A novel C1q family member with fucose-binding activity from surfperch, Neoditrema ransonnetii (Perciformes, Embiotocidae)

Nakamura, Osamu; Wada, Yukihito; Namai, Fumiyo; Saito, Erina; Araki, Kyosuke; Yamamoto, Atsushi; Tsutsui, Shigeyuki

doi:10.1016/j.fsi.2009.09.010

Cited by 20 publications

(5 citation statements)

References 19 publications

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“…It was observed to have a conserved C1q-like domain and possessed LPS binding potential. 91 Thus, by studying various C1q family members, the importance of the evolutionary aspect of C1q evolving into a mammalian homologue can be deduced as well as the discovery of novel functions of C1q family members.…”

Section: C1q Family Proteinsmentioning

confidence: 99%

Complement and non-complement activating functions of C1q: A prototypical innate immune molecule

et al. 2011

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C1q is a versatile innate immune molecule that serves as the initiation subcomponent of the classical complement pathway. In addition, it is also a potent pattern recognition molecule, the versatility of which has fuelled its functional flexibility. C1q recognises an array of self, non-self and altered-self ligands. The broad-spectrum ligand-binding potential of C1q is facilitated by the modular organisation of the heterotrimeric globular head region, its ability to change its conformation in a very subtle way, and the manner in which this ancient molecule appears to have evolved to deal with the different types of ligands. Over recent years, molecules that resemble C1q have been put together to form the C1q family. In this review, we briefly summarise complement-dependent and complement-independent functions of C1q, its cognate receptors and key members of the rapidly growing C1q family.

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Section: C1q Family Proteinsmentioning

confidence: 99%

Complement and non-complement activating functions of C1q: A prototypical innate immune molecule

et al. 2011

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“…Similarly, lectin-like fucose-binding activity was identified in a C1q-like protein from the surfperch ( Neoditrema ransonnetii ); it is expressed in liver, stomach and intestine, and is upregulated by bacterial challenge (Nakamura et al, 2009). Like the pufflectins, an intriguing homotetrameric protein (plumieribetin) from the fin stings and skin mucus of the scorpion-fish ( Scorpaena plumieri ) reveals structural characteristics shared with the plant mannose-binding B-lectins, known for the roles in defense against pathogens.…”

Section: The Lectin Repertoire In Fish: Genomic and Structural DIVmentioning

confidence: 99%

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

Vasta

Niță-Lazăr

Giomarelli

et al. 2011

Developmental & Comparative Immunology

150

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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.

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“…C1q is part of the complement pathway, but C1q domains are also found in a group of non-complement proteins that can act as pattern recognition molecules in innate immunity (Yu et al, 2008). C1qDCS have been identified in lamprey and related to roles in immunity (Nakamura et al, 2009;Pei et al, 2016), while C1q forms part of the complement system. Lamprey C1q is unusual as it acts as a lectin (Matsushita et al, 2004), activating C3 in association with MASP via the lectin pathway (Dodds and Matsushita, 2007;Matsushita 2018).…”

Section: Discussionmentioning

confidence: 99%

Post-translational protein deimination signatures in sea lamprey (Petromyzon marinus) plasma and plasma-extracellular vesicles

Rast

D’Alessio

Kraev

et al. 2021

Developmental & Comparative Immunology

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A novel C1q family member with fucose-binding activity from surfperch, Neoditrema ransonnetii (Perciformes, Embiotocidae)

Cited by 20 publications

References 19 publications

Complement and non-complement activating functions of C1q: A prototypical innate immune molecule

Complement and non-complement activating functions of C1q: A prototypical innate immune molecule

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

Post-translational protein deimination signatures in sea lamprey (Petromyzon marinus) plasma and plasma-extracellular vesicles

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