Literature DB >> 21896283

Structural and functional diversity of the lectin repertoire in teleost fish: relevance to innate and adaptive immunity.

Gerardo R Vasta1, Mihai Nita-Lazar, Barbara Giomarelli, Hafiz Ahmed, Shaojun Du, Matteo Cammarata, Nicolò Parrinello, Mario A Bianchet, L Mario Amzel.   

Abstract

Protein-carbohydrate interactions mediated by lectins have been recognized as key components of innate immunity in vertebrates and invertebrates, not only for recognition of potential pathogens, but also for participating in downstream effector functions, such as their agglutination, immobilization, and complement-mediated opsonization and killing. More recently, lectins have been identified as critical regulators of mammalian adaptive immune responses. Fish are endowed with virtually all components of the mammalian adaptive immunity, and are equipped with a complex lectin repertoire. In this review, we discuss evidence suggesting that: (a) lectin repertoires in teleost fish are highly diversified, and include not only representatives of the lectin families described in mammals, but also members of lectin families described for the first time in fish species; (b) the tissue-specific expression and localization of the diverse lectin repertoires and their molecular partners is consistent with their distinct biological roles in innate and adaptive immunity; (c) although some lectins may bind endogenous ligands, others bind sugars on the surface of potential pathogens; (d) in addition to pathogen recognition and opsonization, some lectins display additional effector roles, such as complement activation and regulation of immune functions; (e) some lectins that recognize exogenous ligands mediate processes unrelated to immunity: they may act as anti-freeze proteins or prevent polyspermia during fertilization.
Copyright © 2011. Published by Elsevier Ltd.

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Year:  2011        PMID: 21896283      PMCID: PMC3429948          DOI: 10.1016/j.dci.2011.08.011

Source DB:  PubMed          Journal:  Dev Comp Immunol        ISSN: 0145-305X            Impact factor:   3.636


  109 in total

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Journal:  Dev Comp Immunol       Date:  2015-09-30       Impact factor: 3.636

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

Authors:  Matteo Cammarata; Maria Giovanna Parisi; Gigliola Benenati; Gerardo R Vasta; Nicolò Parrinello
Journal:  Dev Comp Immunol       Date:  2014-01-28       Impact factor: 3.636

5.  Development of microsatellite markers using next-generation sequencing for the fish Colossoma macropomum.

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