First proteome of the egg perivitelline fluid of a freshwater gastropod with aerial oviposition

Handle URI:
http://hdl.handle.net/10754/562271
Title:
First proteome of the egg perivitelline fluid of a freshwater gastropod with aerial oviposition
Authors:
Sun, Jin; Zhang, Huoming ( 0000-0001-5416-0358 ) ; Wang, Hao; Heras, Horacio; Dreon, Marcos Sebastián; Ituarte, Santiago; Ravasi, Timothy ( 0000-0002-9950-465X ) ; Qian, Peiyuan; Qiu, Jianwen
Abstract:
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.
KAUST Department:
Biosciences Core Lab; Biological and Environmental Sciences and Engineering (BESE) Division; Bioscience Program; Computational Bioscience Research Center (CBRC); Integrative Systems Biology Lab
Publisher:
American Chemical Society (ACS)
Journal:
Journal of Proteome Research
Issue Date:
3-Aug-2012
DOI:
10.1021/pr3003613
PubMed ID:
22738194
Type:
Article
ISSN:
15353893
Sponsors:
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.
Appears in Collections:
Articles; Bioscience Program; Biosciences Core Lab; Computational Bioscience Research Center (CBRC); Biological and Environmental Sciences and Engineering (BESE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorSun, Jinen
dc.contributor.authorZhang, Huomingen
dc.contributor.authorWang, Haoen
dc.contributor.authorHeras, Horacioen
dc.contributor.authorDreon, Marcos Sebastiánen
dc.contributor.authorItuarte, Santiagoen
dc.contributor.authorRavasi, Timothyen
dc.contributor.authorQian, Peiyuanen
dc.contributor.authorQiu, Jianwenen
dc.date.accessioned2015-08-03T09:58:52Zen
dc.date.available2015-08-03T09:58:52Zen
dc.date.issued2012-08-03en
dc.identifier.issn15353893en
dc.identifier.pmid22738194en
dc.identifier.doi10.1021/pr3003613en
dc.identifier.urihttp://hdl.handle.net/10754/562271en
dc.description.abstractPomacea 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.en
dc.description.sponsorshipH.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.en
dc.publisherAmerican Chemical Society (ACS)en
dc.subjectapple snailen
dc.subjectnovel proteinen
dc.subjectperivitelline fluiden
dc.subjectPomacea canaliculataen
dc.subjectproteomicsen
dc.titleFirst proteome of the egg perivitelline fluid of a freshwater gastropod with aerial ovipositionen
dc.typeArticleen
dc.contributor.departmentBiosciences Core Laben
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Divisionen
dc.contributor.departmentBioscience Programen
dc.contributor.departmentComputational Bioscience Research Center (CBRC)en
dc.contributor.departmentIntegrative Systems Biology Laben
dc.identifier.journalJournal of Proteome Researchen
dc.contributor.institutionDepartment of Biology, Hong Kong Baptist University, Hong Kong, Hong Kongen
dc.contributor.institutionDivision of Life Science, Hong Kong University of Science and Technology, Hong Kong, Hong Kongen
dc.contributor.institutionInstituto de Investigaciones Bioquímicas de la Plata (INIBIOLP), CONICET CCT la Plata - Universidad Nacional de la Plata (UNLP), 60 y 120, (1900) La Plata, Argentinaen
kaust.authorZhang, Huomingen
kaust.authorRavasi, Timothyen

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