Lectins of marine hydrobionts

Chernikov, Oleg V.; Molchanova, V. I.; Chikalovets, I. V.; Kondrashina, A. S.; Li, W.; Lukyanov, Pavel

doi:10.1134/s0006297913070080

Cited by 19 publications

(13 citation statements)

References 128 publications

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“…Therefore, the high expression of the serine protease inhibitor in healthy clams supports its involvement in M. mercenaria ’s resistance against QPX, likely by inhibiting the activity of parasite proteases. Moreover, a pathogen recognition protein (c-type lectin domain family 10 member A-like) was significantly higher in healthy clams as compared to diseased animals, which may also contribute to clam resistance against QPX by promoting microbial recognition and encapsulation [ 128 ]. Previous studies demonstrated that clam genetic background affects M. mercenaria resistance toward QPX [ 4 , 129 , 130 ], therefore immune-related transcripts specifically associated with healthy clams represent excellent candidates as molecular markers for further research on screening and breeding QPX-resistant M. mercenaria strains.…”

Section: Resultsmentioning

confidence: 99%

Clam focal and systemic immune responses to QPX infection revealed by RNA-seq technology

et al. 2016

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BackgroundThe hard clam Mercenaria mercenaria is an important seafood species widely exploited along the eastern coasts of the United States and play a crucial role in coastal ecology and economy. Severe hard clam mortalities have been associated with the protistan parasite QPX (Quahog Parasite Unknown). QPX infection establishes in pallial organs with the lesions typically characterized as nodules, which represent inflammatory masses formed by hemocyte infiltration and encapsulation of parasites. QPX infection is known to induce host changes on both the whole-organism level and at specific lesion areas, which imply systemic and focal defense responses, respectively. However, little is known about the molecular mechanisms underlying these alterations.ResultsRNA-seq was performed using Illumina Hiseq 2000 (641 Million 100 bp reads) to characterize M. mercenaria focal and systemic immune responses to QPX. Transcripts were assembled and the expression levels were compared between nodule and healthy tissues from infected clams, and between these and tissues from healthy clams. De novo assembly reconstructed a consensus transcriptome of 62,980 sequences that was functionally-annotated. A total of 3,131 transcripts were identified as differentially expressed in different tissues. Results allowed the identification of host immune factors implicated in the systemic and focal responses against QPX and unraveled the pathways involved in parasite neutralization. Among transcripts significantly modulated upon host-pathogen interactions, those involved in non-self recognition, signal transduction and defense response were over-represented. Alterations in pathways regulating hemocyte focal adhesion, migration and apoptosis were also demonstrated.ConclusionsOur study is the first attempt to thoroughly characterize M. mercenaria transcriptome and identify molecular features associated with QPX infection. It is also one of the first studies contrasting focal and systemic responses to infections in invertebrates using high-throughput sequencing. Results identified the molecular signatures of clam systemic and focal defense responses, to collectively mediate immune processes such as hemocyte recruitment and local inflammation. These investigations improve our understanding of bivalve immunity and provide molecular targets for probing the biological bases of clam resistance towards QPX.Electronic supplementary materialThe online version of this article (doi:10.1186/s12864-016-2493-9) contains supplementary material, which is available to authorized users.

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Section: Resultsmentioning

confidence: 99%

Clam focal and systemic immune responses to QPX infection revealed by RNA-seq technology

et al. 2016

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“…Marine lectins are structurally diverse, and their unique structures have a number of potential uses in biomedical applications. Although more than 300 species of marine lectins have been found, most of these investigations have focused on those with biomedical applications as antibacterial, antifungal, antiviral, antitumour, antinociceptive and anti-inflammatory agents 8 , 29 . Lectins are characterized as immunomodulatory agents and can induce the production of certain cytokines and reactive species to induce efficient immune responses against tumours or microbial infections 30 .…”

Section: Discussionmentioning

confidence: 99%

A GalNAc/Gal-specific lectin from the sea mussel Crenomytilus grayanus modulates immune response in macrophages and in mice

Chernikov

Wong

et al. 2017

Sci Rep

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A GalNAc/Gal-specific lectin (CGL) from the edible mussel Crenomytilus grayanus has been demonstrated to exhibit antibacterial properties. However, the mechanism of immune modulation by CGL in mammalian cells remains unclear. Here, we demonstrated that CGL can activate immune responses in macrophages and in mice. In the in vitro cell models, CGL induced tumour necrosis factor-α and interleukin-6 secretion in mouse RAW264.7 macrophages, mouse bone marrow-derived macrophages, human THP-1 macrophages, human peripheral blood mononuclear cells and human blood monocyte-derived macrophages. The CGL-mediated cytokine production was regulated by reactive oxygen species, mitogen-activated protein kinases, protein kinase C-α/δ and NF-κB. Interestingly, in lipopolysaccharide-activated macrophages, CGL induced endotoxin tolerance (characterized by the downregulation of nitric oxide, inducible nitric oxide synthase, interleukin-6 and cyclooxygenase II) via the downregulation of IRAK2 expression, JNK1/2 phosphorylation and NF-κB activation. CGL also slightly increased the bactericidal activity of macrophages and induced cytokine production in mouse models. Overall, our data indicate that CGL has the potential to be used as an immune modulator in mammals.

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“…Genes of marine invertebrates are considered to closely reflect those of the common ancestor(s) of animals, and are therefore useful for elucidating fundamental evolutionary mechanisms, and for development of molecular tools in biomedical fields. Many novel types of lectins have been found in marine invertebrate species (13)(14)(15)(16), and some of these lectins have been shown to inhibit growth of viruses (17,18), regulate development of symbiotic/pathogenic microorganisms (19,20), or affect mammalian cell cycle (21)(22)(23)(24). D-galactose (Gal) evidently emerged as an important monosaccharide later in evolutionary time than glucose, fructose, or mannose, and therefore plays key roles in cellular recognition (25).…”

Section: A Introductionmentioning

confidence: 99%

Phylogeny and Properties of a Novel Lectin Family with β-Trefoil Folding in Mussels

Fujii

Gerdol

Hasan

et al. 2018

TIGG

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A novel lectin, termed "MytiLec," was isolated and characterized from the mussel Mytilus galloprovincialis, an important food and environmental indicator species found in marine coastal areas worldwide. MytiLec binds to the sugar moiety of globotriose (Gb3), an α-galactoside, leading to apoptosis of Gb3-expressing Burkitt's lymphoma cells. The amino acid sequence of MytiLec is unusual, but 3-dimensional structural analysis reveals the presence of β-trefoil fold, a well-known feature in "R-type" lectins, a family of galactose-binding proteins found in many types of organisms. To date, MytiLec has been found only in a few species of the mollusk family Mytilidae and the phylum Brachiopoda, which also express typical R-type lectins. In this minireview, we discuss: (i) possible reasons for the unusual coexistence of two distinct lectin families in the same animal family; (ii) structural models of MytiLec that are useful for design of lectins with improved anti-cancer properties; (iii) construction of "Mitsuba," an artificial lectin based on MytiLec that has similar carbohydrate-binding activity but a more stable monomeric form; (iv) regulation of cell growth by MytiLec and related lectins through binding to glycans.

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Lectins of marine hydrobionts

Cited by 19 publications

References 128 publications

Clam focal and systemic immune responses to QPX infection revealed by RNA-seq technology

Clam focal and systemic immune responses to QPX infection revealed by RNA-seq technology

A GalNAc/Gal-specific lectin from the sea mussel Crenomytilus grayanus modulates immune response in macrophages and in mice

Phylogeny and Properties of a Novel Lectin Family with β-Trefoil Folding in Mussels

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