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Proteomic endorsed transcriptomic profiles of venom glands from Tityus obscurus and T. serrulatus scorpions
- Source :
- PLoS ONE, Vol 13, Iss 3, p e0193739 (2018), PLoS ONE
- Publication Year :
- 2018
- Publisher :
- Public Library of Science (PLoS), 2018.
-
Abstract
- Background Except for the northern region, where the Amazonian black scorpion, T. obscurus, represents the predominant and most medically relevant scorpion species, Tityus serrulatus, the Brazilian yellow scorpion, is widely distributed throughout Brazil, causing most envenoming and fatalities due to scorpion sting. In order to evaluate and compare the diversity of venom components of Tityus obscurus and T. serrulatus, we performed a transcriptomic investigation of the telsons (venom glands) corroborated by a shotgun proteomic analysis of the venom from the two species. Results The putative venom components represented 11.4% and 16.7% of the total gene expression for T. obscurus and T. serrulatus, respectively. Transcriptome and proteome data revealed high abundance of metalloproteinases sequences followed by sodium and potassium channel toxins, making the toxin core of the venom. The phylogenetic analysis of metalloproteinases from T. obscurus and T. serrulatus suggested an intraspecific gene expansion, as we previously observed for T. bahiensis, indicating that this enzyme may be under evolutionary pressure for diversification. We also identified several putative venom components such as anionic peptides, antimicrobial peptides, bradykinin-potentiating peptide, cysteine rich protein, serine proteinases, cathepsins, angiotensin-converting enzyme, endothelin-converting enzyme and chymotrypsin like protein, proteinases inhibitors, phospholipases and hyaluronidases. Conclusion The present work shows that the venom composition of these two allopatric species of Tityus are considerably similar in terms of the major classes of proteins produced and secreted, although their individual toxin sequences are considerably divergent. These differences at amino acid level may reflect in different epitopes for the same protein classes in each species, explaining the basis for the poor recognition of T. obscurus venom by the antiserum raised against other species.
- Subjects :
- Proteomics
0301 basic medicine
Potassium Channels
Tityus serrulatus
Proteome
Physiology
Sequence Homology
Scorpion Venoms
lcsh:Medicine
Peptide
Venom
Toxicology
Pathology and Laboratory Medicine
Biochemistry
Ion Channels
Database and Informatics Methods
Medicine and Health Sciences
Toxins
lcsh:Science
Peptide sequence
Phylogeny
chemistry.chemical_classification
Multidisciplinary
biology
Physics
Eukaryota
Proteases
Genomics
Enzymes
Electrophysiology
Physical Sciences
Sequence Analysis
Transcriptome Analysis
Research Article
Arthropoda
Bioinformatics
Toxic Agents
Antimicrobial peptides
Biophysics
Scorpion
Neurophysiology
Research and Analysis Methods
complex mixtures
Scorpions
03 medical and health sciences
Species Specificity
Phylogenetics
biology.animal
Arachnida
Genetics
Animals
Amino Acid Sequence
Venoms
lcsh:R
Organisms
Biology and Life Sciences
Proteins
Computational Biology
Genome Analysis
biology.organism_classification
Invertebrates
030104 developmental biology
Gene Expression Regulation
chemistry
Enzymology
Metalloproteases
lcsh:Q
Transcriptome
Sequence Alignment
Neuroscience
Subjects
Details
- Language :
- English
- ISSN :
- 19326203
- Volume :
- 13
- Issue :
- 3
- Database :
- OpenAIRE
- Journal :
- PLoS ONE
- Accession number :
- edsair.doi.dedup.....2fa7c24fb6d60e65c257a7e96f10b6b2