Venom Profiling of the Insular Species Bothrops alcatraz: Characterization of Proteome, Glycoproteome, and N-Terminome Using Terminal Amine Isotopic Labeling of Substrates
Autor: | Solange M.T. Serrano, Silvia Regina Travaglia-Cardoso, Débora Andrade-Silva, Milton Y. Nishiyama, André Zelanis |
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Rok vydání: | 2021 |
Předmět: |
0301 basic medicine
030102 biochemistry & molecular biology biology Toxin Lectin Venom General Chemistry Terminal amine isotopic labeling of substrates Bothrops alcatraz biology.organism_classification medicine.disease_cause complex mixtures Biochemistry 03 medical and health sciences 030104 developmental biology Snake venom Proteome biology.protein medicine Bothrops |
Zdroj: | Journal of Proteome Research. 20:1341-1358 |
ISSN: | 1535-3907 1535-3893 |
Popis: | Bothrops alcatraz, a species endemic to Alcatrazes Islands, is regarded as critically endangered due to its small area of occurrence and the declining quality of its habitat. We recently reported the identification of N-glycans attached to toxins of Bothrops species, showing similar compositions in venoms of the B. jararaca complex (B. jararaca, B. insularis, and B. alcatraz). Here, we characterized B. alcatraz venom using electrophoretic, proteomic, and glycoproteomic approaches. Electrophoresis showed that B. alcatraz venom differs from B. jararaca and B. insularis; however, N-glycan removal revealed similarities between them, indicating that the occupation of N-glycosylation sites contributes to interspecies variability in the B. jararaca complex. Metalloproteinase was the major toxin class identified in the B. alcatraz venom proteome followed by serine proteinase and C-type lectin, and overall, the adult B. alcatraz venom resembles that of B. jararaca juvenile specimens. The comparative glycoproteomic analysis of B. alcatraz venom with B. jararaca and B. insularis indicated that there may be differences in the utilization of N-glycosylation motifs among their different toxin classes. Furthermore, we prospected for the first time the N-terminome of a snake venom using the terminal amine isotopic labeling of substrates (TAILS) approach and report the presence of ∼30% of N-termini corresponding to truncated toxin forms and ∼37% N-terminal sequences blocked by pyroglutamic acid in B. alcatraz venom. These findings underscore a low correlation between venom gland transcriptomes and proteomes and support the view that post-translational processes play a major role in shaping venom phenotypes. |
Databáze: | OpenAIRE |
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