First Proteome of the Egg Perivitelline Fluid of a Freshwater Gastropod with Aerial Oviposition

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 de...

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Bibliographic Details
Published in:Journal of proteome research 2012-08, Vol.11 (8), p.4240-4248
Main Authors: Sun, Jin, Zhang, Huoming, Wang, Hao, Heras, Horacio, Dreon, Marcos S, Ituarte, Santiago, Ravasi, Timothy, Qian, Pei-Yuan, Qiu, Jian-Wen
Format: Article
Language:English
Subjects:
Amino Acid Motifs
Animals
Apocrine Glands - metabolism
Bayes Theorem
Conserved Sequence
Egg Proteins - chemistry
Egg Proteins - genetics
Egg Proteins - metabolism
Female
Gene Expression
Likelihood Functions
Molecular Sequence Data
Oviposition
Ovum - metabolism
Phylogeny
Protein Subunits - genetics
Protein Subunits - metabolism
Proteome - chemistry
Proteome - genetics
Proteome - metabolism
Sequence Analysis, DNA
Snails - cytology
Snails - genetics
Snails - metabolism
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Summary: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.
ISSN:1535-3893
1535-3907
DOI:10.1021/pr3003613