A Lectin from the Mussel Mytilus galloprovincialis Has a Highly Novel Primary Structure and Induces Glycan-mediated Cytotoxicity of Globotriaosylceramide-expressing Lymphoma Cells

Fujii, Yuki; Dohmae, Naoshi; Takio, Koji; Kawsar, Sarkar M. A.; Matsumoto, Ryo; Hasan, Imtiaj; Koide, Yasuhiro; Kanaly, Robert A.; Yasumitsu, Hidetaro; Ogawa, Yukiko; Sugawara, Shigeki; Hosono, Masahiro; Nitta, Kazuo; Hamako, Jiharu; Matsui, Taei; Ozeki, Yasuhiro

doi:10.1074/jbc.m112.418012

Cited by 80 publications

(71 citation statements)

References 58 publications

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“…Overall, about 20 different genes encoding proteins with a ricin domain are present in the C. gigas genome: most of them pertain to the well-known class of a-N-acetylgalactosaminyltransferases, enzymes which are involved in the biosynthesis of Mucin-type O-glycans. A novel lectin named MytiLec, with globotriose-dependent cytotoxicity, has been recently identified in M. galloprovincialis [65], and later a very similar lectin with antibacterial activity was identified in Crenomytilus grayanus [66]. These lectins share a structural motif with three very similar tandem repeats of about 50 amino acids, recognizable as a ricin-type beta trefoil domain.…”

Section: Extracellular Prrsmentioning

confidence: 98%

An updated molecular basis for mussel immunity

Gerdol

Venier

2015

Fish & Shellfish Immunology

134

163

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Non-self recognition with the consequent tolerance or immune reaction is a crucial process to succeed as living organisms. At the same time the interactions between host species and their microbiome, including potential pathogens and parasites, significantly contribute to animal life diversity. Marine filter-feeding bivalves, mussels in particular, can survive also in heavily anthropized coastal waters despite being constantly surrounded by microorganisms. Based on the first outline of the Mytilus galloprovincialis immunome dated 2011, the continuously growing transcript data and the recent release of a draft mussel genome, we explored the available sequence data and scientific literature to reinforce our knowledge on the main gene-encoded elements of the mussel immune responses, from the pathogen recognition to its clearance. We carefully investigated molecules specialized in the sensing and targeting of potential aggressors, expected to show greater molecular diversification, and outlined, whenever relevant, the interconnected cascades of the intracellular signal transduction. Aiming to explore the diversity of extracellular, membrane-bound and intracellular pattern recognition receptors in mussel, we updated a highly complex immune system, comprising molecules which are described here in detail for the first time (e.g. NOD-like receptors) or which had only been partially characterized in bivalves (e.g. RIG-like receptors). Overall, our comparative sequence analysis supported the identification of over 70 novel full-length immunity-related transcripts in M. galloprovincialis. Nevertheless, the multiplicity of gene functions relevant to immunity, the involvement of part of them in other vital processes, and also the lack of a refined mussel genome make this work still not-exhaustive and support the development of more specific studies.

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Section: Extracellular Prrsmentioning

confidence: 98%

An updated molecular basis for mussel immunity

Gerdol

Venier

2015

Fish & Shellfish Immunology

134

163

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“…New Gal-specific lectin MytiLec (later renamed to MytiLec-1 [14], the new name was used in present review) with globotriose-dependent cytotoxicity was recently identified in the mussel Mytilus galloprovincialis [12], and later it was reported about lectin CGL from the mussel Crenomytilus grayanus with similar amino acid sequence and antibacterial activity [15]. Analysis of the protein sequences of these lectins ( Figure 1) showed that they form a novel lectin family, sharing common structure-three tandem repeats with similar sequences to each other consisting of 40 amino acids and three carbohydrate-binding sites in each sub-domain.…”

Section: Novel Lectin Family Structurementioning

confidence: 99%

“…Today a large number of galactosyl-binding lectins have been reported to occur in the invertebrates, which bind to D-galactose, its derivatives, and D-galactose containing complex carbohydrates in a very selective manner [9][10][11][12][13].…”

Section: Introductionmentioning

confidence: 99%

Activity Dependence of a Novel Lectin Family on Structure and Carbohydrate-Binding Properties

et al. 2019

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A GalNAc/Gal-specific lectins named CGL and MTL were isolated and characterized from the edible mussels Crenomytilus grayanus and Mytilus trossulus. Amino acid sequence analysis of these lectins showed that they, together with another lectin MytiLec-1, formed a novel lectin family, adopting β-trefoil fold. In this mini review we discuss the structure, oligomerization, and carbohydrate-binding properties of a novel lectin family. We describe also the antibacterial, antifungal, and antiproliferative activities of these lectins and report about dependence of activities on molecular properties. Summarizing, CGL, MTL, and MytiLec-1 could be involved in the immunity in mollusks and may become a basis for the elaboration of new diagnostic tools or treatments for a variety of cancers.

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“…In the past decades, lectins have been developed to form useful agents to analyze glycofiles and biomarkers for a variety of cancers, including pancreatic cancer [1], aggressive breast cancer [2,3], ovarian cancer [4], prostate cancer [5], and liver cancer [6], as well as cytotoxic agents for inducing cancer cells apoptosis or autophagy [7][8][9][10]. Previously, we determined that, through adenovirus-mediated gene delivery, lectins including mannose binding plant lectin Pinellia pedatisecta agglutinin (PPA) as well as marine lectins such as galectin Anguilla japonica lectin 1 (AJL1), Haliotis discus discus sialic acid binding lectin (HddSBL), Dicentrarchus labrax fucose binding lectin (DlFBL), and Strongylocentrotus purpuratus rhamnose binding lectin (SpRBL) elicited cytotoxicity to a variety of cancer cells [11][12][13][14].…”

Section: Introductionmentioning

confidence: 99%

Ulva pertusa lectin 1 delivery through adenovirus vector affects multiple signaling pathways in cancer cells

Zhao

et al. 2017

Glycoconj J

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Ulva pertusa lectin 1 (UPL1) is a N-acetyl-D-glucosamine (GlcNAc) binding lectin in marine green alga Ulva pertusa. Exogenous UPL1 colocalized with protein arginine methyltransferase 5 (PRMT5), methylosome protein 50 (MEP50), β-actin and β-tubulin, indicating the interaction of UPL1 with the methylosome and cytoskeleton. UPL1 delivery through adenovirus vector (Ad-UPL1) dramatically induced extracellularly regulated protein kinases 1/2 (ERK1/2) phosphorylation in liver cancer cell lines BEL-7404 and Huh7. Signaling pathways including p38 mitogen-activated protein kinase (MAPK), and Akt were also affected by Ad-UPL1 in a cell type dependent manner. MEK1/2 inhibitor U0126, as well as to a lesser extent p38 MAPK inhibitor SB203580 and phosphoinositide 3-kinase (PI3K) inhibitor LY294002, completely eliminated a higher molecular weight isoform of β-tubulin induced by Ad-UPL1, and significantly enhanced the cytotoxicity of Ad-UPL1 in Huh7 cells, suggesting that the inhibition of MEK1/2, p38 MAPK, and PI3K enhanced antiproliferative effect of Ad-UPL1 possibly through regulating the modification of β-tubulin. Ad-UPL1 completely inhibited the expression of autophagy-related factor Beclin1, but induced LC3-II expression in Huh7 cells. In addition, Ad-UPL1 significantly enhanced starvation induced survival suppression in Huh7 cells. Our data elucidated intracellular signaling pathways affected by exogenous UPL1, and may provide insights into a novel way of UPL1 delivery through adenovirus vectors combined with survival signaling inhibitors for cancer treatment.

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A Lectin from the Mussel Mytilus galloprovincialis Has a Highly Novel Primary Structure and Induces Glycan-mediated Cytotoxicity of Globotriaosylceramide-expressing Lymphoma Cells

Cited by 80 publications

References 58 publications

An updated molecular basis for mussel immunity

An updated molecular basis for mussel immunity

Activity Dependence of a Novel Lectin Family on Structure and Carbohydrate-Binding Properties

Ulva pertusa lectin 1 delivery through adenovirus vector affects multiple signaling pathways in cancer cells

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