| Full text | |
| Author(s): |
Tanaka Shibao, Priscila Yumi
[1]
;
Cologna, Camila Takeno
[1]
;
Morandi-Filho, Romualdo
[2]
;
Wiezel, Gisele Adriano
[1]
;
Fujimura, Patricia Tiemi
[2]
;
Ueira-Vieira, Carlos
[2]
;
Arantes, Eliane Candiani
[3, 2]
Total Authors: 7
|
| Affiliation: | [1] Univ Sao Paulo, Lab Anim Toxins, Sch Pharmaceut Sci Ribeirao Preto, Ave Cafe S-N, Ribeirao Preto, SP - Brazil
[2] Univ Fed Uberlandia, Lab Genet LABGEN, Inst Genet & Biochem, Campus Umuarama, Ave Para, BR-1720 Uberlandia, MG - Brazil
[3] Univ Sao Paulo, Dept Phys & Chem, Sch Pharmaceut Sci Ribeirao Preto, Av Cafe S-N, BR-14040903 Ribeirao Preto, SP - Brazil
Total Affiliations: 3
|
| Document type: | Journal article |
| Source: | Journal of Venomous Animals and Toxins including Tropical Diseases; v. 24, NOV 29 2018. |
| Web of Science Citations: | 1 |
| Abstract | |
Abstract Background: Animal poisons and venoms are sources of biomolecules naturally selected. Rhinella schneideri toads are widespread in the whole Brazilian territory and they have poison glands and mucous gland. Recently, protein from toads’ secretion has gaining attention. Frog skin is widely known to present great number of host defense peptides and we hypothesize toads present them as well. In this study, we used a RNA-seq analysis from R. schneideri skin and biochemical tests with the gland secretion to unravel its protein molecules. Methods: Total RNA from the toad skin was extracted using TRizol reagent, sequenced in duplicate using Illumina Hiseq2500 in paired end analysis. The raw reads were trimmed and de novo assembled using Trinity. The resulting sequences were submitted to functional annotation against non-redundant NCBI database and Database of Anuran Defense Peptide. Furthermore, we performed caseinolytic activity test to assess the presence of serine and metalloproteases in skin secretion and it was fractionated by fast liquid protein chromatography using a reverse-phase column. The fractions were partially sequenced by Edman's degradation. Results: We were able to identify several classes of antimicrobial peptides, such as buforins, peroniins and brevinins, as well as PLA2, lectins and galectins, combining protein sequencing and RNA-seq analysis for the first time. In addition, we could isolate a PLA2 from the skin secretion and infer the presence of serine proteases in cutaneous secretion. Conclusions: We identified novel toxins and proteins from R. schneideri mucous glands. Besides, this is a pioneer study that presented the in depth characterization of protein molecules richness from this toad secretion. The results obtained herein showed evidence of novel AMP and enzymes that need to be further explored. (AU) | |
| FAPESP's process: | 15/18432-0 - Bioprospection of animal toxins with biotechnological interest through omic tools |
| Grantee: | Eliane Candiani Arantes Braga |
| Support Opportunities: | Regular Research Grants |
| FAPESP's process: | 13/26200-6 - Venomics Plataform of Pachycondyla villosa Proteome, Transcriptome, Cloning and Expression of toxins with biotechnological potential |
| Grantee: | Camila Takeno Cologna |
| Support Opportunities: | Scholarships in Brazil - Post-Doctoral |
| FAPESP's process: | 14/15644-3 - Rhinella schneideri mucous gland trascriptome |
| Grantee: | Priscila Yumi Tanaka Shibao |
| Support Opportunities: | Scholarships in Brazil - Master |