Mannan-Binding Lectin of the Sea Urchin Strongylocentrotus nudus

Bulgakov, Aleksandr; Елисейкина, М. Г.; Kovalchuk, Svetlana N.; Petrova, Irina Y.; Likhatskaya, G. N.; Shamshurina, E. V.; Rasskazov, V. A.

doi:10.1007/s10126-012-9460-5

Cited by 11 publications

(5 citation statements)

References 49 publications

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“…The eponymous cells within the coelomic fluid, the coelomocytes, are critical for both cellular and humoral elements of the immune response, including phagocytosis and the release of antimicrobial enzymes to target and destroy foreign antigens [ 4 ]. Laboratory studies have established the existence of echinoderm recognition proteins [ 5 , 6 ], cytokine signaling molecules [ 7 ], and effector mechanisms, such as antimicrobial peptides [ 8 ]. Conserved immune response pathways identified in genomic and proteomic screens of echinoderms include the complement system, Toll pathway, and cell adhesion regulation [ 3 , 9 , 10 ].…”

Section: Introductionmentioning

confidence: 99%

Up in Arms: Immune and Nervous System Response to Sea Star Wasting Disease

et al. 2015

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Echinoderms, positioned taxonomically at the base of deuterostomes, provide an important system for the study of the evolution of the immune system. However, there is little known about the cellular components and genes associated with echinoderm immunity. The 2013–2014 sea star wasting disease outbreak is an emergent, rapidly spreading disease, which has led to large population declines of asteroids in the North American Pacific. While evidence suggests that the signs of this disease, twisting arms and lesions, may be attributed to a viral infection, the host response to infection is still poorly understood. In order to examine transcriptional responses of the sea star Pycnopodia helianthoides to sea star wasting disease, we injected a viral sized fraction (0.2 μm) homogenate prepared from symptomatic P. helianthoides into apparently healthy stars. Nine days following injection, when all stars were displaying signs of the disease, specimens were sacrificed and coelomocytes were extracted for RNA-seq analyses. A number of immune genes, including those involved in Toll signaling pathways, complement cascade, melanization response, and arachidonic acid metabolism, were differentially expressed. Furthermore, genes involved in nervous system processes and tissue remodeling were also differentially expressed, pointing to transcriptional changes underlying the signs of sea star wasting disease. The genomic resources presented here not only increase understanding of host response to sea star wasting disease, but also provide greater insight into the mechanisms underlying immune function in echinoderms.

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Section: Introductionmentioning

confidence: 99%

Up in Arms: Immune and Nervous System Response to Sea Star Wasting Disease

et al. 2015

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“…This is despite that a growing number of genes involved in the innate immunity have recently been identified from the sea cucumber Apostichopus japonicus [27e30]. Thus far, a few CTLs from echinoderms have been identified and characterized, such as MBL-SN from the sea urchin Strongylocentrotus nudus [31], echinoidin from the sea urchin Anthocidaris crassispina [32], and AMUL from the starfish Asterias amurensis [33]. Numbers of CTLs were discovered in the genome of purple sea urchin Strongylocentrotus purpuratus in 2006 [34], which laied a foundation for further study on CTLs in sea urchin.…”

Section: Introductionmentioning

confidence: 99%

Critical roles of sea cucumber C-type lectin in non-self recognition and bacterial clearance

Wei

Liu

Yang

et al. 2015

Fish & Shellfish Immunology

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a b s t r a c t C-type lectin is one important pattern recognition receptor (PRR) that plays crucial roles in multiple immune responses. A C-type lectin from sea cucumber Apostichopus japonicus (AjCTL-1) was characterized in the present study. The amino acid sequence of AjCTL-1 shared high similarities with other Ctype lectins from invertebrates and vertebrates. The C-type lectin domain (CTLD) of AjCTL-1 contained a Ca 2þ -binding site 2 and four conserved cysteine residues. AjCTL-1 mRNA expression patterns in tissues and after bacterial challenge were then analysed. Quantitative PCR revealed that AjCTL-1 mRNA was widely expressed in the tested tissues of healthy sea cucumber. The highest expression level occurred in gonad followed by body wall, coelomocytes, tentacle, intestinum and longitudinal muscle, and the lowest expression level was in respiratory tree. AjCTL-1 mRNA expression in coelomocytes was significantly induced by gram-negative Listonella anguillarum and gram-positive Micrococcus luteus, with different upregulation patterns post-challenge. Recombinant AjCTL-1 exhibited the ability to bind peptidoglycan directly, agglutinate M. luteus, Staphylococcus aureus and Escherichia coli, in a Ca 2þ -dependant manner, and enhance the phagocytosis of coelomocytes against E. coli in vitro. The results indicated that AjCTL-1 could act as a PRR in Apostichopus japonicus and had critical roles in non-self recognition and bacterial clearance against invading microbes.

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“…The effects of pH, temperature, and divalent cations on GYL were evaluated, as described previously [ 62 ]. Briefly, to study the effect of temperature, aliquots of the lectin (0.05 mL, 1 mg/mL) were incubated at 4, 20, 37, 40, 45, 50, and 60 °C for 30 min, and the hemagglutination assay was performed after cooling.…”

Section: Methodsmentioning

confidence: 99%

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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Mannan-Binding Lectin of the Sea Urchin Strongylocentrotus nudus

Cited by 11 publications

References 49 publications

Up in Arms: Immune and Nervous System Response to Sea Star Wasting Disease

Up in Arms: Immune and Nervous System Response to Sea Star Wasting Disease

Critical roles of sea cucumber C-type lectin in non-self recognition and bacterial clearance

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

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