A serum fucose-binding lectin (DlFBL) from adult Dicentrarchus labrax is expressed in larva and juvenile tissues and contained in eggs

Parisi, Maria Giovanna; Cammarata, Matteo; Benenati, Gigliola; Salerno, Giuseppina; Mangano, Valentina; Vizzini, Aiti; Parrinello, Nicolò

doi:10.1007/s00441-010-1004-6

Cited by 19 publications

(13 citation statements)

References 48 publications

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“…In subsequent studies (Cammarata et al 2007; Salerno et al 2009; Cammarata et al 2012) we established that DlFBL and SauFBL, a lectin from the gilt head sea bream ( Sparus aurata ) of similar binding properties, were both members of the F-type lectin family,and are also present in eggs (Parisi et al 2010). During affinity chromatography of D. labrax serum on L-fucose-agarose a protein peak with hemagglutinating activity that was susceptible to inhibition by L-rhamnose and D-galactose but not by L-fucose was identified, suggesting that this was a serum lectin distinct from DlFBL.…”

Section: Discussionmentioning

confidence: 96%

A rhamnose-binding lectin from sea bass (Dicentrarchus labrax) plasma agglutinates and opsonizes pathogenic bacteria

Cammarata

Parisi

Benenati

et al. 2014

Developmental & Comparative Immunology

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The discovery of rhamnose-binding lectins (RBLs) in teleost fish eggs led to the identification of a novel lectin family characterized by a unique sequence motif and a structural fold, and initially proposed to modulate fertilization. Further studies of the RBL tissue localization and gene organization were also suggestive of role(s) in innate immunity. Here we describe the purification, and biochemical and functional characterization of a novel RBL (DlRBL) from sea bass (Dicentrarchus labrax) serum. The purified DlRBL had electrophoretic mobilities corresponding to 24 kDa and 100 kDa under reducing and non-reducing conditions, respectively, suggesting that in plasma the DlRBL is present as a physiological homotetramer. DlRBL subunit transcripts revealed an open reading frame encoding 212 amino acid residues that included two tandemly-arrayed carbohydrate-recognition domains, and an 18-residue signal sequence at the N-terminus. The deduced size of 24.1 kDa for the mature protein was in good agreement with the subunit size of the isolated lectin. Binding activity of DlRBL for rabbit erythrocytes could be inhibited in the presence of rhamnose or galactose, did not require calcium, and was optimal at around 20°C and within the pH 6.5–8.0 range. DlRBL agglutinated Gram positive and Gram negative bacteria, and exposure of formalin-killed E. coli to DlRBL enhanced their phagocytosis by D. labrax peritoneal macrophages relative to the unexposed controls. Taken together, the results suggest that plasma DlRBL may play a role in immune recognition of microbial pathogens and facilitate their clearance by phagocytosis.

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Section: Discussionmentioning

confidence: 96%

A rhamnose-binding lectin from sea bass (Dicentrarchus labrax) plasma agglutinates and opsonizes pathogenic bacteria

Cammarata

Parisi

Benenati

et al. 2014

Developmental & Comparative Immunology

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“…The molecular property of DlFBL showed two tandem carbohydrate-recognition domains displaying F-type sequence motif. In situ hybridization showed that DlFBL distributed in hepatocytes and intestinal cells, as well as in embryonic yolk residues during fish ontogeny12. The function of DlFBL in Dicentrarchus labrax has been linked to enhancing the phagocytosis of microorganisms by macrophages11.…”

mentioning

confidence: 99%

Exogenous expression of marine lectins DlFBL and SpRBL induces cancer cell apoptosis possibly through PRMT5-E2F-1 pathway

Yang

Duan

et al. 2014

Sci Rep

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Lectins are widely existed in marine bioresources, and some purified marine lectins were found toxic to cancer cells. In this report, genes encoding Dicentrarchus labrax fucose-binding lectin (DlFBL) and Strongylocentrotus purpuratus rhamnose-binding lectin (SpRBL) were inserted into an adenovirus vector to form Ad.FLAG-DlFBL and Ad.FLAG-SpRBL, which elicited significant in vitro suppressive effect on a variety of cancer cells. Anti-apoptosis factors Bcl-2 and XIAP were determined to be downregulated by Ad.FLAG-DlFBL and Ad.FLAG-SpRBL. Subcellular localization studies showed that DlFBL but not SpRBL widely distributed in membrane systems. Both DlFBL and SpRBL were shown associated with protein arginine methyltransferase 5 (PRMT5), and PRMT5-E2F-1 pathway was suggested to be responsible for the DlFBL and SpRBL induced apoptosis. Further investigations revealed that PRMT5 acted as a common binding target for various exogenous lectin and non-lectin proteins, suggesting a role of PRMT5 as a barrier for foreign gene invasion. The cellular response to exogenous lectins may provide insights into a novel way for cancer gene therapy.

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“…20,23,30,31 They are expressed in larval and juvenile tissues and are also stored in eggs. 33 The scarcity of bacteria possessing FTL CRDs suggests that it may have been acquired through horizontal transfer from metazoans. 20 The absence of the FTL CRD in higher vertebrates is an evolutionary enigma that coincides with land colonization after cleidoic egg appearance.…”

Section: Fucose-binding Lectinsmentioning

confidence: 99%

“…17,27 For example, based on the identification of a novel CRD sequence motif 20 and a unique structural fold, 28 the FTL family was identified both in prokaryotes and in fluids and tissues of invertebrates and vertebrates. [29][30][31][32][33][34] …”

Section: Fish Lectinsmentioning

confidence: 99%

Evolution and Immune Function of Fish Lectins

Cammarata¹,

Parisi²,

Vasta³

2016

Lessons in Immunity

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Any queries or remarks that have arisen during the processing of your manuscript are listed below and are highlighted by flags in the proof. (AU indicates author queries; ED indicates editor queries; and TS/TY indicates typesetter queries.) Please check your proof carefully and answer all AU queries. Mark all corrections and query answers at the appropriate place in the proof using on-screen annotation in the PDF file. For a written tutorial on how to annotate PDFs, click http://www.elsevier.com/__data/assets/ pdf_file/0007/98953/Annotating-PDFs-Adobe-Reader-9-X-or-XI.pdf. A video tutorial is also available at http://www.screencast. com/t/9OIDFhihgE9a. Alternatively, you may compile them in a separate list and tick off below to indicate that you have answered the query. Please return your input as instructed by the project manager. Location in articleQuery / remark AU1, page 244 Please provide the expansion for genus names "S. purpuratus" and "C. intestinalis" in the sentence "In contrast, the N…". ■ AU4, page 250 Please check the term "conCL-s" mentioned in the sentence "In the latter, conCL-s…". ■ AU5, page 243The citation 'Ogawa et al.,25 ' in the legend of To protect the rights of the author(s) and publisher we inform you that this PDF is an uncorrected proof for internal business use only by the author(s), editor(s), reviewer(s), Elsevier and typesetter TNQ Books and Journals Pvt Ltd. It is not allowed to publish this proof online or in print. This proof copy is the copyright property of the publisher and is confidential until formal publication. 10018-BALLARIN-9780128032527Chapter 18 Evolution and Immune Function of Fish LectinsMatteo Cammarata, Maria G. Parisi University of Palermo, Palermo, Italy Gerardo R. Vasta University of Maryland School of Medicine, Baltimore, MD, United States c0018 INTRODUCTIONThe term "lectin" is commonly used to encompass a wide variety of carbohydrate-binding proteins, widely distributed in viruses, prokaryotes, and eukaryotes. 1 The first invertebrate lectins were described in the early 1900s in the snail Helix pomatia, 2 the horseshoe crab Limulus polyphemus, 3 and the lobster Homarus americanus. 3 Among the vertebrates, Watkins and Morgan 4 first described an l-fucose-specific lectin in the European eel Anguilla anguilla, which led to the discovery of the carbohydrate nature of the H blood substance. Animal lectins are grouped in various molecular families, differing in carbohydrate recognition domain (CRD) structure and organization. 1,[5][6][7] Based on their CRD sequence motifs and cation requirements, animal lectins can be categorized in several families, such as C-type lectins (CTLs), galectins (formerly S-type lectins), rhamnose-binding lectins (RBLs), F-type lectins (FTLs), X-type lectins (XTLs), I-type lectins, P-type lectins, and pentraxins. 1,[5][6][7] Lectins are involved in a variety of key biological processes ranging from development to immune responses. 1,[7][8][9][10][11] The roles of lectin-carbohydrate interactions in self/non-self recognition in early dev...

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A serum fucose-binding lectin (DlFBL) from adult Dicentrarchus labrax is expressed in larva and juvenile tissues and contained in eggs

Cited by 19 publications

References 48 publications

A rhamnose-binding lectin from sea bass (Dicentrarchus labrax) plasma agglutinates and opsonizes pathogenic bacteria

A rhamnose-binding lectin from sea bass (Dicentrarchus labrax) plasma agglutinates and opsonizes pathogenic bacteria

Exogenous expression of marine lectins DlFBL and SpRBL induces cancer cell apoptosis possibly through PRMT5-E2F-1 pathway

Evolution and Immune Function of Fish Lectins

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