Biochemical Characterization of Oyster and Clam Galectins: Selective Recognition of Carbohydrate Ligands on Host Hemocytes and Perkinsus Parasites

Vasta, Gerardo R.; Feng, Chiguang; Tasumi, Satoshi; Abernathy, Kelsey; Bianchet, M.A.; Wilson, Iain B. H.; Paschinger, Katharina; Wang, Lai-Xi; Iqbal, Muddasar; Ghosh, Anita; Amin, Md. Ruhul; Smith, Brina A.; Brown, Sean M.; Vista, Aren

doi:10.3389/fchem.2020.00098

Cited by 12 publications

(5 citation statements)

References 59 publications

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“…Two neighboring galectins on chromosome 3, galectin-4-like (LOC117323441) and LOC117323440, have a typical bivalve galectin structure of four tandem-repeat CRDs. This particular type of galectin has previously been studied in the oyster Crassostrea virginica , which also has two of these proteins, CvGal1 and CvGal2 ( 33 ). Synteny, gene structure and amino acid sequence show a close relationship of these galectins between oyster and scallop.…”

Section: Resultsmentioning

confidence: 99%

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A brief history of galectin evolution

Günther

Galuska

2023

Front. Immunol.

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Galectins are a family of carbohydrate-binding proteins found in vertebrates in great abundance and diversity in terms of both structure and ligand-binding properties as well as physiological function. Proteins with clear relationships to vertebrate galectins are already found in primitive Bilateria. The increasing amount of accessible well-annotated bilaterian genomes has allowed us to reveal, through synteny analyses, a new hypothesis about the phylogenetic history of the galectin family in this animal group. Thus, we can trace the genomic localization of the putative ancestral Bilateria galectin back to the scallops as a still very primitive slow-evolving bilaterian lineage. Intriguingly, our analyses show that the primordial galectin of the Deuterostomata most likely exhibited galectin-8-like characteristics. This basal standing galectin is characterized by a tandem-repeat type with two carbohydrate recognition domains as well as by a sialic acid binding property of the N-terminal domain, which is typical for galectin-8. With the help of synteny, the amplification of this potential primordial galectin to the broad galectin cosmos of modern jawed vertebrates can be reconstructed. Therefore, it is possible to distinguish between the paralogs resulting from small-scale duplication and the ohnologues generated by whole-genome duplication. Our findings support a substantially new hypothesis about the origin of the various members of the galectin family in vertebrates. This allows us to reveal new theories on the kinship relationships of the galectins of Gnatostomata. In addition, we focus for the first time on the galectines of the Cyclostomata, which as a sister group of jawed vertebrates providing important insights into the evolutionary history of the entire subphylum. Our studies also highlight a previously neglected member of the galectin family, galectin-related protein 2. This protein appears to be a widespread ohnologue of the original tandem-repeat ancestor within Gnathostomata that has not been the focus of galectin research due to its nonclassical galactose binding sequence motif and the fact that it was lost during mammalian evolution.

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Section: Resultsmentioning

confidence: 99%

“…In the oyster, CvGal1 and 2 are produced by hemocytes, the phagocytes of the bivalve ( 34 ). Galectins bind exogenous glycans, for example, from pathogens, as well as endogenous glycans on the surface of hemocytes via their different CRDs ( 33 ). Thus, they can function as phagocytosis-mediating opsonins.…”

Section: Resultsmentioning

confidence: 99%

A brief history of galectin evolution

Günther

Galuska

2023

Front. Immunol.

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“…Lectin-like proteins: 9 genes were annotated as C-type lectins or lectin domain-containing proteins. They may participate in biological defense mechanisms 48 , and they may also be involved in specific conformation of fps or collagens by regulating glycosylation, in cooperation with enzymes involved in sugar chain regulation. The sets of genes, pvir_s00346g40/pvir_s00346g41 and pvir_s00466g48/pvir_s00466g49, of which the latter accompanies one similar gene pvir_s00466g47 with lower TPM, were found in tandem, suggesting amplification by tandem duplication.…”

Section: Resultsmentioning

confidence: 99%

Genomics and transcriptomics of the green mussel explain the durability of its byssus

Inoue

Yoshioka

Tanaka

et al. 2021

Sci Rep

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Mussels, which occupy important positions in marine ecosystems, attach tightly to underwater substrates using a proteinaceous holdfast known as the byssus, which is tough, durable, and resistant to enzymatic degradation. Although various byssal proteins have been identified, the mechanisms by which it achieves such durability are unknown. Here we report comprehensive identification of genes involved in byssus formation through whole-genome and foot-specific transcriptomic analyses of the green mussel, Perna viridis. Interestingly, proteins encoded by highly expressed genes include proteinase inhibitors and defense proteins, including lysozyme and lectins, in addition to structural proteins and protein modification enzymes that probably catalyze polymerization and insolubilization. This assemblage of structural and protective molecules constitutes a multi-pronged strategy to render the byssus highly resistant to environmental insults.

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“…Here, the disruption in the GlcNAc immune signal in gametes could be a signal to activate hemocytes mediated by PRRs as a response to thermal stress, thus controlling immune processes such as cell death and phagocytosis. GlcNAc-binding lectins present in hemocytes have been widely described in the immune activation of mollusks [14,40,41], reported hemocyte infiltration and phagocytic activity increased significantly over the thermal stress application (12 °C to 21 °C) in C. gigas, but also in the mussel Mytilus galloprovincialis and the cockle Katelysa rhytiphora. Bigger differences between the acclimation temperature and stress temperature can affect negatively hemocyte response, producing decreased total hemocyte count, hemocyte adhesion, and phagocytic activity in invertebrates [12], including Crassotrea.…”

Section: Discussionmentioning

confidence: 99%

Untitled

2023

AAF

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The present study evaluates the presence and location of carbohydrates in general, and the monosaccharide N-acetylglucosamine (GlcNAc) on tissues of temperate oyster Crassostrea gigas and tropical oyster C. corteziensis during an increase in temperature during reproduction, a stress which is probably one of the main causes of the oyster's summer mass mortality events. Adult oysters from both species were placed at 22 °C and exposed to a gradual increase in temperature (1 °C day-1) until reaching 34 °C. The values of the GlcNAc index were higher in C. corteziensis compared to C. gigas in the gonads, vesicular connective tissue and digestive gland of males and females during the experiment, except for the hemocytes in the gonads, where the GlcNAc index was significantly highest in C. gigas at 34 °C. A PCA revealed an inverse association between GlcNAc in tissues (gonad, digestive gland, and vesicular connective tissue) and GlcNAc in hemocytes for females and males. The present study shows evidence that water temperature increase affects the overall immune system capability and hemocyte-tissues signaling function, with deep differences between C. gigas and C. corteziensis, particularly in females. This information provides valuable insights for further studies into the immunological mechanisms of oyster summer mortality events.

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Biochemical Characterization of Oyster and Clam Galectins: Selective Recognition of Carbohydrate Ligands on Host Hemocytes and Perkinsus Parasites

Cited by 12 publications

References 59 publications

A brief history of galectin evolution

A brief history of galectin evolution

Genomics and transcriptomics of the green mussel explain the durability of its byssus

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