TY - JOUR
T1 - First proteome of the egg perivitelline fluid of a freshwater gastropod with aerial oviposition
AU - Sun, Jin
AU - Zhang, Huoming
AU - Wang, Hao
AU - Heras, Horacio
AU - Dreon, Marcos Sebastián
AU - Ituarte, Santiago
AU - Ravasi, Timothy
AU - Qian, Pei-Yuan
AU - Qiu, Jian-Wen
N1 - KAUST Repository Item: Exported on 2020-10-01
Acknowledgements: H.H. and S.I. are members of Carrera del Investigador CONICET, Argentina. M.S.D. is a member of Carrera del Investigador CICBA, Argentina. This study was supported by a HKBU postgraduate scholarship to J.S. and a grant (HKBU FRG2/10-11/009) to J.W.Q.
PY - 2012/7/13
Y1 - 2012/7/13
N2 - Pomacea canaliculata is a freshwater snail that deposits eggs on solid substrates above the water surface. Previous studies have emphasized the nutritional and protective functions of the three most abundant perivitelline fluid (PVF) protein complexes (ovorubin, PV2, and PV3) during its embryonic development, but little is known about the structure and function of other less abundant proteins. Using 2-DE, SDS-PAGE, MALDI TOF/TOF, and LC-MS/MS, we identified 59 proteins from the PVF of P. canaliculata, among which 19 are novel. KEGG analysis showed that the functions of the majority of these proteins are "unknown" (n = 34), "environmental information processing" (10), 9 of which are related to innate immunity, and "metabolism" (7). Suppressive subtractive hybridization revealed 21 PVF genes to be specific to the albumen gland, indicating this organ is the origin of many of the PVF proteins. Further, the 3 ovorubin subunits were identified with 30.2-35.0% identity among them, indicating their common origin but ancient duplications. Characterization of the PVF proteome has opened the gate for further studies aiming to understand the evolution of the novel proteins and their contribution to the switch to aerial oviposition. © 2012 American Chemical Society.
AB - Pomacea canaliculata is a freshwater snail that deposits eggs on solid substrates above the water surface. Previous studies have emphasized the nutritional and protective functions of the three most abundant perivitelline fluid (PVF) protein complexes (ovorubin, PV2, and PV3) during its embryonic development, but little is known about the structure and function of other less abundant proteins. Using 2-DE, SDS-PAGE, MALDI TOF/TOF, and LC-MS/MS, we identified 59 proteins from the PVF of P. canaliculata, among which 19 are novel. KEGG analysis showed that the functions of the majority of these proteins are "unknown" (n = 34), "environmental information processing" (10), 9 of which are related to innate immunity, and "metabolism" (7). Suppressive subtractive hybridization revealed 21 PVF genes to be specific to the albumen gland, indicating this organ is the origin of many of the PVF proteins. Further, the 3 ovorubin subunits were identified with 30.2-35.0% identity among them, indicating their common origin but ancient duplications. Characterization of the PVF proteome has opened the gate for further studies aiming to understand the evolution of the novel proteins and their contribution to the switch to aerial oviposition. © 2012 American Chemical Society.
UR - http://hdl.handle.net/10754/562271
UR - https://pubs.acs.org/doi/10.1021/pr3003613
UR - http://www.scopus.com/inward/record.url?scp=84864614809&partnerID=8YFLogxK
U2 - 10.1021/pr3003613
DO - 10.1021/pr3003613
M3 - Article
C2 - 22738194
SN - 1535-3893
VL - 11
SP - 4240
EP - 4248
JO - Journal of Proteome Research
JF - Journal of Proteome Research
IS - 8
ER -