ArticleScientific reports2015
CfLec-3 from scallop: an entrance to non-self recognition mechanism of invertebrate C-type lectin.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers, 1 of them a synthesis that pooled it.
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Who cites it
11 citing papers in PubMed, 1 synthesis or guideline pooled it, 52 citations in OpenAlex.
- C-Type Lectins from Marine Bivalves: Functional Diversity and Structural Insights.Marine drugs · 2025Pooled it
- MicroRNA-1985 enhances the redox capability of scallop (Frontiers in immunology · 2025Article
- DC-SIGN of Largemouth Bass (International journal of molecular sciences · 2024Article
- A c-type lectinFrontiers in immunology · 2024Article
- Functional Diversity of Novel Lectins with Unique Structural Features in Marine Animals.Cells · 2023Review
- Hepatopancreas-Specific Lectin Participates in the Antibacterial Immune Response by Regulating the Expression of Antibacterial Proteins.Frontiers in immunology · 2021Article
- The Members of the Highly DiverseFrontiers in immunology · 2020Article
- Pathogen-Derived Carbohydrate Recognition in Molluscs Immune Defense.International journal of molecular sciences · 2018Review
- Microbial Diseases of Bivalve Mollusks: Infections, Immunology and Antimicrobial Defense.Marine drugs · 2017Review
- An invertebrate-specific miRNA targeted the ancient cholinergic neuroendocrine system of oyster.Open biology · 2016Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A C-type lectin (CfLec-3) from Chlamys farreri with three carbohydrate-recognition domains (CRDs) was selected to dissect the possible mechanisms of PAMP binding and functional differentiation of invertebrate lectins. CfLec-3 distributed broadly, and its mRNA expression in hemocytes increased significantly after stimulations with LPS, PGN or β-glucan, but not poly(I:C). The recombinant CfLec-3 (rCfLec-3) could bind PAMPs and several microbes. rCfLec-3 mediated hemocytes phagocytosis against Escherichia coli and encapsulation towards agarose beads. Obvious functional differentiation occurred among the three CRDs, as CRD1 exhibited higher activity to bind PAMPs, while CRD2/3 were expert in promoting hemocyte mediated opsonisation. The tertiary structural differences were suspected to be associated with such functional differentiation. PAMP binding abilities of CfLec-3 were determined by Ca(2+)-binding site 2 motif. When Pro in this motif of each CRD was mutated into Ser, their PAMP binding abilities were deprived absolutely. rCRD2 acquired mannan binding capability when its EPD was replaced by EPN, but lost when EPN in rCRD3 was changed into EPD. The Pro in Ca(2+)-binding site 2 was indispensable for PAMPs binding, while Asn was determinant for specific binding to mannan. It shed new insight into PAMPs binding mechanism of invertebrate C-type lectins and their functional differentiation.
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