A C1q domain containing protein from Crassostrea gigas serves as pattern recognition receptor and opsonin with high binding affinity to LPS. Issue 2 (August 2015)
- Record Type:
- Journal Article
- Title:
- A C1q domain containing protein from Crassostrea gigas serves as pattern recognition receptor and opsonin with high binding affinity to LPS. Issue 2 (August 2015)
- Main Title:
- A C1q domain containing protein from Crassostrea gigas serves as pattern recognition receptor and opsonin with high binding affinity to LPS
- Authors:
- Jiang, Shuai
Li, Hui
Zhang, Daoxiang
Zhang, Huan
Wang, Lingling
Sun, Jinsheng
Song, Linsheng - Abstract:
- <abstract xml:lang="en" abstract-type="author" id="abs0010"> <title id="sectitle0010">Abstract</title> <sec> <p id="abspara0010">C1q proteins serve as pattern recognition receptors and involve in the pathogen recognition and complement pathway activation. In the present study, a novel C1q domain containing protein from <italic>Crassostrea gigas</italic> (designated CgC1qDC-1) was isolated by liposaccharide-Sepharose 6B affinity chromatography. The coding sequence of CgC1qDC-1 gene was determined by performing a homologous search of eight tryptic peptides identified by MALDI-TOF/TOF-MS against the genome of <italic>C. gigas</italic>. The coding sequence of CgC1qDC-1 was of 387 bp encoding a polypeptide of 128 amino acids containing a typical globular C1q domain. The globular C1q domain possessed eight β strands with a jelly-roll topology structure, which was similar to the structure of human gC1q domain. The mRNA transcripts of CgC1qDC-1 were dominantly expressed in mantle and hemocytes, while low expressed in hepatopancreas, gonad, gill and muscle. The expression level of CgC1qDC-1 increased drastically at 6 h after <italic>Vibrio splendidus</italic> stimulation, and then gradually fell to the normal level at about 24 h. ELISA assay quantified that CgC1qDC-1 bound to LPS with high binding affinity (<italic>K</italic>d = 0.09 × 10<sup>−6</sup> M). Moreover, CgC1qDC-1 significantly enhanced the phagocytosis of oyster hemocytes towards Gram-negative bacteria <italic>Escherichia<abstract xml:lang="en" abstract-type="author" id="abs0010"> <title id="sectitle0010">Abstract</title> <sec> <p id="abspara0010">C1q proteins serve as pattern recognition receptors and involve in the pathogen recognition and complement pathway activation. In the present study, a novel C1q domain containing protein from <italic>Crassostrea gigas</italic> (designated CgC1qDC-1) was isolated by liposaccharide-Sepharose 6B affinity chromatography. The coding sequence of CgC1qDC-1 gene was determined by performing a homologous search of eight tryptic peptides identified by MALDI-TOF/TOF-MS against the genome of <italic>C. gigas</italic>. The coding sequence of CgC1qDC-1 was of 387 bp encoding a polypeptide of 128 amino acids containing a typical globular C1q domain. The globular C1q domain possessed eight β strands with a jelly-roll topology structure, which was similar to the structure of human gC1q domain. The mRNA transcripts of CgC1qDC-1 were dominantly expressed in mantle and hemocytes, while low expressed in hepatopancreas, gonad, gill and muscle. The expression level of CgC1qDC-1 increased drastically at 6 h after <italic>Vibrio splendidus</italic> stimulation, and then gradually fell to the normal level at about 24 h. ELISA assay quantified that CgC1qDC-1 bound to LPS with high binding affinity (<italic>K</italic>d = 0.09 × 10<sup>−6</sup> M). Moreover, CgC1qDC-1 significantly enhanced the phagocytosis of oyster hemocytes towards Gram-negative bacteria <italic>Escherichia coli</italic> and <italic>V</italic>. <italic>splendidus</italic>. These results collectively indicated that CgC1qDC-1 could serve as pattern recognition receptor and opsonin in the innate immune response against invading Gram-negative bacteria.</p> </sec> </abstract> … (more)
- Is Part Of:
- Fish & shellfish immunology. Volume 45:Issue 2(2015:Aug.)
- Journal:
- Fish & shellfish immunology
- Issue:
- Volume 45:Issue 2(2015:Aug.)
- Issue Display:
- Volume 45, Issue 2 (2015)
- Year:
- 2015
- Volume:
- 45
- Issue:
- 2
- Issue Sort Value:
- 2015-0045-0002-0000
- Page Start:
- 583
- Page End:
- 591
- Publication Date:
- 2015-08
- Subjects:
- Fishes -- Immunology -- Periodicals
Shellfish -- Immunology -- Periodicals
Poissons -- Immunologie -- Périodiques
Crustacés -- Immunologie -- Périodiques
571.9617 - Journal URLs:
- http://www.sciencedirect.com/science/journal/10504648 ↗
http://firstsearch.oclc.org ↗
http://firstsearch.oclc.org/journal=1050-4648;screen=info;ECOIP ↗
http://www.sciencedirect.com/science/journal/latest/10504648 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.fsi.2015.05.021 ↗
- Languages:
- English
- ISSNs:
- 1050-4648
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3934.880000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 3644.xml