PhTX-II a Basic Myotoxic Phospholipase A2 from Porthidium hyoprora Snake Venom, Pharmacological Characterization and Amino Acid Sequence by Mass Spectrometry
A monomeric basic PLA₂ (PhTX-II) of 14149.08 Da molecular weight was purified to homogeneity from Porthidium hyoprora venom. Amino acid sequence by in tandem mass spectrometry revealed that PhTX-II belongs to Asp49 PLA₂ enzyme class and displays conserved domains as the catalytic network, Ca²⁺-bindi...
Guardado en:
| Autores principales: | , , |
|---|---|
| Formato: | Artículo |
| Lenguaje: | inglés |
| Publicado: |
2014
|
| Materias: | |
| Acceso en línea: | Ver en el sistema de origen Ver en el sistema de origen Enlace permanente (DOI o Handle) Enlace permanente (DOI o Handle) |
| Etiquetas: |
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
| _version_ | 1881508861801660416 |
|---|---|
| author | Huancahuire Vega, Salomon Ponce-Soto, Luis Marangoni, Sergio |
| author_browse | Huancahuire Vega, Salomon Marangoni, Sergio Ponce-Soto, Luis |
| author_facet | Huancahuire Vega, Salomon Ponce-Soto, Luis Marangoni, Sergio |
| author_sort | Huancahuire Vega, Salomon |
| collection | Producción científica |
| description | A monomeric basic PLA₂ (PhTX-II) of 14149.08 Da molecular weight was purified to homogeneity from Porthidium hyoprora venom. Amino acid sequence by in tandem mass spectrometry revealed that PhTX-II belongs to Asp49 PLA₂ enzyme class and displays conserved domains as the catalytic network, Ca²⁺-binding loop and the hydrophobic channel of access to the catalytic site, reflected in the high catalytic activity displayed by the enzyme. Moreover, PhTX-II PLA₂ showed an allosteric behavior and its enzymatic activity was dependent on Ca²⁺. Examination of PhTX-II PLA₂ by CD spectroscopy indicated a high content of alpha-helical structures, similar to the known structure of secreted phospholipase IIA group suggesting a similar folding. PhTX-II PLA₂ causes neuromuscular blockade in avian neuromuscular preparations with a significant direct action on skeletal muscle function, as well as, induced local edema and myotoxicity, in mice. The treatment of PhTX-II by BPB resulted in complete loss of their catalytic activity that was accompanied by loss of their edematogenic effect. On the other hand, enzymatic activity of PhTX-II contributes to this neuromuscular blockade and local myotoxicity is dependent not only on enzymatic activity. These results show that PhTX-II is a myotoxic Asp49 PLA₂ that contributes with toxic actions caused by P. hyoprora venom. |
| format | Article |
| id | oai:cris.upeu.edu.pe:20.500.15037/1526 |
| institution | UPeU |
| language | English |
| publishDate | 2014 |
| publishDateRange | 2014 |
| publishDateSort | 2014 |
| record_format | dspace |
| spelling | oai:cris.upeu.edu.pe:20.500.15037/15262026-11-02T12:57:04ZPhTX-II a Basic Myotoxic Phospholipase A2 from Porthidium hyoprora Snake Venom, Pharmacological Characterization and Amino Acid Sequence by Mass SpectrometryHuancahuire Vega, SalomonPonce-Soto, LuisMarangoni, SergioPhTX-IIAsp-49 PLA2Porthidium hyoproramyotoxinedema-forming activityA monomeric basic PLA₂ (PhTX-II) of 14149.08 Da molecular weight was purified to homogeneity from Porthidium hyoprora venom. Amino acid sequence by in tandem mass spectrometry revealed that PhTX-II belongs to Asp49 PLA₂ enzyme class and displays conserved domains as the catalytic network, Ca²⁺-binding loop and the hydrophobic channel of access to the catalytic site, reflected in the high catalytic activity displayed by the enzyme. Moreover, PhTX-II PLA₂ showed an allosteric behavior and its enzymatic activity was dependent on Ca²⁺. Examination of PhTX-II PLA₂ by CD spectroscopy indicated a high content of alpha-helical structures, similar to the known structure of secreted phospholipase IIA group suggesting a similar folding. PhTX-II PLA₂ causes neuromuscular blockade in avian neuromuscular preparations with a significant direct action on skeletal muscle function, as well as, induced local edema and myotoxicity, in mice. The treatment of PhTX-II by BPB resulted in complete loss of their catalytic activity that was accompanied by loss of their edematogenic effect. On the other hand, enzymatic activity of PhTX-II contributes to this neuromuscular blockade and local myotoxicity is dependent not only on enzymatic activity. These results show that PhTX-II is a myotoxic Asp49 PLA₂ that contributes with toxic actions caused by P. hyoprora venom.Articlehttps://pubmed.ncbi.nlm.nih.gov/25365526https://www.mdpi.com/2072-6651/6/11/3077/pdf?version=1414752838https://doi.org/10.3390/toxins6113077PMC424725110.3390/toxins6113077https://hdl.handle.net/20.500.15037/152625365526W2036929275enToxins2072-66512014-10-312026-06-13T13:21:57Z2026-06-13T13:21:57Z |
| spellingShingle | PhTX-II Asp-49 PLA2 Porthidium hyoprora myotoxin edema-forming activity Huancahuire Vega, Salomon Ponce-Soto, Luis Marangoni, Sergio PhTX-II a Basic Myotoxic Phospholipase A2 from Porthidium hyoprora Snake Venom, Pharmacological Characterization and Amino Acid Sequence by Mass Spectrometry |
| title | PhTX-II a Basic Myotoxic Phospholipase A2 from Porthidium hyoprora Snake Venom, Pharmacological Characterization and Amino Acid Sequence by Mass Spectrometry |
| title_full | PhTX-II a Basic Myotoxic Phospholipase A2 from Porthidium hyoprora Snake Venom, Pharmacological Characterization and Amino Acid Sequence by Mass Spectrometry |
| title_fullStr | PhTX-II a Basic Myotoxic Phospholipase A2 from Porthidium hyoprora Snake Venom, Pharmacological Characterization and Amino Acid Sequence by Mass Spectrometry |
| title_full_unstemmed | PhTX-II a Basic Myotoxic Phospholipase A2 from Porthidium hyoprora Snake Venom, Pharmacological Characterization and Amino Acid Sequence by Mass Spectrometry |
| title_short | PhTX-II a Basic Myotoxic Phospholipase A2 from Porthidium hyoprora Snake Venom, Pharmacological Characterization and Amino Acid Sequence by Mass Spectrometry |
| title_sort | phtx ii a basic myotoxic phospholipase a2 from porthidium hyoprora snake venom pharmacological characterization and amino acid sequence by mass spectrometry |
| topic | PhTX-II Asp-49 PLA2 Porthidium hyoprora myotoxin edema-forming activity |
| topic_facet | PhTX-II Asp-49 PLA2 Porthidium hyoprora myotoxin edema-forming activity |
| url | https://pubmed.ncbi.nlm.nih.gov/25365526 https://www.mdpi.com/2072-6651/6/11/3077/pdf?version=1414752838 https://doi.org/10.3390/toxins6113077 https://hdl.handle.net/20.500.15037/1526 |
| work_keys_str_mv | AT huancahuirevegasalomon phtxiiabasicmyotoxicphospholipasea2fromporthidiumhyoprorasnakevenompharmacologicalcharacterizationandaminoacidsequencebymassspectrometry AT poncesotoluis phtxiiabasicmyotoxicphospholipasea2fromporthidiumhyoprorasnakevenompharmacologicalcharacterizationandaminoacidsequencebymassspectrometry AT marangonisergio phtxiiabasicmyotoxicphospholipasea2fromporthidiumhyoprorasnakevenompharmacologicalcharacterizationandaminoacidsequencebymassspectrometry |