Travaglia-Cardoso, Silvia R.
Nishiyama, Jr., Milton Y.
Serrano, Solange M. T.
Total Authors: 5
 Inst Butantan, Ctr Toxins Immune Response & Cell Signaling CeTIC, Lab Toxinol Aplicada, BR-05503900 Sao Paulo - Brazil
 Univ Fed Sao Paulo, Dept Sci & Technol, Funct Prote Lab, ICT UNIFESP, BR-12231280 Sao Jose Dos Campos, SP - Brazil
 Inst Butantan, Museu Biol, BR-05503100 Sao Paulo - Brazil
Total Affiliations: 3
JOURNAL OF PROTEOME RESEARCH;
FEB 5 2021.
Web of Science Citations:
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 similar to 30% of N-termini corresponding to truncated toxin forms and similar to 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. (AU)