title: Structural and functional diversity of the lectin repertoire in teleost fish: relevance to innate and adaptive immunity.
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.
authors: Department of Microbiology and Immunology, University of Maryland School of Medicine, Program in the Biology of Model Systems, Baltimore, MD 21202, USA. gvasta@som.umbi.umaryland.edu
authors: Gerardo R
authors: GR
authors: Vasta
authors: Mihai
authors: M
authors: Nita-Lazar
authors: Barbara
authors: B
authors: Giomarelli
authors: Hafiz
authors: H
authors: Ahmed
authors: Shaojun
authors: S
authors: Du
authors: Matteo
authors: M
authors: Cammarata
authors: Nicolò
authors: N
authors: Parrinello
authors: Mario A
authors: MA
authors: Bianchet
authors: L Mario
authors: LM
authors: Amzel
mesh_terms: D056704:Adaptive Immunity; D000818:Animals; D021301:Antifreeze Proteins / Q000235:genetics / Q000276:immunology; D000942:Antigens, Bacterial / Q000276:immunology / Q000378:metabolism; D000956:Antigens, Viral / Q000276:immunology / Q000378:metabolism; D001419:Bacteria / Q000276:immunology; D003167:Complement Activation / Q000276:immunology*; D003165:Complement System Proteins / Q000276:immunology; D029941:Fish Proteins / Q000737:chemistry / Q000145:classification / Q000235:genetics / Q000276:immunology* / Q000378:metabolism; D005399:Fishes / Q000276:immunology; D005786:Gene Expression Regulation / Q000276:immunology; D007113:Immunity, Innate; D007448:Invertebrates / Q000276:immunology; D037102:Lectins / Q000737:chemistry / Q000145:classification / Q000235:genetics / Q000276:immunology* / Q000378:metabolism; D008958:Models, Molecular; D009895:Opsonin Proteins / Q000235:genetics / Q000276:immunology; D009928:Organ Specificity; D010587:Phagocytosis / Q000276:immunology; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D014714:Vertebrates / Q000276:immunology; D014780:Viruses / Q000276:immunology
chemical_list: D021301:Antifreeze Proteins; D000942:Antigens, Bacterial; D000956:Antigens, Viral; D029941:Fish Proteins; D037102:Lectins; D009895:Opsonin Proteins; D003165:Complement System Proteins