Isolation and characterization of a fish F-type lectin from gilt head bream (Sparus aurata) serum

Cammarata, Matteo; Benenati, Gigliola; Odom, Eric W.; Salerno, Giuseppina; Vizzini, Aiti; Vasta, Gerardo R.; Parrinello, Nicolò

doi:10.1016/j.bbagen.2006.09.015

Cited by 42 publications

(33 citation statements)

References 21 publications

(41 reference statements)

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“…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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Section: Fish Lectinsmentioning

confidence: 99%

Evolution and Immune Function of Fish Lectins

Cammarata¹,

Parisi²,

Vasta³

2016

Lessons in Immunity

Self Cite

View full text Add to dashboard Cite

show abstract

“…Recently, isolation of lectins from various sources has been described using numerous sugars, such as lactose (Almanza et al, 2004;Braga et al, 2006;Fujii et al, 2011;Hamako et al, 2007;Kawsar et al, 2009;Mendonça-Franqueiro et al, 2011;Naeem et al, 2007b;Pohleven et al, 2009;Rocha et al, 2009;Silva et al, 2007), sucrose and glucose (Pohleven et al, 2011), galactose (Konami et al, 1991;Lavanya Latha et al, 2006;Mo et al, 2000;Moreira et al, 1998;Naeem et al, 2007b;Nagata, 2005), mannose (Andon et al, 2003;Ooi et al, 2010;Suseelan et al, 2002), fucose (Cammarata et al, 2007;Mansour & Abdul-Salam, 2009), L-rhamnose (Jimbo et al, 2007;Watanabe et al, 2008), and sugars with 2'-acetamido groups N-acetylgalactosamine (Gerlach et al, 2005;Perçin et al, 2009;Qureshi et al, 2006), N-acetylglucosamine (Kaur et al, 2005;Kim et al, 2006;Maheswari et al, 2002;Wang & Ng, 2003), and N,N'-diacetylchitobiose (Konami et al, 1991;Koyama et al, 2002).…”

Section: Mono-and Disaccharidesmentioning

confidence: 99%

Affinity Chromatography of Lectins

Pohleven¹,

Štrukelj²,

Kos³

2012

Affinity Chromatography

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“…SauFBL was purified by affinity chromatography following Cammarata et al (2007). Briefly, the serum (2-5 ml), was diluted 10-fold in TBS, filtered through a 0.22-µm filter (Millex GV, Millipore), applied to an L-fucose-agarose column (1.6×5 cm, 5 ml) equilibrated with TBS, and washed with TBS (10 vols).…”

Section: Purification Of Serum Fucose-binding Lectinmentioning

confidence: 99%

“…The structure of MsFBP32 in complex with L-fucose revealed a trimeric organization with two globular opposite halves containing, respectively, the N-CRDs and the C-CRDs (Bianchet et al 2010). We proposed that fish F-lectins mediate immune defense responses both in the blood stream (Bianchet et al 2002(Bianchet et al , 2010Odom & Vasta 2006) and intestinal mucus (Cammarata et al 2001(Cammarata et al , 2007Salerno et al 2009). …”

Section: Introductionmentioning

confidence: 99%

“…Previously, we reported the purification of sea bass (DlFBP) and gilt head bream (SauFBP32) serum FBPs (Cammarata et al 2001(Cammarata et al , 2007Salerno et al 2009), and that SauFBP32 displays epitopes recognized by anti-DlFBP specific antibodies. Further, based on the DlFBP cDNA sequence, we showed that it is a bona fide F-lectin, shares carbohydrate specificity and biochemical properties with other well characterized F-lectins (Salerno et al 2009), is expressed in larval and juvenile tissues and is contained in eggs (Parisi et al 2010).…”

Section: Introductionmentioning

confidence: 99%

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Primary structure and opsonic activity of an F-lectin from serum of the gilt head breamSparus aurata(Pisces, Sparidae)

Cammarata

Salerno

Parisi

et al. 2012

Italian Journal of Zoology

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The recently described fucose-binding agglutinin from the European eel revealed a novel lectin fold (the 'F-type' fold) that is shared with other carbohydrate-binding proteins and proteins from prokaryotes to vertebrates clustered under the newly established F-type lectin (FTL) family. We previously reported the purification and biochemical characterization of a fucose-binding protein (FBP) isolated from serum of the gilt head bream (Sparus aurata, SauFBP). In the present article, the complete coding sequence of SauFBP revealed that it is a member of the FTL family, consisting of two tandem carbohydrate recognition domains (CRD) that display the F-type sequence motif. In vitro opsonization assays showed that the isolated SauFBP binds to formalin-killed Escherichia coli and enhances their phagocytosis by peritoneal macrophages.

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Isolation and characterization of a fish F-type lectin from gilt head bream (Sparus aurata) serum

Cited by 42 publications

References 21 publications

Evolution and Immune Function of Fish Lectins

Evolution and Immune Function of Fish Lectins

Affinity Chromatography of Lectins

Primary structure and opsonic activity of an F-lectin from serum of the gilt head breamSparus aurata(Pisces, Sparidae)

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