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...

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Autores principales:	Daniela P Almenara, Joselene P de Moura, Cristiane P Scarabotto, Russolina B Zingali, Carlos E Winter
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/91996723914b4b4e80e1b8525af94b7e
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spelling	oai:doaj.org-article:91996723914b4b4e80e1b8525af94b7e2021-11-18T08:02:29ZThe molecular and structural characterization of two vitellogenins from the free-living nematode Oscheius tipulae.1932-620310.1371/journal.pone.0053460https://doaj.org/article/91996723914b4b4e80e1b8525af94b7e2013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23308227/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203This 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.Daniela P AlmenaraJoselene P de MouraCristiane P ScarabottoRussolina B ZingaliCarlos E WinterPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 1, p e53460 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Daniela P Almenara Joselene P de Moura Cristiane P Scarabotto Russolina B Zingali Carlos E Winter The molecular and structural characterization of two vitellogenins from the free-living nematode Oscheius tipulae.
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.
format	article
author	Daniela P Almenara Joselene P de Moura Cristiane P Scarabotto Russolina B Zingali Carlos E Winter
author_facet	Daniela P Almenara Joselene P de Moura Cristiane P Scarabotto Russolina B Zingali Carlos E Winter
author_sort	Daniela P Almenara
title	The molecular and structural characterization of two vitellogenins from the free-living nematode Oscheius tipulae.
title_short	The molecular and structural characterization of two vitellogenins from the free-living nematode Oscheius tipulae.
title_full	The molecular and structural characterization of two vitellogenins from the free-living nematode Oscheius tipulae.
title_fullStr	The molecular and structural characterization of two vitellogenins from the free-living nematode Oscheius tipulae.
title_full_unstemmed	The molecular and structural characterization of two vitellogenins from the free-living nematode Oscheius tipulae.
title_sort	molecular and structural characterization of two vitellogenins from the free-living nematode oscheius tipulae.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/91996723914b4b4e80e1b8525af94b7e
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The molecular and structural characterization of two vitellogenins from the free-living nematode Oscheius tipulae.

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