The molecular and structural characterization of two vitellogenins from the free-living nematode Oscheius tipulae
This paper describes the purification of yolk proteins, which are important for the reproduction of egg-laying animals, and the structural characterization of two vitellogenins, VT1 and OTI-VIT-6, of the nematode Oscheius tipulae. O. tipulae is an alternative model organism to its relative, the wide...
Gespeichert in:
| Veröffentlicht in: | PloS one 2013-01, Vol.8 (1), p.e53460-e53460 |
|---|---|
| Hauptverfasser: | , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | e53460 |
|---|---|
| container_issue | 1 |
| container_start_page | e53460 |
| container_title | PloS one |
| container_volume | 8 |
| creator | Almenara, Daniela P de Moura, Joselene P Scarabotto, Cristiane P Zingali, Russolina B Winter, Carlos E |
| description | This paper describes the purification of yolk proteins, which are important for the reproduction of egg-laying animals, and the structural characterization of two vitellogenins, VT1 and OTI-VIT-6, of the nematode Oscheius tipulae. O. tipulae is an alternative model organism to its relative, the widely used Caenorhabditis elegans, and is a good model to understand reproduction in insect parasitic nematodes of the genus Heterorhabditis. The native purified O. tipulae vitellogenin is composed of three polypeptides (VT1, VT2 and VT3), whereas in C. elegans, vitellogenin is composed of four polypeptides. The gene (Oti-vit-1) encoding yolk polypeptide VT1 has been recently identified in the genome of O. tipulae. Immunoblotting and N-terminal sequencing confirmed that VT1 is indeed coded by Oti-vit-1. Utilizing the same experimental approaches, we showed that the polypeptides VT2 and VT3 are derived from the proteolytic processing of the C- and N-terminal portions of the precursor OTI-VIT-6, respectively. We also showed that the recombinant polypeptide (P40), corresponding to the N-terminal sequence of OTI-VIT-6, preferentially interacts with a 100-kDa polypeptide found in adult worm extracts, as we have previously shown for the native vitellins of O. tipulae. Using the putative nematode vitellogenin amino acid sequences available in the UniProtKB database, we constructed a phylogenetic tree and showed that the O. tipulae vitellogenins characterized in this study are orthologous to those of the Caenorhabditis spp. Together, these results represent the first structural and functional comparative study of nematode yolk proteins outside the Caenorhabditis genus and provide insight into the evolution of these lipoproteins within the Nematode Phylum. |
| doi_str_mv | 10.1371/journal.pone.0053460 |
| format | Article |
| fullrecord | <record><control><sourceid>gale_plos_</sourceid><recordid>TN_cdi_plos_journals_1289070159</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A478401150</galeid><doaj_id>oai_doaj_org_article_91996723914b4b4e80e1b8525af94b7e</doaj_id><sourcerecordid>A478401150</sourcerecordid><originalsourceid>FETCH-LOGICAL-c692t-e77b54a7481ce9c3c4fda05e94b05a4511ecb8e73971d2999f44cf918cb015dd3</originalsourceid><addsrcrecordid>eNqNk12L1DAUhoso7jr6D0QDgujFjEmTTpsbYVn8GFgY0NXbkKanbYY2mU3S8ePXmzrdZSp7IblIOHnOe5I3OUnynOAVoTl5t7ODM7Jb7a2BFcYZZWv8IDknnKbLdYrpw5P1WfLE-90IFev14-QspRQXaZqfJzfXLaDedqCGTjokTYV8cIMKg5MdUq10UgVw-rcM2hpkaxR-WHTQAbrONmC08ah2tkch6tQOYNnpgzYNMtDLYCtAW69a0INHQe9jDXiaPKpl5-HZNC-Sbx8_XF9-Xl5tP20uL66Was3TsIQ8LzMmc1YQBVxRxepK4gw4K3EmWUYIqLKAnPKcVCnnvGZM1ZwUqsQkqyq6SF4edfed9WJyywuSFhznEeGR2ByJysqd2DvdS_dLWKnF34B1jZAuaNWB4ITzdZ5STlgZBxQYSFlkaSbreKAcotb7qdpQ9lApMCEaOBOd7xjdisYeBI1vkrE0CryZBJy9GcAH0WuvosvSgB3Gc-eUMUzjtEhe_YPef7uJamS8gDa1jXXVKCouWF4wTEiGI7W6h4qjgl6r-LVqHeOzhLezhMgE-BkaOXgvNl-__D-7_T5nX5-wLcgutN52w_jt_BxkR1A5672D-s5kgsXYGbduiLEzxNQZMe3F6QPdJd22Av0DgCIJzg</addsrcrecordid><sourcetype>Open Website</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1289070159</pqid></control><display><type>article</type><title>The molecular and structural characterization of two vitellogenins from the free-living nematode Oscheius tipulae</title><source>MEDLINE</source><source>DOAJ Directory of Open Access Journals</source><source>Public Library of Science (PLoS)</source><source>EZB-FREE-00999 freely available EZB journals</source><source>PubMed Central</source><source>Free Full-Text Journals in Chemistry</source><creator>Almenara, Daniela P ; de Moura, Joselene P ; Scarabotto, Cristiane P ; Zingali, Russolina B ; Winter, Carlos E</creator><contributor>Ruvinsky, Ilya</contributor><creatorcontrib>Almenara, Daniela P ; de Moura, Joselene P ; Scarabotto, Cristiane P ; Zingali, Russolina B ; Winter, Carlos E ; Ruvinsky, Ilya</creatorcontrib><description>This paper describes the purification of yolk proteins, which are important for the reproduction of egg-laying animals, and the structural characterization of two vitellogenins, VT1 and OTI-VIT-6, of the nematode Oscheius tipulae. O. tipulae is an alternative model organism to its relative, the widely used Caenorhabditis elegans, and is a good model to understand reproduction in insect parasitic nematodes of the genus Heterorhabditis. The native purified O. tipulae vitellogenin is composed of three polypeptides (VT1, VT2 and VT3), whereas in C. elegans, vitellogenin is composed of four polypeptides. The gene (Oti-vit-1) encoding yolk polypeptide VT1 has been recently identified in the genome of O. tipulae. Immunoblotting and N-terminal sequencing confirmed that VT1 is indeed coded by Oti-vit-1. Utilizing the same experimental approaches, we showed that the polypeptides VT2 and VT3 are derived from the proteolytic processing of the C- and N-terminal portions of the precursor OTI-VIT-6, respectively. We also showed that the recombinant polypeptide (P40), corresponding to the N-terminal sequence of OTI-VIT-6, preferentially interacts with a 100-kDa polypeptide found in adult worm extracts, as we have previously shown for the native vitellins of O. tipulae. Using the putative nematode vitellogenin amino acid sequences available in the UniProtKB database, we constructed a phylogenetic tree and showed that the O. tipulae vitellogenins characterized in this study are orthologous to those of the Caenorhabditis spp. Together, these results represent the first structural and functional comparative study of nematode yolk proteins outside the Caenorhabditis genus and provide insight into the evolution of these lipoproteins within the Nematode Phylum.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0053460</identifier><identifier>PMID: 23308227</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Amino Acid Sequence ; Amino acids ; Animals ; Apolipoproteins ; Biochemistry ; Biology ; Caenorhabditis - genetics ; Caenorhabditis elegans ; Comparative studies ; Egg laying ; Eggs ; Embryos ; Escherichia coli - genetics ; Female ; Gene Expression ; Gene sequencing ; Genes ; Genomes ; Genomics ; Immunoblotting ; Insects ; Laboratories ; Ligands ; Lipids ; Lipoproteins ; Molecular Sequence Data ; Nematodes ; Ovum - chemistry ; Parasitology ; Peptides - chemistry ; Peptides - genetics ; Phylogeny ; Polypeptides ; Protein purification ; Protein Structure, Tertiary ; Proteins ; Proteolysis ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Reproduction ; Rhabditoidea - genetics ; Roundworms ; Sequence Homology, Amino Acid ; Structural analysis ; Structure-function relationships ; Vitellogenin ; Vitellogenins - chemistry ; Vitellogenins - classification ; Vitellogenins - genetics ; Worms ; Yolk</subject><ispartof>PloS one, 2013-01, Vol.8 (1), p.e53460-e53460</ispartof><rights>COPYRIGHT 2013 Public Library of Science</rights><rights>2013 Almenara et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2013 Almenara et al 2013 Almenara et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c692t-e77b54a7481ce9c3c4fda05e94b05a4511ecb8e73971d2999f44cf918cb015dd3</citedby><cites>FETCH-LOGICAL-c692t-e77b54a7481ce9c3c4fda05e94b05a4511ecb8e73971d2999f44cf918cb015dd3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3538542/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3538542/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2100,2926,23864,27922,27923,53789,53791,79370,79371</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23308227$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Ruvinsky, Ilya</contributor><creatorcontrib>Almenara, Daniela P</creatorcontrib><creatorcontrib>de Moura, Joselene P</creatorcontrib><creatorcontrib>Scarabotto, Cristiane P</creatorcontrib><creatorcontrib>Zingali, Russolina B</creatorcontrib><creatorcontrib>Winter, Carlos E</creatorcontrib><title>The molecular and structural characterization of two vitellogenins from the free-living nematode Oscheius tipulae</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>This paper describes the purification of yolk proteins, which are important for the reproduction of egg-laying animals, and the structural characterization of two vitellogenins, VT1 and OTI-VIT-6, of the nematode Oscheius tipulae. O. tipulae is an alternative model organism to its relative, the widely used Caenorhabditis elegans, and is a good model to understand reproduction in insect parasitic nematodes of the genus Heterorhabditis. The native purified O. tipulae vitellogenin is composed of three polypeptides (VT1, VT2 and VT3), whereas in C. elegans, vitellogenin is composed of four polypeptides. The gene (Oti-vit-1) encoding yolk polypeptide VT1 has been recently identified in the genome of O. tipulae. Immunoblotting and N-terminal sequencing confirmed that VT1 is indeed coded by Oti-vit-1. Utilizing the same experimental approaches, we showed that the polypeptides VT2 and VT3 are derived from the proteolytic processing of the C- and N-terminal portions of the precursor OTI-VIT-6, respectively. We also showed that the recombinant polypeptide (P40), corresponding to the N-terminal sequence of OTI-VIT-6, preferentially interacts with a 100-kDa polypeptide found in adult worm extracts, as we have previously shown for the native vitellins of O. tipulae. Using the putative nematode vitellogenin amino acid sequences available in the UniProtKB database, we constructed a phylogenetic tree and showed that the O. tipulae vitellogenins characterized in this study are orthologous to those of the Caenorhabditis spp. Together, these results represent the first structural and functional comparative study of nematode yolk proteins outside the Caenorhabditis genus and provide insight into the evolution of these lipoproteins within the Nematode Phylum.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Apolipoproteins</subject><subject>Biochemistry</subject><subject>Biology</subject><subject>Caenorhabditis - genetics</subject><subject>Caenorhabditis elegans</subject><subject>Comparative studies</subject><subject>Egg laying</subject><subject>Eggs</subject><subject>Embryos</subject><subject>Escherichia coli - genetics</subject><subject>Female</subject><subject>Gene Expression</subject><subject>Gene sequencing</subject><subject>Genes</subject><subject>Genomes</subject><subject>Genomics</subject><subject>Immunoblotting</subject><subject>Insects</subject><subject>Laboratories</subject><subject>Ligands</subject><subject>Lipids</subject><subject>Lipoproteins</subject><subject>Molecular Sequence Data</subject><subject>Nematodes</subject><subject>Ovum - chemistry</subject><subject>Parasitology</subject><subject>Peptides - chemistry</subject><subject>Peptides - genetics</subject><subject>Phylogeny</subject><subject>Polypeptides</subject><subject>Protein purification</subject><subject>Protein Structure, Tertiary</subject><subject>Proteins</subject><subject>Proteolysis</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Reproduction</subject><subject>Rhabditoidea - genetics</subject><subject>Roundworms</subject><subject>Sequence Homology, Amino Acid</subject><subject>Structural analysis</subject><subject>Structure-function relationships</subject><subject>Vitellogenin</subject><subject>Vitellogenins - chemistry</subject><subject>Vitellogenins - classification</subject><subject>Vitellogenins - genetics</subject><subject>Worms</subject><subject>Yolk</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>DOA</sourceid><recordid>eNqNk12L1DAUhoso7jr6D0QDgujFjEmTTpsbYVn8GFgY0NXbkKanbYY2mU3S8ePXmzrdZSp7IblIOHnOe5I3OUnynOAVoTl5t7ODM7Jb7a2BFcYZZWv8IDknnKbLdYrpw5P1WfLE-90IFev14-QspRQXaZqfJzfXLaDedqCGTjokTYV8cIMKg5MdUq10UgVw-rcM2hpkaxR-WHTQAbrONmC08ah2tkch6tQOYNnpgzYNMtDLYCtAW69a0INHQe9jDXiaPKpl5-HZNC-Sbx8_XF9-Xl5tP20uL66Was3TsIQ8LzMmc1YQBVxRxepK4gw4K3EmWUYIqLKAnPKcVCnnvGZM1ZwUqsQkqyq6SF4edfed9WJyywuSFhznEeGR2ByJysqd2DvdS_dLWKnF34B1jZAuaNWB4ITzdZ5STlgZBxQYSFlkaSbreKAcotb7qdpQ9lApMCEaOBOd7xjdisYeBI1vkrE0CryZBJy9GcAH0WuvosvSgB3Gc-eUMUzjtEhe_YPef7uJamS8gDa1jXXVKCouWF4wTEiGI7W6h4qjgl6r-LVqHeOzhLezhMgE-BkaOXgvNl-__D-7_T5nX5-wLcgutN52w_jt_BxkR1A5672D-s5kgsXYGbduiLEzxNQZMe3F6QPdJd22Av0DgCIJzg</recordid><startdate>20130107</startdate><enddate>20130107</enddate><creator>Almenara, Daniela P</creator><creator>de Moura, Joselene P</creator><creator>Scarabotto, Cristiane P</creator><creator>Zingali, Russolina B</creator><creator>Winter, Carlos E</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>IOV</scope><scope>ISR</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20130107</creationdate><title>The molecular and structural characterization of two vitellogenins from the free-living nematode Oscheius tipulae</title><author>Almenara, Daniela P ; de Moura, Joselene P ; Scarabotto, Cristiane P ; Zingali, Russolina B ; Winter, Carlos E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c692t-e77b54a7481ce9c3c4fda05e94b05a4511ecb8e73971d2999f44cf918cb015dd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Animals</topic><topic>Apolipoproteins</topic><topic>Biochemistry</topic><topic>Biology</topic><topic>Caenorhabditis - genetics</topic><topic>Caenorhabditis elegans</topic><topic>Comparative studies</topic><topic>Egg laying</topic><topic>Eggs</topic><topic>Embryos</topic><topic>Escherichia coli - genetics</topic><topic>Female</topic><topic>Gene Expression</topic><topic>Gene sequencing</topic><topic>Genes</topic><topic>Genomes</topic><topic>Genomics</topic><topic>Immunoblotting</topic><topic>Insects</topic><topic>Laboratories</topic><topic>Ligands</topic><topic>Lipids</topic><topic>Lipoproteins</topic><topic>Molecular Sequence Data</topic><topic>Nematodes</topic><topic>Ovum - chemistry</topic><topic>Parasitology</topic><topic>Peptides - chemistry</topic><topic>Peptides - genetics</topic><topic>Phylogeny</topic><topic>Polypeptides</topic><topic>Protein purification</topic><topic>Protein Structure, Tertiary</topic><topic>Proteins</topic><topic>Proteolysis</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - genetics</topic><topic>Reproduction</topic><topic>Rhabditoidea - genetics</topic><topic>Roundworms</topic><topic>Sequence Homology, Amino Acid</topic><topic>Structural analysis</topic><topic>Structure-function relationships</topic><topic>Vitellogenin</topic><topic>Vitellogenins - chemistry</topic><topic>Vitellogenins - classification</topic><topic>Vitellogenins - genetics</topic><topic>Worms</topic><topic>Yolk</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Almenara, Daniela P</creatorcontrib><creatorcontrib>de Moura, Joselene P</creatorcontrib><creatorcontrib>Scarabotto, Cristiane P</creatorcontrib><creatorcontrib>Zingali, Russolina B</creatorcontrib><creatorcontrib>Winter, Carlos E</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Opposing Viewpoints</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Nursing & Allied Health Database</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Meteorological & Geoastrophysical Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>Meteorological & Geoastrophysical Abstracts - Academic</collection><collection>ProQuest Engineering Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Engineering Database</collection><collection>Nursing & Allied Health Premium</collection><collection>Advanced Technologies & Aerospace Database</collection><collection>ProQuest Advanced Technologies & Aerospace Collection</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environmental Science Database</collection><collection>Materials Science Collection</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>Engineering Collection</collection><collection>Environmental Science Collection</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Almenara, Daniela P</au><au>de Moura, Joselene P</au><au>Scarabotto, Cristiane P</au><au>Zingali, Russolina B</au><au>Winter, Carlos E</au><au>Ruvinsky, Ilya</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The molecular and structural characterization of two vitellogenins from the free-living nematode Oscheius tipulae</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2013-01-07</date><risdate>2013</risdate><volume>8</volume><issue>1</issue><spage>e53460</spage><epage>e53460</epage><pages>e53460-e53460</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>This paper describes the purification of yolk proteins, which are important for the reproduction of egg-laying animals, and the structural characterization of two vitellogenins, VT1 and OTI-VIT-6, of the nematode Oscheius tipulae. O. tipulae is an alternative model organism to its relative, the widely used Caenorhabditis elegans, and is a good model to understand reproduction in insect parasitic nematodes of the genus Heterorhabditis. The native purified O. tipulae vitellogenin is composed of three polypeptides (VT1, VT2 and VT3), whereas in C. elegans, vitellogenin is composed of four polypeptides. The gene (Oti-vit-1) encoding yolk polypeptide VT1 has been recently identified in the genome of O. tipulae. Immunoblotting and N-terminal sequencing confirmed that VT1 is indeed coded by Oti-vit-1. Utilizing the same experimental approaches, we showed that the polypeptides VT2 and VT3 are derived from the proteolytic processing of the C- and N-terminal portions of the precursor OTI-VIT-6, respectively. We also showed that the recombinant polypeptide (P40), corresponding to the N-terminal sequence of OTI-VIT-6, preferentially interacts with a 100-kDa polypeptide found in adult worm extracts, as we have previously shown for the native vitellins of O. tipulae. Using the putative nematode vitellogenin amino acid sequences available in the UniProtKB database, we constructed a phylogenetic tree and showed that the O. tipulae vitellogenins characterized in this study are orthologous to those of the Caenorhabditis spp. Together, these results represent the first structural and functional comparative study of nematode yolk proteins outside the Caenorhabditis genus and provide insight into the evolution of these lipoproteins within the Nematode Phylum.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>23308227</pmid><doi>10.1371/journal.pone.0053460</doi><tpages>e53460</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1932-6203 |
| ispartof | PloS one, 2013-01, Vol.8 (1), p.e53460-e53460 |
| issn | 1932-6203 1932-6203 |
| language | eng |
| recordid | cdi_plos_journals_1289070159 |
| source | MEDLINE; DOAJ Directory of Open Access Journals; Public Library of Science (PLoS); EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Sequence Amino acids Animals Apolipoproteins Biochemistry Biology Caenorhabditis - genetics Caenorhabditis elegans Comparative studies Egg laying Eggs Embryos Escherichia coli - genetics Female Gene Expression Gene sequencing Genes Genomes Genomics Immunoblotting Insects Laboratories Ligands Lipids Lipoproteins Molecular Sequence Data Nematodes Ovum - chemistry Parasitology Peptides - chemistry Peptides - genetics Phylogeny Polypeptides Protein purification Protein Structure, Tertiary Proteins Proteolysis Recombinant Proteins - chemistry Recombinant Proteins - genetics Reproduction Rhabditoidea - genetics Roundworms Sequence Homology, Amino Acid Structural analysis Structure-function relationships Vitellogenin Vitellogenins - chemistry Vitellogenins - classification Vitellogenins - genetics Worms Yolk |
| title | The molecular and structural characterization of two vitellogenins from the free-living nematode Oscheius tipulae |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-14T01%3A41%3A34IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_plos_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20molecular%20and%20structural%20characterization%20of%20two%20vitellogenins%20from%20the%20free-living%20nematode%20Oscheius%20tipulae&rft.jtitle=PloS%20one&rft.au=Almenara,%20Daniela%20P&rft.date=2013-01-07&rft.volume=8&rft.issue=1&rft.spage=e53460&rft.epage=e53460&rft.pages=e53460-e53460&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0053460&rft_dat=%3Cgale_plos_%3EA478401150%3C/gale_plos_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1289070159&rft_id=info:pmid/23308227&rft_galeid=A478401150&rft_doaj_id=oai_doaj_org_article_91996723914b4b4e80e1b8525af94b7e&rfr_iscdi=true |