A Genomic and Transcriptomic Analysis of the C-Type Lectin Gene Family Reveals Highly Expanded and Diversified Repertoires in Bivalves

Saco, Amaro; Suárez, Hugo; Novoa, Beatriz; Figueras, António

doi:10.3390/md21040254

Cited by 9 publications

(2 citation statements)

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“…These observations strongly suggest that invertebrate C-type lectins function as patternrecognition molecules and play a role in innate immunity. The importance of C-type lectins for the immune system in invertebrates is supported by the wide distribution of C-type CRDs or CTLDs among different animal species [42][43][44].…”

Section: Introductionmentioning

confidence: 99%

Functional Diversity of Novel Lectins with Unique Structural Features in Marine Animals

Hatakeyama

Unno

2023

Cells

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Due to their remarkable structural diversity, glycans play important roles as recognition molecules on cell surfaces of living organisms. Carbohydrates exist in numerous isomeric forms and can adopt diverse structures through various branching patterns. Despite their relatively small molecular weights, they exhibit extensive structural diversity. On the other hand, lectins, also known as carbohydrate-binding proteins, not only recognize and bind to the diverse structures of glycans but also induce various biological reactions based on structural differences. Initially discovered as hemagglutinins in plant seeds, lectins have been found to play significant roles in cell recognition processes in higher vertebrates. However, our understanding of lectins in marine animals, particularly marine invertebrates, remains limited. Recent studies have revealed that marine animals possess novel lectins with unique structures and glycan recognition mechanisms not observed in known lectins. Of particular interest is their role as pattern recognition molecules in the innate immune system, where they recognize the glycan structures of pathogens. Furthermore, lectins serve as toxins for self-defense against foreign enemies. Recent discoveries have identified various pore-forming proteins containing lectin domains in fish venoms and skins. These proteins utilize lectin domains to bind target cells, triggering oligomerization and pore formation in the cell membrane. These findings have spurred research into the new functions of lectins and lectin domains. In this review, we present recent findings on the diverse structures and functions of lectins in marine animals.

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Section: Introductionmentioning

confidence: 99%

Functional Diversity of Novel Lectins with Unique Structural Features in Marine Animals

Hatakeyama

Unno

2023

Cells

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“…In organisms devoid of an immunoglobulin-and T-cell receptor-based adaptive immune system, lectins gain a primary role as a first barrier to prevent microbial invasion. Hence, it is not surprising that a significant number of lectin families underwent massive expansion during evolution in different lineages, fueled by tandem gene duplication events and subsequent fast molecular diversification (and functional specialization) via positive selection [7][8][9][10][11].…”

Section: Introductionmentioning

confidence: 99%

Taxonomic Distribution and Molecular Evolution of Mytilectins

Gerdol,

Nerelli,

Martelossi

et al. 2023

Marine Drugs

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R-type lectins are a widespread group of sugar-binding proteins found in nearly all domains of life, characterized by the presence of a carbohydrate-binding domain that adopts a β-trefoil fold. Mytilectins represent a recently described subgroup of β-trefoil lectins, which have been functionally characterized in a few mussel species (Mollusca, Bivalvia) and display attractive properties, which may fuel the development of artificial lectins with different biotechnological applications. The detection of different paralogous genes in mussels, together with the description of orthologous sequences in brachiopods, supports the formal description of mytilectins as a gene family. However, to date, an investigation of the taxonomic distribution of these lectins and their molecular diversification and evolution was still lacking. Here, we provide a comprehensive overview of the evolutionary history of mytilectins, revealing an ancient monophyletic evolutionary origin and a very broad but highly discontinuous taxonomic distribution, ranging from heteroscleromorphan sponges to ophiuroid and crinoid echinoderms. Moreover, the overwhelming majority of mytilectins display a chimera-like architecture, which combines the β-trefoil carbohydrate recognition domain with a C-terminal pore-forming domain, suggesting that the simpler structure of most functionally characterized mytilectins derives from a secondary domain loss.

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