Molecular characterization and transcriptional analysis of the female-enriched chondroitin proteoglycan 2 of Toxocara canis. Issue 2 (24th April 2017)
- Record Type:
- Journal Article
- Title:
- Molecular characterization and transcriptional analysis of the female-enriched chondroitin proteoglycan 2 of Toxocara canis. Issue 2 (24th April 2017)
- Main Title:
- Molecular characterization and transcriptional analysis of the female-enriched chondroitin proteoglycan 2 of Toxocara canis
- Authors:
- Ma, G.X.
Zhou, R.Q.
Hu, L.
Luo, Y.L.
Luo, Y.F.
Zhu, H.H. - Abstract:
- Abstract: Toxocara canis is an important but neglected zoonotic parasite, and is the causative agent of human toxocariasis. Chondroitin proteoglycans are biological macromolecules, widely distributed in extracellular matrices, with a great diversity of functions in mammals. However, there is limited information regarding chondroitin proteoglycans in nematode parasites. In the present study, a female-enriched chondroitin proteoglycan 2 gene of T. canis ( Tc-cpg-2 ) was cloned and characterized. Quantitative real-time polymerase chain reaction (qRT-PCR) was employed to measure the transcription levels of Tc-cpg-2 among tissues of male and female adult worms. A 485-amino-acid (aa) polypeptide was predicted from a continuous 1458-nuleotide open reading frame and designated as Tc CPG2, which contains a 21-aa signal peptide. Conserved domain searching indicated three chitin-binding peritrophin-A (CBM_14) domains in the amino acid sequence of Tc CPG2. Multiple alignment with the inferred amino acid sequences of Caenorhabditis elegans and Ascaris suum showed that CBM_14 domains were well conserved among these species. Phylogenetic analysis suggested that Tc CPG2 was closely related to the sequence of chondroitin proteoglycan 2 of A. suum . Interestingly, a high level of Tc-cpg-2 was detected in female germline tissues, particularly in the oviduct, suggesting potential roles of this gene in reproduction (e.g. oogenesis and embryogenesis) of adult T. canis . The functional roles ofAbstract: Toxocara canis is an important but neglected zoonotic parasite, and is the causative agent of human toxocariasis. Chondroitin proteoglycans are biological macromolecules, widely distributed in extracellular matrices, with a great diversity of functions in mammals. However, there is limited information regarding chondroitin proteoglycans in nematode parasites. In the present study, a female-enriched chondroitin proteoglycan 2 gene of T. canis ( Tc-cpg-2 ) was cloned and characterized. Quantitative real-time polymerase chain reaction (qRT-PCR) was employed to measure the transcription levels of Tc-cpg-2 among tissues of male and female adult worms. A 485-amino-acid (aa) polypeptide was predicted from a continuous 1458-nuleotide open reading frame and designated as Tc CPG2, which contains a 21-aa signal peptide. Conserved domain searching indicated three chitin-binding peritrophin-A (CBM_14) domains in the amino acid sequence of Tc CPG2. Multiple alignment with the inferred amino acid sequences of Caenorhabditis elegans and Ascaris suum showed that CBM_14 domains were well conserved among these species. Phylogenetic analysis suggested that Tc CPG2 was closely related to the sequence of chondroitin proteoglycan 2 of A. suum . Interestingly, a high level of Tc-cpg-2 was detected in female germline tissues, particularly in the oviduct, suggesting potential roles of this gene in reproduction (e.g. oogenesis and embryogenesis) of adult T. canis . The functional roles of Tc-cpg-2 in reproduction and development in this parasite and related parasitic nematodes warrant further functional studies. … (more)
- Is Part Of:
- Journal of helminthology. Volume 92:Issue 2(2018)
- Journal:
- Journal of helminthology
- Issue:
- Volume 92:Issue 2(2018)
- Issue Display:
- Volume 92, Issue 2 (2018)
- Year:
- 2018
- Volume:
- 92
- Issue:
- 2
- Issue Sort Value:
- 2018-0092-0002-0000
- Page Start:
- 154
- Page End:
- 160
- Publication Date:
- 2017-04-24
- Subjects:
- Helminthology -- Periodicals
592.3 - Journal URLs:
- http://journals.cambridge.org/action/displayJournal?jid=JHL ↗
http://www.ingentaconnect.com/content/cabi/joh ↗ - DOI:
- 10.1017/S0022149X17000359 ↗
- Languages:
- English
- ISSNs:
- 0022-149X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library STI - ELD Digital store
- Ingest File:
- 9636.xml