Source:http://linkedlifedata.com/resource/pubmed/id/16930711
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2006-9-26
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pubmed:abstractText |
Pattern recognition proteins (PRPs), such as lipopolysaccharide and beta-1,3-glucan binding protein (LGBP), have been identified in many animals and play a crucial role in invertebrate defense systems. In the current study, an LGBP gene was cloned from fleshy prawn (Fenneropenaeus chinensis, Fc-LGBP) utilizing homology cloning and RACE methods. The full cDNA of the Fc-LGBP gene in fleshy prawn was 1253bp in size with a deduced 366 amino acid protein that includes a glycosyl hydrolase domain. Northern blot and RT-PCR data suggested that Fc-LGBP mRNA was mostly synthesized in haemocytes and that the expression was down-regulated 24h post-injection of bacteria. In situ hybridization demonstrated that Fc-LGBP mRNA was only detected in haemocyte cytoplasm, with no detection in other tissues. The molecular weight of the purified recombinantly expressed Fc-LGBP was approximately 46kDa. Immunohistochemistry of haemocytes revealed that Fc-LGBP protein was localized on the membrane of most cells. Data from bacterial binding assays utilizing purified protein suggested that rFc-LGBP had strong binding activity to Gram-negative bacteria.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acute-Phase Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Pattern Recognition,
http://linkedlifedata.com/resource/pubmed/chemical/beta-1,3-D-glucan,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Glucans,
http://linkedlifedata.com/resource/pubmed/chemical/lipopolysaccharide-binding protein
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0161-5890
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
44
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1085-94
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pubmed:meshHeading |
pubmed-meshheading:16930711-Acute-Phase Proteins,
pubmed-meshheading:16930711-Amino Acid Sequence,
pubmed-meshheading:16930711-Animals,
pubmed-meshheading:16930711-Base Sequence,
pubmed-meshheading:16930711-Carrier Proteins,
pubmed-meshheading:16930711-Cloning, Molecular,
pubmed-meshheading:16930711-Lipopolysaccharides,
pubmed-meshheading:16930711-Membrane Glycoproteins,
pubmed-meshheading:16930711-Molecular Sequence Data,
pubmed-meshheading:16930711-Penaeidae,
pubmed-meshheading:16930711-Protein Binding,
pubmed-meshheading:16930711-Receptors, Pattern Recognition,
pubmed-meshheading:16930711-beta-Glucans
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pubmed:year |
2007
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pubmed:articleTitle |
Molecular cloning and characterization of a lipopolysaccharide and beta-1,3-glucan binding protein from fleshy prawn (Fenneropenaeus chinensis).
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pubmed:affiliation |
School of Life Sciences, Shandong University, Jinan, Shandong 250100, China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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