Abstract

Nematodes are a very diverse phylum that has adapted to nearly every ecosystem. They have developed specialized lifestyles, dividing the phylum into free-living, animal, and plant parasitic species. Their sheer abundance in numbers and presence in nearly every ecosystem make them the most prevalent animals on earth. In this research nematode-specific profiles were designed to retrieve predicted lectin-like domains from the sequence data of nematode genomes and transcriptomes. Lectins are carbohydrate-binding proteins that play numerous roles inside and outside the cell depending on their sugar specificity and associated protein domains. The sugar-binding properties of the retrieved lectin-like proteins were predicted in silico. Although most research has focused on C-type lectin-like, galectin-like, and calreticulin-like proteins in nematodes, we show that the lectin-like repertoire in nematodes is far more diverse. We focused on C-type lectins, which are abundantly present in all investigated nematode species, but seem to be far more abundant in free-living species. Although C-type lectin-like proteins are omnipresent in nematodes, we have shown that only a small part possesses the residues that are thought to be essential for carbohydrate binding. Curiously, hevein, a typical plant lectin domain not reported in animals before, was found in some nematode species.

Highlights

  • IntroductionAnimals, and microorganisms. they are best known for their carbohydrate binding properties, some of them are involved in protein–protein, protein–lipid, or protein–nucleic acid interactions [1]

  • Lectins occur in plants, animals, and microorganisms

  • Most research has focused on C-type lectin-like, galectin-like, and calreticulin-like proteins in nematodes, we show that the lectin-like repertoire in nematodes is far more diverse

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Summary

Introduction

Animals, and microorganisms. they are best known for their carbohydrate binding properties, some of them are involved in protein–protein, protein–lipid, or protein–nucleic acid interactions [1]. Lectins are defined as proteins that have at least one non-catalytic domain that reversibly binds to a specific mono- or oligosaccharide [2]. These carbohydrate-binding proteins may be involved in a variety of functions, ranging from innate immunity to glycoprotein synthesis [3]. Stillmark [4] discovered that this extremely toxic protein was able to clot red blood cells It took over 60 years to assign the agglutination activity to the ability of lectins to recognize and bind carbohydrate structures on the surface of erythrocytes [5]. A hepatic lectin was found in the rabbit liver in 1974 and was claimed to be the first lectin of mammalian origin [8]

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