Evidence map›Paper›PMID 23192616›Full record

ArticleMolecular biology reports2013

Identification and molecular characterization of a C-type lectin-like protein from Chinese shrimp (Fenneropenaeus chinensis).

Xiaofang Lai, Jie Kong, Qingyin Wang, Weiji Wang, Xianhong Meng

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Article in Molecular biology reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
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1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

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4 · The record

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PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Xiaofang LaiOcean and Fisheries College, Huaihai Institute of Technology, Lianyungang, 222005, China. lai.xiaofang@163.com
Jie Kong
Qingyin Wang
Weiji Wang
Xianhong Meng

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A C-type lectin-like protein was cloned and characterized from the Chinese shrimp Fenneropenaeus chinensis, and named as FcCTL. The results indicated that the full length cDNA of 859 bp had an open reading frame encoded a polypeptide of 220 amino acids with one carbohydrate-recognition domain, six conserved Cys and one key motif EPGD. The theoretical molecular weight and pI of mature protein was 25.3 kDa and 5.4. Sequence comparison of the deduced amino acid sequence of FcCTL showed varied identity of 26-34, 34, 31 and 30 % with those of F. chinensis, Portunus trituberculatus, Tetraodon nigroviridis, Penaeus monodon, respectively. qRT-PCR analysis indicated that FcCTL was expressed highest in hepatopancreas of normal shrimp, and it's expression was up-regulated in hepatopancreas and gills post white spot syndrome virus challenge. The purified recombinant FcCTL showed higher antimicrobial activity against Gram-positive bacteria than against Gram-negative bacteria and fungi. And the hemagglutinating activity of rFcCTL could be completely inhibited by GlcNAc (5 μg/ml), LPS (2.5 μg/ml), D-galactose (100 mM) and maltose (100 mM). These data suggested that FcCTL might play an important role in shrimp immune and would be helpful to better understand the innate immunity mechanism of shrimp.

Indexed as

Amino Acid SequenceAnimalsAnti-Infective AgentsBase SequenceCarbohydratesDNA, ComplementaryGene ExpressionLectins, C-TypeMicrobial Sensitivity TestsMolecular Sequence DataOrgan SpecificityPenaeidaeProtein BindingRecombinant ProteinsSequence AlignmentAnti-Infective AgentsCarbohydratesDNA, ComplementaryLectins, C-TypeRecombinant Proteins

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.