Isolation of two basic phospholipases A2 from Bothrops diporus snake venom : Comparative characterization and synergism between Asp49 and Lys49 variants
Bothrops diporus, previously considered a subspecies of the B. neuwiedi complex, is a medically relevant viperid in Northeastern Argentina. The venom of this species causes local tissue damage characterized by myonecrosis, hemorrhage, blistering, and edema. In the present study, two basic phosphol...
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| Formato: | Artículo |
| Lenguaje: | Español |
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Elsevier Ltd.
2025
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| Acceso en línea: | http://repositorio.unne.edu.ar/handle/123456789/58045 |
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I48-R184-123456789-580452025-10-22T11:44:55Z Isolation of two basic phospholipases A2 from Bothrops diporus snake venom : Comparative characterization and synergism between Asp49 and Lys49 variants Bustillo, Soledad Fernández, Julián Chaves-Araya, Stephanie Angulo, Yamileth Leiva, Laura Cristina Ana Lomonte, Bruno Snake venom Bothrops diporus Phospholipase A2 Synergism Myotoxicity Cytotoxicity Bothrops diporus, previously considered a subspecies of the B. neuwiedi complex, is a medically relevant viperid in Northeastern Argentina. The venom of this species causes local tissue damage characterized by myonecrosis, hemorrhage, blistering, and edema. In the present study, two basic phospholipases A2 (PLA2-I and PLA2-II) were isolated from this venom, and their pathological effects upon murine skeletal muscle and myogenic cells in culture were analyzed. Partial amino acid sequencing showed that PLA2-I and PLA2-II are Asp49 and Lys49 PLA2s, respectively. In agreement with this, PLA2-I showed PLA2 activity, whereas PLA2-II did not. Functional assays revealed differences in their myotoxicity, cytotoxicity, and anti-adhesion activity, and in the ability to inhibit cell migration, all of which were greater for the Lys49 variant. Native electrophoresis showed that PLA2-I was less basic than PLA2-II. The two proteins act synergistically to affect the integrity of C2C12 myogenic cells, providing a further example of the concerted action of coexisting snake venom components. PLA2-I and PLA2-II, together with additional basic PLA2s revealed by RP-HPLC, probably play an important role in myonecrosis after envenomation by B. diporus. 2025-08-20T10:38:55Z 2025-08-20T10:38:55Z 2019-10-16 Artículo Bustillo, Soledad, et. al, 2019. Isolation of two basic phospholipases A2 from Bothrops diporus snake venom : Comparative characterization and synergism between Asp49 and Lys49 variants. Toxicon: Países Bajos, Elsevier Ltd., p. 113-121, ISSN 0041-0101. 0041-0101 http://repositorio.unne.edu.ar/handle/123456789/58045 spa https://doi.org/10.1016/j.toxicon.2019.07.004 openAccess http://creativecommons.org/licenses/by-nc-nd/2.5/ar/ application/pdf p. 113-121 application/pdf Elsevier Ltd. Toxicon, 2019, vol. 168, p. 113-121. |
| institution |
Universidad Nacional del Nordeste |
| institution_str |
I-48 |
| repository_str |
R-184 |
| collection |
RIUNNE - Repositorio Institucional de la Universidad Nacional del Nordeste (UNNE) |
| language |
Español |
| topic |
Snake venom Bothrops diporus Phospholipase A2 Synergism Myotoxicity Cytotoxicity |
| spellingShingle |
Snake venom Bothrops diporus Phospholipase A2 Synergism Myotoxicity Cytotoxicity Bustillo, Soledad Fernández, Julián Chaves-Araya, Stephanie Angulo, Yamileth Leiva, Laura Cristina Ana Lomonte, Bruno Isolation of two basic phospholipases A2 from Bothrops diporus snake venom : Comparative characterization and synergism between Asp49 and Lys49 variants |
| topic_facet |
Snake venom Bothrops diporus Phospholipase A2 Synergism Myotoxicity Cytotoxicity |
| description |
Bothrops diporus, previously considered a subspecies of the B. neuwiedi complex, is a medically relevant viperid in
Northeastern Argentina. The venom of this species causes local tissue damage characterized by myonecrosis,
hemorrhage, blistering, and edema. In the present study, two basic phospholipases A2 (PLA2-I and PLA2-II) were
isolated from this venom, and their pathological effects upon murine skeletal muscle and myogenic cells in
culture were analyzed. Partial amino acid sequencing showed that PLA2-I and PLA2-II are Asp49 and Lys49
PLA2s, respectively. In agreement with this, PLA2-I showed PLA2 activity, whereas PLA2-II did not. Functional
assays revealed differences in their myotoxicity, cytotoxicity, and anti-adhesion activity, and in the ability to
inhibit cell migration, all of which were greater for the Lys49 variant. Native electrophoresis showed that PLA2-I
was less basic than PLA2-II. The two proteins act synergistically to affect the integrity of C2C12 myogenic cells,
providing a further example of the concerted action of coexisting snake venom components. PLA2-I and PLA2-II,
together with additional basic PLA2s revealed by RP-HPLC, probably play an important role in myonecrosis after
envenomation by B. diporus. |
| format |
Artículo |
| author |
Bustillo, Soledad Fernández, Julián Chaves-Araya, Stephanie Angulo, Yamileth Leiva, Laura Cristina Ana Lomonte, Bruno |
| author_facet |
Bustillo, Soledad Fernández, Julián Chaves-Araya, Stephanie Angulo, Yamileth Leiva, Laura Cristina Ana Lomonte, Bruno |
| author_sort |
Bustillo, Soledad |
| title |
Isolation of two basic phospholipases A2 from Bothrops diporus snake venom : Comparative characterization and synergism between Asp49 and Lys49 variants |
| title_short |
Isolation of two basic phospholipases A2 from Bothrops diporus snake venom : Comparative characterization and synergism between Asp49 and Lys49 variants |
| title_full |
Isolation of two basic phospholipases A2 from Bothrops diporus snake venom : Comparative characterization and synergism between Asp49 and Lys49 variants |
| title_fullStr |
Isolation of two basic phospholipases A2 from Bothrops diporus snake venom : Comparative characterization and synergism between Asp49 and Lys49 variants |
| title_full_unstemmed |
Isolation of two basic phospholipases A2 from Bothrops diporus snake venom : Comparative characterization and synergism between Asp49 and Lys49 variants |
| title_sort |
isolation of two basic phospholipases a2 from bothrops diporus snake venom : comparative characterization and synergism between asp49 and lys49 variants |
| publisher |
Elsevier Ltd. |
| publishDate |
2025 |
| url |
http://repositorio.unne.edu.ar/handle/123456789/58045 |
| work_keys_str_mv |
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