F-type lectin involved in defense against bacterial infection in the pearl oyster (Pinctada martensii)

Chen, Jinhui; Xiao, Shijun; Zhou, Yu

doi:10.1016/j.fsi.2010.12.025

Cited by 36 publications

(19 citation statements)

References 36 publications

(28 reference statements)

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“…F-type lectins have been widely investigated in many invertebrates but, comparatively, their role in bivalve immunity received much less attention, as only two F-type lectins of Pinctada spp. involved in PAMP recognition and up-regulated in the hemocytes of challenged oysters have been identified [67,68].…”

Section: Extracellular Prrsmentioning

confidence: 99%

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: 99%

An updated molecular basis for mussel immunity

Gerdol

Venier

2015

Fish & Shellfish Immunology

134

163

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“…Five individuals were randomly sampled in each tank in 2, 4, 6, 8, 12, 24, 36 h after Vibrio challenge. Hemolymph from both animals in each group was collected as previously described [17].…”

Section: Experimental Oysters Immune Challenge and Salinity Stressmentioning

confidence: 99%

Cloning and expression of a heat shock protein (HSP) 90 gene in the haemocytes of Crassostrea hongkongensis under osmotic stress and bacterial challenge

Chen

Zhang

et al. 2011

Fish & Shellfish Immunology

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“…Certain lectin-coding genes in bivalves have been found to be up-or down-regulated in association with infection by pathogenic microorganisms, indicating that the lectins are able to respond to external/environmental stimuli (3,4). Several lectins with characteristic structures have been described in bivalves, including C-type lectins and galectins (5,6), fibrinogen-type (7), C1q-type (8), and F-type lectins (fucolectin) (9). A Gal/GalNAc-binding lectin (information on primary structure unavailable) was reported in Crenomytilus, a genus related to Mytilus (10).…”

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confidence: 99%

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

Fujii

Dohmae

Takio

et al. 2012

Journal of Biological Chemistry

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Background: Studies on the diversity of carbohydrate-binding proteins (lectins) are important in glycobiology. Results: A lectin having a novel primary structure was isolated from a mussel and found to have a globotriose-dependent cytotoxicity on Burkitt lymphoma cells. Conclusion: A new primary structure quite distinct from known lectin is described. Significance: Discovery of similar lectin structures from vertebrates will lead to progress in medical sciences.

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F-type lectin involved in defense against bacterial infection in the pearl oyster (Pinctada martensii)

Cited by 36 publications

References 36 publications

An updated molecular basis for mussel immunity

An updated molecular basis for mussel immunity

Cloning and expression of a heat shock protein (HSP) 90 gene in the haemocytes of Crassostrea hongkongensis under osmotic stress and bacterial challenge

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

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