TY - JOUR
T1 - A snapshot of Bothrops jararaca snake venom gland subcellular proteome
AU - Camacho, Maurício Frota
AU - Stuginski, Daniel R.
AU - Andrade-Silva, Débora
AU - Nishiyama-Jr, Milton Y.
AU - Valente, Richard H.
AU - Zelanis, André
N1 - Publisher Copyright:
© 2023 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM)
PY - 2023/11
Y1 - 2023/11
N2 - Snake venom protein synthesis undergoes finely regulated processes in the specialized secretory epithelium within the venom gland. Such processes occur within a defined period in the cell and at specific cellular locations. Thus, the determination of subcellular proteomes allows the characterization of protein groups for which the site may be relevant to their biological roles, thereby allowing the deconvolution of complex biological circuits into functional information. In this regard, we performed subcellular fractionation of proteins from B. jararaca venom gland, focusing on nuclear proteins since this cellular compartment comprises key effectors that shape gene expression. Our results provided a snapshot of B. jararaca's subcellular venom gland proteome and pointed to a ‘conserved’ proteome core among different life stages (newborn and adult) and between sexes (adult male and female). Overall, the top 15 highly abundant proteins identified in B. jararaca venom glands mirrored the panel of highly expressed genes in human salivary glands. Therefore, the expression profile observed for such a protein set could be considered a conserved core signature of salivary gland secretory epithelium. Moreover, the newborn venom gland displayed a unique expression signature of transcription factors involved in regulating transcription and biosynthetic processes and may mirror biological constraints of the ontogenetic development of B. jararaca, contributing to venom proteome diversity.
AB - Snake venom protein synthesis undergoes finely regulated processes in the specialized secretory epithelium within the venom gland. Such processes occur within a defined period in the cell and at specific cellular locations. Thus, the determination of subcellular proteomes allows the characterization of protein groups for which the site may be relevant to their biological roles, thereby allowing the deconvolution of complex biological circuits into functional information. In this regard, we performed subcellular fractionation of proteins from B. jararaca venom gland, focusing on nuclear proteins since this cellular compartment comprises key effectors that shape gene expression. Our results provided a snapshot of B. jararaca's subcellular venom gland proteome and pointed to a ‘conserved’ proteome core among different life stages (newborn and adult) and between sexes (adult male and female). Overall, the top 15 highly abundant proteins identified in B. jararaca venom glands mirrored the panel of highly expressed genes in human salivary glands. Therefore, the expression profile observed for such a protein set could be considered a conserved core signature of salivary gland secretory epithelium. Moreover, the newborn venom gland displayed a unique expression signature of transcription factors involved in regulating transcription and biosynthetic processes and may mirror biological constraints of the ontogenetic development of B. jararaca, contributing to venom proteome diversity.
KW - Bothrops jararaca
KW - Snake venom
KW - Subcellular proteome
KW - Venom gland
KW - Venom variability
UR - http://www.scopus.com/inward/record.url?scp=85162105675&partnerID=8YFLogxK
U2 - 10.1016/j.biochi.2023.06.005
DO - 10.1016/j.biochi.2023.06.005
M3 - Article
C2 - 37315762
AN - SCOPUS:85162105675
SN - 0300-9084
VL - 214
SP - 1
EP - 10
JO - Biochimie
JF - Biochimie
ER -