High Innate Immune Specificity through Diversified C-Type Lectin-Like Domain Proteins in Invertebrates

Pees, Barbara; Yang, Wentao; Zárate-Potes, Alejandra; Schulenburg, Hinrich; Dierking, Katja

doi:10.1159/000441475

Cited by 125 publications

(119 citation statements)

References 83 publications

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“…Characterization of the domain architecture of MjGCTL demonstrates its uniqueness and binding-specificity is attributed not only to its binding motif but more importantly to its proper folding and glycosylation6. Here we speculate that the shift in the molecular weight detected of the purified rMjGCTL from its predicted size based on its amino acid sequence (35 kDa), may be due to the addition of carbohydrate moieties that is most likely to the presence of glycosylation.…”

Section: Discussionmentioning

confidence: 76%

“…However, evidences of the invertebrate immune system’s capability of discriminating between pathogen at species and even strain level refute the notion that invertebrate innate immune system is naïve in every infection even with the same pathogen6789. Thus, there is a growing interest in invertebrate immune research in learning how the invertebrate immune system can have high levels of specificity in the absence of antibody-mediated immune responses6. Having pathogen-specific immune responses requires a diverse array of pathogen recognition receptors (PRRs) that recognize and initiate the immune response through pathogen-associated molecular patterns (PAMPs)1011.…”

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confidence: 99%

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Pathogen recognition of a novel C-type lectin from Marsupenaeus japonicus reveals the divergent sugar-binding specificity of QAP motif

Alenton

Koiwai

Miyaguchi

et al. 2017

Sci Rep

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C-type lectins (CTLs) are calcium-dependent carbohydrate-binding proteins known to assist the innate immune system as pattern recognition receptors (PRRs). The binding specificity of CTLs lies in the motif of their carbohydrate recognition domain (CRD), the tripeptide motifs EPN and QPD bind to mannose and galactose, respectively. However, variants of these motifs were discovered including a QAP sequence reported in shrimp believed to have the same carbohydrate specificity as QPD. Here, we characterized a novel C-type lectin (MjGCTL) possessing a CRD with a QAP motif. The recombinant MjGCTL has a calcium-dependent agglutinating capability against both Gram-negative and Gram-positive bacteria, and its sugar specificity did not involve either mannose or galactose. In an encapsulation assay, agarose beads coated with rMjGCTL were immediately encapsulated from 0 h followed by melanization at 4 h post-incubation with hemocytes. These results confirm that MjGCTL functions as a classical CTL. The structure of QAP motif and carbohydrate-specificity of rMjGCTL was found to be different to both EPN and QPD, suggesting that QAP is a new motif. Furthermore, MjGCTL acts as a PRR binding to hemocytes to activate their adherent state and initiate encapsulation.

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Section: Discussionmentioning

confidence: 76%

mentioning

confidence: 99%

Pathogen recognition of a novel C-type lectin from Marsupenaeus japonicus reveals the divergent sugar-binding specificity of QAP motif

Alenton

Koiwai

Miyaguchi

et al. 2017

Sci Rep

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“…All C-type lectins share a highly conserved domain, the carbohydrate recognition (CRD) or C-type lectin-like domain (CTLD). The CTLD gene family is highly diverse in C. elegans, comprising more than 280 genes and being the seventh most abundant gene family in the worm (reviewed in [87]). Although vertebrate CTLD proteins are known to be involved in pathogen recognition, some mammalian CTLD proteins of the RegIII family possess antibacterial activity and function in pathogen elimination [88,89].…”

Section: Future Challenges: Functional Evidence For Worm Immune Effecmentioning

confidence: 99%

Antimicrobial effectors in the nematode Caenorhabditis elegans : an outgroup to the Arthropoda

Dierking

Yang

Schulenburg

2016

Phil. Trans. R. Soc. B

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One contribution of 13 to a theme issue 'Evolutionary ecology of arthropod antimicrobial peptides'. Nematodes and arthropods likely form the taxon Ecdysozoa. Information on antimicrobial effectors from the model nematode Caenorhabditis elegans may thus shed light on the evolutionary origin of these defences in arthropods. This nematode species possesses an extensive armory of putative antimicrobial effector proteins, such as lysozymes, caenopores (or saposin-like proteins), defensin-like peptides, caenacins and neuropeptide-like proteins, in addition to the production of reactive oxygen species and autophagy. As C. elegans is a bacterivore that lives in microbe-rich environments, some of its effector peptides and proteins likely function in both digestion of bacterial food and pathogen elimination. In this review, we provide an overview of C. elegans immune effector proteins and mechanisms. We summarize the experimental evidence of their antimicrobial function and involvement in the response to pathogen infection. We further evaluate the microbe-induced expression of effector genes using WormExp, a recently established database for C. elegans gene expression analysis. We emphasize the need for further analysis at the protein level to demonstrate an antimicrobial activity of these molecules both in vitro and in vivo.This article is part of the themed issue 'Evolutionary ecology of arthropod antimicrobial peptides'.

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“…Notably, this report is in line with another review article by Scordo et al [13] wondering whether alveolar epithelial cells are active players or innocent bystanders in Mycobacterium tuberculosis infections. C-type lectins are an ancient arm of innate immunity, underlining their fundamental importance [14]. In this issue of Journal of Innate Immunity , Dong et al [15] show for the first time that the C-type lectin collectin-11 is expressed in both the murine and human neural retina.…”

mentioning

confidence: 99%

Bystander Cells Taking Action

Herwald

Egesten

2017

J Innate Immun

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High Innate Immune Specificity through Diversified C-Type Lectin-Like Domain Proteins in Invertebrates

Abstract: CTLD genes could contribute to immune specificity. In spite of recent achievements, the exact functions of the diversified invertebrate CTLD genes are still largely unknown. Our review therefore specifically discusses promising research approaches to rectify this knowledge gap.

Cited by 125 publications

References 83 publications

Pathogen recognition of a novel C-type lectin from Marsupenaeus japonicus reveals the divergent sugar-binding specificity of QAP motif

Pathogen recognition of a novel C-type lectin from Marsupenaeus japonicus reveals the divergent sugar-binding specificity of QAP motif

Antimicrobial effectors in the nematode Caenorhabditis elegans : an outgroup to the Arthropoda

Bystander Cells Taking Action

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