Comparative venomic profiles of three spiders of the genus
Ion channels
Phoneutria
Protein profile
Spider venom
Toxins
Journal
The journal of venomous animals and toxins including tropical diseases
ISSN: 1678-9199
Titre abrégé: J Venom Anim Toxins Incl Trop Dis
Pays: Brazil
ID NLM: 101201501
Informations de publication
Date de publication:
2022
2022
Historique:
received:
05
04
2021
accepted:
20
07
2021
entrez:
14
3
2022
pubmed:
15
3
2022
medline:
15
3
2022
Statut:
epublish
Résumé
Spider venoms induce different physio-pharmacological effects by binding with high affinity on molecular targets, therefore being of biotechnological interest. Some of these toxins, acting on different types of ion channels, have been identified in the venom of spiders of the genus Biochemical and functional comparison of the venoms were carried out by SDS-PAGE, HPLC, mass spectrometry, enzymatic activities and electrophysiological assays (whole-cell patch clamp). The employed approach revealed that all three venoms had an overall similarity in their components, with only minor differences. The presence of a high number of similar proteins was evident, particularly toxins in the mass range of ~6.0 kDa. Hyaluronidase and proteolytic activities were detected in all venoms, in addition to isoforms of the toxins Tx1 and Tx2-6. All Tx1 isoforms blocked Nav1.6 ion currents, with slight differences. Our findings showed that Pn-V, Pe-V and Pp-V are highly similar concerning protein composition and enzymatic activities, containing isoforms of the same toxins sharing high sequence homology, with minor modifications. However, these structural and functional variations are very important for venom diversity. In addition, our findings will contribute to the comprehension of the molecular diversity of the venoms of the other species from
Sections du résumé
Background
UNASSIGNED
Spider venoms induce different physio-pharmacological effects by binding with high affinity on molecular targets, therefore being of biotechnological interest. Some of these toxins, acting on different types of ion channels, have been identified in the venom of spiders of the genus
Methods
UNASSIGNED
Biochemical and functional comparison of the venoms were carried out by SDS-PAGE, HPLC, mass spectrometry, enzymatic activities and electrophysiological assays (whole-cell patch clamp).
Results
UNASSIGNED
The employed approach revealed that all three venoms had an overall similarity in their components, with only minor differences. The presence of a high number of similar proteins was evident, particularly toxins in the mass range of ~6.0 kDa. Hyaluronidase and proteolytic activities were detected in all venoms, in addition to isoforms of the toxins Tx1 and Tx2-6. All Tx1 isoforms blocked Nav1.6 ion currents, with slight differences.
Conclusion
UNASSIGNED
Our findings showed that Pn-V, Pe-V and Pp-V are highly similar concerning protein composition and enzymatic activities, containing isoforms of the same toxins sharing high sequence homology, with minor modifications. However, these structural and functional variations are very important for venom diversity. In addition, our findings will contribute to the comprehension of the molecular diversity of the venoms of the other species from
Identifiants
pubmed: 35283937
doi: 10.1590/1678-9199-JVATITD-2021-0042
pmc: PMC8875809
doi:
Types de publication
Journal Article
Langues
eng
Pagination
e20210042Déclaration de conflit d'intérêts
Competing interests: The authors declare that they have no competing interests.
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