A galectin with quadruple-domain from red abalone Haliotis rufescens involved in the immune innate response against to Vibrio anguillarum

Maldonado-Aguayo, Waleska; Teneb, Jaime; Gallardo‐Escárate, Cristian

doi:10.1016/j.fsi.2014.06.013

Cited by 27 publications

(7 citation statements)

References 34 publications

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“…However, the increasing expression to 48 h evidences a recovery of the immune response (Figure 6). Similar results have been reported for the galectin from the red abalone Haliotis rufescens, where a peak in expression was observed 3 h post-challenge with V. alginolyticus [54], as well as in the clam Tegillarca granosa exposed to V. parahaemolyticus [55] and the bivalve M. trossulus post-challenge using V. proteolyticus [45]. No significant variation in expression levels was observed in the group exposed to diesel fuel alone (Figure 6).…”

Section: Temporal Levels Of Gyl After Microbial Challenge and Anthropogenic Pollutionsupporting

confidence: 86%

Identification and Characterization of a Novel Lectin from the Clam Glycymeris yessoensis and Its Functional Characterization under Microbial Stimulation and Environmental Stress

et al. 2021

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Lectin from the bivalve Glycymeris yessoensis (GYL) was purified by affinity chromatography on porcine stomach mucin–Sepharose. GYL is a dimeric protein with a molecular mass of 36 kDa, as established by SDS-PAGE and MALDI-TOF analysis, consisting of 18 kDa subunits linked by a disulfide bridge. According to circular dichroism data, GYL is a β/α-protein with the predominance of β-structure. GYL preferentially agglutinates enzyme-treated rabbit erythrocytes and recognizes glycoproteins containing O-glycosidically linked glycans, such as porcine stomach mucin (PSM), fetuin, thyroglobulin, and ovalbumin. The amino acid sequences of five segments of GYL were acquired via mass spectrometry. The sequences have no homology with other known lectins. GYL is Ca2+-dependent and stable over a range above a pH of 8 and temperatures up to 20 °C for 30 min. GYL is a pattern recognition receptor, as it binds common pathogen-associated molecular patterns, such as peptidoglycan, LPS, β-1,3-glucan and mannan. GYL possesses a broad microbial-binding spectrum, including Gram-positive (Bacillus subtilis, Staphylococcus aureus) and Gram-negative bacteria (Escherichia coli, Vibrio proteolyticus), but not the fungus Candida albicans. Expression levels of GYL in the hemolymph were significantly upregulated after bacterial challenge by V. proteolyticus plus environmental stress (diesel fuel). Results indicate that GYL is probably a new member of the C-type lectin family, and may be involved in the immune response of G. yessoensis to bacterial attack.

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Section: Temporal Levels Of Gyl After Microbial Challenge and Anthropogenic Pollutionsupporting

confidence: 86%

Identification and Characterization of a Novel Lectin from the Clam Glycymeris yessoensis and Its Functional Characterization under Microbial Stimulation and Environmental Stress

et al. 2021

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“…The decrease of HrGal transcript levels in hemocytes 6-12 h post-challenge may be due to the HrGal translation process in response to a bacterial infection. However, an increase in expression from 24 to 32 h indicates a restoration of the immune response [38]. Similar data were obtained in the clam Tegillarca granosa after Vibrio parahaemolyticus exposition [39], as well as in the mollusk Ruditapes philippinarum, where an expression peak was observed at 24 h after infection with Vibrio alginolyticus [40].…”

Section: Effect On Bacteria and Fungisupporting

confidence: 81%

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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“…No AMP was identified during our manual search, but two galectins were identified (Table ), and galectin-1 was identified in the WB proteome (Table ). Galectin-1 possesses 44% identity with a galectin identified in Haliotis rufescens gills, Hcts, and mantle, which is overexpressed in Hcts after challenge with Vibrio anguillarum . All these factors may be involved in bacterial recognition by and elimination from the cuttlefish WB.…”

Section: Resultsmentioning

confidence: 99%

“…Galectin-1 possesses 44% identity with a galectin identified in Haliotis rufescens gills, Hcts, and mantle, which is overexpressed in Hcts after challenge with Vibrio anguillarum. 144 All these factors may be involved in bacterial recognition by and elimination from the cuttlefish WB. Among the factors involved in the immune system response, we also detected four heat shock proteins (HSPs) (HSP 70, 71, 78, and 90) (Table 4) in the cuttlefish WB and Hct proteome.…”

Section: Involvement Of the Wb In Immunity And The Stress Responsementioning

confidence: 99%

-Omic Analysis of the Sepia officinalis White Body: New Insights into Multifunctionality and Haematopoiesis Regulation

Benoist

Corre

Bernay³

et al. 2020

J. Proteome Res.

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Cephalopods, like other Protostomes, lack an adaptive immune system and only rely on an innate immune system. The main immune cells are haemocytes, able to respond to pathogens and external attacks. First reports based on morphological observations suggested that the white body located in the optic sinuses of cuttlefish was at the origin of haemocytes. Combining transcriptomic and proteomic analyses, we identified several factors known to be involved in haematopoiesis in Vertebrate species in cuttlefish white body. Among these factors, members of the JAK-STAT signalling pathway were identified, some of them for the first time in a molluscan transcriptome and proteome. Immune factors such as members of the Toll/NF-κB signalling pathway, pattern recognition proteins and receptors, and members of the oxidative stress responses were also identified, and support an immune role of the white body. Both transcriptome and proteome analyses revealed that the white body harbours an intense metabolism concurrent with the haematopoietic function. Finally, a comparative analysis of the white body and haemocyte proteomes revealed many proteins in common, confirming previous morphological studies on the origin of haemocytes in cuttlefish. This molecular work demonstrates that the white body is multifunctional and provides bases for haematopoiesis regulation in cuttlefish.

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A galectin with quadruple-domain from red abalone Haliotis rufescens involved in the immune innate response against to Vibrio anguillarum

Cited by 27 publications

References 34 publications

Identification and Characterization of a Novel Lectin from the Clam Glycymeris yessoensis and Its Functional Characterization under Microbial Stimulation and Environmental Stress

Identification and Characterization of a Novel Lectin from the Clam Glycymeris yessoensis and Its Functional Characterization under Microbial Stimulation and Environmental Stress

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

-Omic Analysis of the Sepia officinalis White Body: New Insights into Multifunctionality and Haematopoiesis Regulation

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