Proteomics and immunocharacterization of Asian mountain pit viper (Ovophis monticola) venom.
The venomic profile of Asian mountain pit viper Ovophis monticola is clarified in the present study. Using mass spectrometry-based proteomics, 247 different proteins were identified in crude venom of O. monticola found in Thailand. The most abundant proteins were snake venom metalloproteases (SVMP)...
| Main Authors: | , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2021-01-01
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| Series: | PLoS ONE |
| Online Access: | https://doi.org/10.1371/journal.pone.0260496 |
| _version_ | 1818966203792621568 |
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| author | Siravit Sitprija Lawan Chanhome Onrapak Reamtong Tipparat Thiangtrongjit Taksa Vasaruchapong Orawan Khow Jureeporn Noiphrom Panithi Laoungbua Arissara Tubtimyoy Narongsak Chaiyabutr Supeecha Kumkate |
| author_facet | Siravit Sitprija Lawan Chanhome Onrapak Reamtong Tipparat Thiangtrongjit Taksa Vasaruchapong Orawan Khow Jureeporn Noiphrom Panithi Laoungbua Arissara Tubtimyoy Narongsak Chaiyabutr Supeecha Kumkate |
| author_sort | Siravit Sitprija |
| collection | DOAJ |
| description | The venomic profile of Asian mountain pit viper Ovophis monticola is clarified in the present study. Using mass spectrometry-based proteomics, 247 different proteins were identified in crude venom of O. monticola found in Thailand. The most abundant proteins were snake venom metalloproteases (SVMP) (36.8%), snake venom serine proteases (SVSP) (31.1%), and phospholipases A2 (PLA2) (12.1%). Less abundant proteins included L-amino acid oxidase (LAAO) (5.7%), venom nerve growth factor (3.6%), nucleic acid degrading enzymes (3.2%), C-type lectins (CTL) (1.6%), cysteine-rich secretory proteins (CRISP) (1.2%) and disintegrin (1.2%). The immunoreactivity of this viper's venom to a monovalent antivenom against green pit viper Trimeresurus albolabris, or to a polyvalent antivenom against hemotoxic venom was investigated by indirect ELISA and two-dimensional (2D) immunoblotting. Polyvalent antivenom showed substantially greater reactivity levels than monovalent antivenom. A titer for the monovalent antivenom was over 1:1.28x107 dilution while that of polyvalent antivenom was 1:5.12x107. Of a total of 89 spots comprising 173 proteins, 40 spots of predominantly SVMP, SVSP and PLA2 were specific antigens for antivenoms. The 49 unrecognized spots containing 72 proteins were characterized as non-reactive proteins, and included certain types of CTLs and CRISPs. These neglected venom constituents could limit the effectiveness of antivenom-based therapy currently available for victims of pit viper envenomation. |
| first_indexed | 2024-12-20T13:29:10Z |
| format | Article |
| id | doaj.art-b89f9ea2d10c4be88357ba225d94d61c |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-20T13:29:10Z |
| publishDate | 2021-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-b89f9ea2d10c4be88357ba225d94d61c2022-12-21T19:39:10ZengPublic Library of Science (PLoS)PLoS ONE1932-62032021-01-011612e026049610.1371/journal.pone.0260496Proteomics and immunocharacterization of Asian mountain pit viper (Ovophis monticola) venom.Siravit SitprijaLawan ChanhomeOnrapak ReamtongTipparat ThiangtrongjitTaksa VasaruchapongOrawan KhowJureeporn NoiphromPanithi LaoungbuaArissara TubtimyoyNarongsak ChaiyabutrSupeecha KumkateThe venomic profile of Asian mountain pit viper Ovophis monticola is clarified in the present study. Using mass spectrometry-based proteomics, 247 different proteins were identified in crude venom of O. monticola found in Thailand. The most abundant proteins were snake venom metalloproteases (SVMP) (36.8%), snake venom serine proteases (SVSP) (31.1%), and phospholipases A2 (PLA2) (12.1%). Less abundant proteins included L-amino acid oxidase (LAAO) (5.7%), venom nerve growth factor (3.6%), nucleic acid degrading enzymes (3.2%), C-type lectins (CTL) (1.6%), cysteine-rich secretory proteins (CRISP) (1.2%) and disintegrin (1.2%). The immunoreactivity of this viper's venom to a monovalent antivenom against green pit viper Trimeresurus albolabris, or to a polyvalent antivenom against hemotoxic venom was investigated by indirect ELISA and two-dimensional (2D) immunoblotting. Polyvalent antivenom showed substantially greater reactivity levels than monovalent antivenom. A titer for the monovalent antivenom was over 1:1.28x107 dilution while that of polyvalent antivenom was 1:5.12x107. Of a total of 89 spots comprising 173 proteins, 40 spots of predominantly SVMP, SVSP and PLA2 were specific antigens for antivenoms. The 49 unrecognized spots containing 72 proteins were characterized as non-reactive proteins, and included certain types of CTLs and CRISPs. These neglected venom constituents could limit the effectiveness of antivenom-based therapy currently available for victims of pit viper envenomation.https://doi.org/10.1371/journal.pone.0260496 |
| spellingShingle | Siravit Sitprija Lawan Chanhome Onrapak Reamtong Tipparat Thiangtrongjit Taksa Vasaruchapong Orawan Khow Jureeporn Noiphrom Panithi Laoungbua Arissara Tubtimyoy Narongsak Chaiyabutr Supeecha Kumkate Proteomics and immunocharacterization of Asian mountain pit viper (Ovophis monticola) venom. PLoS ONE |
| title | Proteomics and immunocharacterization of Asian mountain pit viper (Ovophis monticola) venom. |
| title_full | Proteomics and immunocharacterization of Asian mountain pit viper (Ovophis monticola) venom. |
| title_fullStr | Proteomics and immunocharacterization of Asian mountain pit viper (Ovophis monticola) venom. |
| title_full_unstemmed | Proteomics and immunocharacterization of Asian mountain pit viper (Ovophis monticola) venom. |
| title_short | Proteomics and immunocharacterization of Asian mountain pit viper (Ovophis monticola) venom. |
| title_sort | proteomics and immunocharacterization of asian mountain pit viper ovophis monticola venom |
| url | https://doi.org/10.1371/journal.pone.0260496 |
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