem diferença entre elas (P>0,05, teste de Bonferroni). Observou-se atividade hemaglutinante nas frações de C. spectabilis e M. oleifera, de hemolisina em A. lebbeck e M. oleifera, de atividade inibidora de protease da serina em A. lebbeck, I. asarifolia, J. curcas, M. oleifera

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Section: Introductionmentioning

confidence: 99%

Lectin, hemolysin and protease inhibitors in seed fractions with ovicidal activity against Haemonchus contortus

Salles

Braga

Nascimento³

et al. 2014

Rev. Bras. Parasitol. Vet.

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“…The present work is an attempt to serologically diagnose hookworm infection in dogs by indirect ELISA using recombinant AcCP2, a Cathepsin B protease of A. caninum. Since, AcCP2 is secreted by both the adult and larval hookworms (Yang et al 2011), it may prove to be a useful candidate for use in serodiagnosis of hookworm infections. In the present study, 1023 bp AcCP2 gene was amplified (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Cathepsin B protease activity has been reported to be present in the adult, larvae and eggs of A. caninum (Harrop et al 1995a, b, Yang et al 2011. The immunolocalization of cathepsin B proteinase (AcCP2) in eggs and larval stages of A. caninum suggests that these proteases, besides helping in development of parasitism and nutrient digestion, also relate to the embryo and larval development (Yang et al 2011).…”

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confidence: 99%

Standardization of recombinant Ancylostoma caninum cysteine protease 2 (rAcCP2) based indirect ELISA for serodiagnosis of hookworm infection in dogs

Uke

Garg

Rafiqi

et al. 2018

Indian J of Anim Sci

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Diagnosis of hookworm infection in dogs during pre-patentency or in pregnant bitches harbouring encysted larvae in tissues can be achieved by employing serological tests using proteins derived from somatic or excretorysecretory products of adult or larvae of Ancylostoma caninum. In the present study, cathepsin-B protease (AcCP2) of A. caninum, which helps in development of parasitism and nutrient digestion, was used to develop an indirect ELISA for detection of specific antibodies to A. caninum in dogs. The rAcCP2 (approx. 59.0 kDa) was cloned, expressed and purified under denaturing conditions. Serum samples of 20 known A. caninum positive and 15 known negative dogs were used for the standardization of indirect ELISA. The sensitivity and specificity of the assay was determined by using sera samples from 123 dogs (48 positive for A. caninum eggs in faeces and 75 faecal negative). Out of the 48 A. caninum faecal positive sera, 46 were tested positive (OD > 0.306) by indirect ELISA; whereas, 14 out of 75 faecal negative samples were also tested positive (OD > 0.306) by indirect ELISA. Based on the results, the sensitivity and specificity of rAcCP2 based indirect ELISA was calculated to be 95.8% and 84.3%, respectively. No cross-reactions were observed with serum from dogs naturally infected with B. canis vogeli, B. gibsoni, E. canis, Dirofilaria immitis and Toxocara canis. The results of the present study indicate that indirect ELISA with rAcCP2 protein might be appropriate in large scale epidemiological screening and for serological diagnosis of A. caninum infection in dogs.

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“…Therefore, in these blood-feeding nematodes the cysteine proteases are generally located in the digestive system such as intestines and pharynx (Harrop et al, 1995;Jasmer et al, 2001;Williamson et al, 2002;Yang et al, 2011). Similarly, A. cantonensis cysteine protease AC-cathB-1, and -2 were located on the digestive tract or gut microvilli.…”

Section: Discussionmentioning

confidence: 97%

Immunolocalization and developmental expression patterns of two cathepsin B proteases (AC-cathB-1, -2) of Angiostrongylus cantonensis

Yu¹,

Wang²,

Zhang³

et al. 2014

Experimental Parasitology

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Characterization of cathepsin B proteinase (AcCP-2) in eggs and larvae stages of hookworm Ancylostoma caninum

Cited by 10 publications

References 35 publications

Lectin, hemolysin and protease inhibitors in seed fractions with ovicidal activity against Haemonchus contortus

Lectin, hemolysin and protease inhibitors in seed fractions with ovicidal activity against Haemonchus contortus

Standardization of recombinant Ancylostoma caninum cysteine protease 2 (rAcCP2) based indirect ELISA for serodiagnosis of hookworm infection in dogs

Immunolocalization and developmental expression patterns of two cathepsin B proteases (AC-cathB-1, -2) of Angiostrongylus cantonensis

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