Molecular cloning and functional characterization of a novel i‐type lysozyme in the freshwater mussel Cristaria plicata. (December 2015)
- Record Type:
- Journal Article
- Title:
- Molecular cloning and functional characterization of a novel i‐type lysozyme in the freshwater mussel Cristaria plicata. (December 2015)
- Main Title:
- Molecular cloning and functional characterization of a novel i‐type lysozyme in the freshwater mussel Cristaria plicata
- Authors:
- Dai, Wenjuan
Wu, Dan
Zhang, Ming
Wen, Chungen
Xie, Yanhai
Hu, Baoqing
Jian, Shaoqing
Zeng, Mingyu
Tao, Zhiying - Abstract:
- ABSTRACT: The freshwater bivalve Cristaria plicata, which is widely distributed in Eastern Asia, is a key species in the pearl culture industry. In this study, a novel invertebrate‐type lysozyme, designated as CpLYZ2, was cloned from hemocytes of C. plicata . This lysozyme shares high sequence identity and is homologous to a previously identified lysozyme CpLYZ1 isolated from C. plicata and with HcLyso3 isolated from Hyriopsis cumingii . The full‐length cDNA of CpLYZ2 is 913 bp long, which includes an open reading frame (ORF) of 486 bp, a 3′ untranslated region (UTR) of 389 bp and a 5′ UTR of 38 bp. The ORF encodes a putative polypeptide of 161 amino acids with a predicted molecular mass of 18.2 kDa and a theoretical isoelectric point of 6.56. CpLYZ2 mRNA transcripts can be detected in hemocytes, hepatopancreas, muscle, gills and mantle tissues, the greatest expression being observed in the gills. CpLYZ2 expression in hemocytes, hepatopancreas and gills increased significantly after the mussel was challenged with Aeromonas hydrophila . Furthermore, the optimal pH and temperature for enzyme activity of the recombinant CpLYZ2 were 5.5 and 50°C, respectively. The recombinant lysozyme protein exhibited bacteriolytic activity against Escherichia coli, A. hydrophila, Staphyloccocus aureus, Bacillus subtilis, Streptococcus sp. and Staphylococcus epidermidis . The findings of this study help to elucidate immune responses in molluscs and will thus expedite disease management of theseABSTRACT: The freshwater bivalve Cristaria plicata, which is widely distributed in Eastern Asia, is a key species in the pearl culture industry. In this study, a novel invertebrate‐type lysozyme, designated as CpLYZ2, was cloned from hemocytes of C. plicata . This lysozyme shares high sequence identity and is homologous to a previously identified lysozyme CpLYZ1 isolated from C. plicata and with HcLyso3 isolated from Hyriopsis cumingii . The full‐length cDNA of CpLYZ2 is 913 bp long, which includes an open reading frame (ORF) of 486 bp, a 3′ untranslated region (UTR) of 389 bp and a 5′ UTR of 38 bp. The ORF encodes a putative polypeptide of 161 amino acids with a predicted molecular mass of 18.2 kDa and a theoretical isoelectric point of 6.56. CpLYZ2 mRNA transcripts can be detected in hemocytes, hepatopancreas, muscle, gills and mantle tissues, the greatest expression being observed in the gills. CpLYZ2 expression in hemocytes, hepatopancreas and gills increased significantly after the mussel was challenged with Aeromonas hydrophila . Furthermore, the optimal pH and temperature for enzyme activity of the recombinant CpLYZ2 were 5.5 and 50°C, respectively. The recombinant lysozyme protein exhibited bacteriolytic activity against Escherichia coli, A. hydrophila, Staphyloccocus aureus, Bacillus subtilis, Streptococcus sp. and Staphylococcus epidermidis . The findings of this study help to elucidate immune responses in molluscs and will thus expedite disease management of these key freshwater species, in turn boosting pearl culture in eastern Asia. … (more)
- Is Part Of:
- Microbiology and immunology. Volume 59:Number 12(2015:Dec.)
- Journal:
- Microbiology and immunology
- Issue:
- Volume 59:Number 12(2015:Dec.)
- Issue Display:
- Volume 59, Issue 12 (2015)
- Year:
- 2015
- Volume:
- 59
- Issue:
- 12
- Issue Sort Value:
- 2015-0059-0012-0000
- Page Start:
- 744
- Page End:
- 755
- Publication Date:
- 2015-12
- Subjects:
- Cristaria plicata -- expression pattern -- lysozyme -- protein characterization
Microbiology -- Periodicals
Immunology -- Periodicals
Allergy and Immunology -- Periodicals
Microbiology -- Periodicals
Microbiologie -- Périodiques
Immunologie -- Périodiques
579 - Journal URLs:
- http://bibpurl.oclc.org/web/42307 ↗
http://bibpurl.oclc.org/web/7904 ↗
http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1348-0421 ↗
http://www.sanbi.co.jp/capj/ ↗
http://www3.interscience.wiley.com/journal/118902525/home ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/1348-0421.12341 ↗
- Languages:
- English
- ISSNs:
- 0385-5600
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 5757.791000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 2070.xml