Purification, characterization and molecular cloning of chymotrypsin inhibitor peptides from the venom of Burmese Daboia russelii siamensis

Guo, Chun-teng; McClean, Stephen; Shaw, Chris; Rao, Pingfan; Ye, Mingyu; Bjourson, Anthony J.

doi:10.1016/j.peptides.2013.02.009

Cited by 9 publications

(7 citation statements)

References 41 publications

(40 reference statements)

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“…siamensis 37 , although more recently this protein has been isolated from the Myanmese and Chinese D . siamensis venoms 29 , 30 . The KSPI proteoforms detected in the present study showed sequences matched to those reported previously for D .…”

Section: Discussionmentioning

confidence: 99%

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Venom proteomics and antivenom neutralization for the Chinese eastern Russell’s viper, Daboia siamensis from Guangxi and Taiwan

Tan

2018

Sci Rep

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The eastern Russell’s viper (Daboia siamensis) causes primarily hemotoxic envenomation. Applying shotgun proteomic approach, the present study unveiled the protein complexity and geographical variation of eastern D. siamensis venoms originated from Guangxi and Taiwan. The snake venoms from the two geographical locales shared comparable expression of major proteins notwithstanding variability in their toxin proteoforms. More than 90% of total venom proteins belong to the toxin families of Kunitz-type serine protease inhibitor, phospholipase A2, C-type lectin/lectin-like protein, serine protease and metalloproteinase. Daboia siamensis Monovalent Antivenom produced in Taiwan (DsMAV-Taiwan) was immunoreactive toward the Guangxi D. siamensis venom, and effectively neutralized the venom lethality at a potency of 1.41 mg venom per ml antivenom. This was corroborated by the antivenom effective neutralization against the venom procoagulant (ED = 0.044 ± 0.002 µl, 2.03 ± 0.12 mg/ml) and hemorrhagic (ED50 = 0.871 ± 0.159 µl, 7.85 ± 3.70 mg/ml) effects. The hetero-specific Chinese pit viper antivenoms i.e. Deinagkistrodon acutus Monovalent Antivenom and Gloydius brevicaudus Monovalent Antivenom showed negligible immunoreactivity and poor neutralization against the Guangxi D. siamensis venom. The findings suggest the need for improving treatment of D. siamensis envenomation in the region through the production and the use of appropriate antivenom.

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Section: Discussionmentioning

confidence: 99%

“…Several toxins had been isolated previously from D . siamensis venom, including Kunitz-type serine protease inhibitors 29 , 30 , phospholipases A 2 31 , snaclecs 32 , snake venom serine proteases 33 and snake venom metalloproteinases 34 – 36 . The venom proteome of the Myanmese D .…”

Section: Introductionmentioning

confidence: 99%

Venom proteomics and antivenom neutralization for the Chinese eastern Russell’s viper, Daboia siamensis from Guangxi and Taiwan

Tan

2018

Sci Rep

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“…A Kunitz-type inhibitor homolog (RVV inhibitor II, UniProtKB P00990) was further sequenced from the venom of the Eastern Russel’s viper (= Daboia siamensis ) [115]. Recently, similar polypeptides were identified in the venom of Daboia siamensis [49,50]. From the Burmese specie, BBPTI-1 (Table 1) was shown to strongly inhibit chymotrypsin activity, with no detectable inhibitory activity against trypsin [49].…”

Section: Pis From Terrestrial Venomous Animalsmentioning

confidence: 99%

“…Recently, similar polypeptides were identified in the venom of Daboia siamensis [49,50]. From the Burmese specie, BBPTI-1 (Table 1) was shown to strongly inhibit chymotrypsin activity, with no detectable inhibitory activity against trypsin [49]. From the Chinese one, two trypsin inhibitors (CBPTI-1 and CBPTI-2, Table 1) and one chymotrypsin inhibitor (CBPTI-3, Table 1) were purified and cloned [50].…”

Section: Pis From Terrestrial Venomous Animalsmentioning

confidence: 99%

Protease Inhibitors from Marine Venomous Animals and Their Counterparts in Terrestrial Venomous Animals

Mourão

Schwartz

2013

Marine Drugs

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The Kunitz-type protease inhibitors are the best-characterized family of serine protease inhibitors, probably due to their abundance in several organisms. These inhibitors consist of a chain of ~60 amino acid residues stabilized by three disulfide bridges, and was first observed in the bovine pancreatic trypsin inhibitor (BPTI)-like protease inhibitors, which strongly inhibit trypsin and chymotrypsin. In this review we present the protease inhibitors (PIs) described to date from marine venomous animals, such as from sea anemone extracts and Conus venom, as well as their counterparts in terrestrial venomous animals, such as snakes, scorpions, spiders, Anurans, and Hymenopterans. More emphasis was given to the Kunitz-type inhibitors, once they are found in all these organisms. Their biological sources, specificity against different proteases, and other molecular blanks (being also K+ channel blockers) are presented, followed by their molecular diversity. Whereas sea anemone, snakes and other venomous animals present mainly Kunitz-type inhibitors, PIs from Anurans present the major variety in structure length and number of Cys residues, with at least six distinguishable classes. A representative alignment of PIs from these venomous animals shows that, despite eventual differences in Cys assignment, the key-residues for the protease inhibitory activity in all of them occupy similar positions in primary sequence. The key-residues for the K+ channel blocking activity was also compared.

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“…Esses peptídeos atuam basicamente por competir com o substrato pelo sítio catalítico da enzima, impedindo a hidrólise. Esse mecanismo pode ser dependente da conformação da enzima, o tripeptídeo <EKW perde siginificativamente a habilidade de inibir a atividade da metalopeptidases como a bothropasin em presença de 1 mM CaCl2 (Marques- Porto, et.al., 2008 Earl, et.al., 2012;Qiu et al, 2013;Guo et al, 2013;Mourao & Schwartz, 2013;Mukherjee et. al., 2014).…”

Section: Inibidores De Peptidase E Peptídeosunclassified

Purificação e caracterização de inibidores de proteases de veneno de <i>Bitis gabonica rhinoceros</i> com potencial farmacológico

Fucase¹

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Agradeço a Deus pelo dom da vida e toda a proteção no decorrer do caminho. Ao meu orientador e querido amigo Dr. Patrick Jack Spencer pelo apoio e confiança. Ao meu amigo e ex-colega de trabalho Dr.Vincent Louis Viala sempre me apoiando em todos os experimentos. Aos amigos e companheiros de bancada Marcela Di Giacomo Messias e Samuel Levindo por todo carinho, ajuda, paciência e confiança Ao querido amigo Rodolfo Ferreira e minha amiguinha Larissa Miranda por todo apoio e conselhos

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Purification, characterization and molecular cloning of chymotrypsin inhibitor peptides from the venom of Burmese Daboia russelii siamensis

Cited by 9 publications

References 41 publications

Venom proteomics and antivenom neutralization for the Chinese eastern Russell’s viper, Daboia siamensis from Guangxi and Taiwan

Venom proteomics and antivenom neutralization for the Chinese eastern Russell’s viper, Daboia siamensis from Guangxi and Taiwan

Protease Inhibitors from Marine Venomous Animals and Their Counterparts in Terrestrial Venomous Animals

Purificação e caracterização de inibidores de proteases de veneno de <i>Bitis gabonica rhinoceros</i> com potencial farmacológico

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