Expression and antimicrobial activity of c-type lysozyme in taimen (Hucho taimen, Pallas). (October 2016)
- Record Type:
- Journal Article
- Title:
- Expression and antimicrobial activity of c-type lysozyme in taimen (Hucho taimen, Pallas). (October 2016)
- Main Title:
- Expression and antimicrobial activity of c-type lysozyme in taimen (Hucho taimen, Pallas)
- Authors:
- Li, Shaowu
Wang, Di
Liu, Hongbai
Yin, Jiasheng
Lu, Tongyan - Abstract:
- Abstract: Lysozymes are important defense proteins of the innate immune system and possess high antibacterial activities. In the present study, a full-length c-type lysozyme cDNA (HtLysC) was cloned and characterized from taimen ( Hucho taimen, Pallas). The cDNA contains an open reading frame (ORF) of 432 bp encoding 143 amino acid (aa), with 97% identity to LysC of Rainbow trout ( Oncorhynchus mykiss ). The amino acid sequence possessed a LYZ1 domain (16–140 aa) which contained two conserved residues (Glu 50 and Asp 67), eight conserved cysteine residues and a calcium binding site. RT-PCR analysis showed that HtLysC transcripts were most abundant in liver and less in muscle. The expression of HtLysC was up-regulated in the liver when challenged with Yersinia ruckeri . The recombinant HtLysC (rHtLysC) had lytic activities against Micrococcus lysodeikticus, Aeromonas salmonicida and Y. ruckeri . Enzyme assay showed that the optimal temperature and pH of rHtLysC were 55 °C and 6.0, respectively. Taken together, these results indicated that HtLysC might play an important role in innate immune defense against bacterial pathogens as a functional lysozyme. Highlights: A c-type lysozyme (HtLysC) from Hucho taimen was cloned and characterized. HtLysC contains a typical c-type lysozyme domain. HtLysC is constitutively expressed in the liver, intestine, blood, spleen, kidney and gill. Expression of HtLysC in the liver was up-regulated after challenged with Yersinia ruckeri . rHtLysCAbstract: Lysozymes are important defense proteins of the innate immune system and possess high antibacterial activities. In the present study, a full-length c-type lysozyme cDNA (HtLysC) was cloned and characterized from taimen ( Hucho taimen, Pallas). The cDNA contains an open reading frame (ORF) of 432 bp encoding 143 amino acid (aa), with 97% identity to LysC of Rainbow trout ( Oncorhynchus mykiss ). The amino acid sequence possessed a LYZ1 domain (16–140 aa) which contained two conserved residues (Glu 50 and Asp 67), eight conserved cysteine residues and a calcium binding site. RT-PCR analysis showed that HtLysC transcripts were most abundant in liver and less in muscle. The expression of HtLysC was up-regulated in the liver when challenged with Yersinia ruckeri . The recombinant HtLysC (rHtLysC) had lytic activities against Micrococcus lysodeikticus, Aeromonas salmonicida and Y. ruckeri . Enzyme assay showed that the optimal temperature and pH of rHtLysC were 55 °C and 6.0, respectively. Taken together, these results indicated that HtLysC might play an important role in innate immune defense against bacterial pathogens as a functional lysozyme. Highlights: A c-type lysozyme (HtLysC) from Hucho taimen was cloned and characterized. HtLysC contains a typical c-type lysozyme domain. HtLysC is constitutively expressed in the liver, intestine, blood, spleen, kidney and gill. Expression of HtLysC in the liver was up-regulated after challenged with Yersinia ruckeri . rHtLysC had lytic activities against several bacterial pathogens, including gram-positive and gram-negative bacteria. … (more)
- Is Part Of:
- Developmental and comparative immunology. Volume 63(2016)
- Journal:
- Developmental and comparative immunology
- Issue:
- Volume 63(2016)
- Issue Display:
- Volume 63, Issue 2016 (2016)
- Year:
- 2016
- Volume:
- 63
- Issue:
- 2016
- Issue Sort Value:
- 2016-0063-2016-0000
- Page Start:
- 156
- Page End:
- 162
- Publication Date:
- 2016-10
- Subjects:
- Hucho taimen -- C-type lysozyme -- Expression -- Antimicrobial activity
Immunology -- Periodicals
Developmental immunology -- Periodicals
616.079 - Journal URLs:
- http://www.sciencedirect.com/science/journal/0145305X ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.dci.2016.06.003 ↗
- Languages:
- English
- ISSNs:
- 0145-305X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3579.051000
British Library DSC - BLDSS-3PM
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- 1043.xml