Antimicrobial properties and immune-related gene expression of a C-type lectin isolated from Pinctada fucata martensii

He, Jun-Jun; Shen, Chenghao; Liang, Haiying; Fang, Xiaochen; Lu, Jinzhao

doi:10.1016/j.fsi.2020.07.017

Cited by 26 publications

(11 citation statements)

References 47 publications

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“…A total of 21 sequences were obtained (Table S1). All the 21 sequences are interesting, some sequences have been studied and published in our previous study (He et al, 2020;Liang et al, 2022), other sequences are in study. One of the immune effector molecules identified as PmlysG was selected for follow-up studies in this manuscript.…”

Section: Methodsmentioning

confidence: 99%

“…The tissues, including mantle, hemocytes, gonads, gills, hepatopancreas, and adductor muscle were obtained from 10 pearl oysters and immediately stored in liquid nitrogen for further use. The total RNA was extracted from the samples according to a previously reported method (He et al, 2020). After obtaining the total RNA from various tissues, it was reverse transcribed into cDNA.…”

Section: Tissue Expression Analysismentioning

confidence: 99%

“…Unlike advanced animals, mollusks are typical invertebrates without any unique immune system. In this regard, the innate immune factors play a crucial role in invertebrate immunity (Wang et al, 2013;He et al, 2019;He et al, 2020), including heme-mediated cellular and humoral immune responses (Fan et al, 2022;Lv et al, 2022). The innate immune factors dissolve the invading microorganisms or bacterial tissues using constitutive and inducible antibacterial molecules (Rolff and Siva-Jothy, 2003;He et al, 2018).…”

Section: Introductionmentioning

confidence: 99%

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Immune characterization and expression analysis of a goose-type lysozyme gene from Pinctada fucata martensii

Guo

Shen²,

Liang³

et al. 2022

Front. Mar. Sci.

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In the present study, a g-type lysozyme was successfully screened and cloned from Pinctada fucata martensii (designated as PmlysG). The cDNA has a length of 973 bp with an open reading frame (ORF) of 769 bp, encoding a protein of 255 amino acids. The PmlysG transcript was detected in multiple tissues by quantitative real-time PCR (qRT-PCR), with the highest expression being in the hepatopancreas. Additionally, the temporal expression of PmlysG mRNA in the hepatopancreas after in vivo stimulation with pathogen-associated molecular patterns (PAMPs), such as lipopolysaccharide (LPS), peptidoglycan (PGN) and polyinosinic acid (PolyI:C) was detected by qRT-PCR. Although PmlysG responded to all three stimulation modes, it rapidly responded to PGN stimulation. Meanwhile, the recombinant protein of g-type lysozyme of P.f. martensii (rPmlysG) was used for antibacterial function analysis, and the results showed that rPmlysG has antibacterial function against Vibrio parahaemolyticus, Aeromonas hydrophila, and Pseudomonas aeruginosa. Overall, these study results suggest that the identified PmlysG participates in the innate immune responses of P.f. martensii against pathogen infection.

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Section: Methodsmentioning

confidence: 99%

Section: Tissue Expression Analysismentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Immune characterization and expression analysis of a goose-type lysozyme gene from Pinctada fucata martensii

Guo

Shen²,

Liang³

et al. 2022

Front. Mar. Sci.

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“…In addition, a significant increase in expression of a C-type lectin (PmCTL-1) was observed in pearl oysters in response to bacterial stimulation. Purified PmCTL-1 additionally exerted strong antimicrobial activity against Gram-positive bacterial such as M icrococcus luteus , S. aureus , and B. subtilis [ 129 ].…”

Section: Physiological Functions Of Lectins In Host Bodymentioning

confidence: 99%

An Update of Lectins from Marine Organisms: Characterization, Extraction Methodology, and Potential Biofunctional Applications

et al. 2022

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Lectins are a unique group of nonimmune carbohydrate-binding proteins or glycoproteins that exhibit specific and reversible carbohydrate-binding activity in a non-catalytic manner. Lectins have diverse sources and are classified according to their origins, such as plant lectins, animal lectins, and fish lectins. Marine organisms including fish, crustaceans, and mollusks produce a myriad of lectins, including rhamnose binding lectins (RBL), fucose-binding lectins (FTL), mannose-binding lectin, galectins, galactose binding lectins, and C-type lectins. The widely used method of extracting lectins from marine samples is a simple two-step process employing a polar salt solution and purification by column chromatography. Lectins exert several immunomodulatory functions, including pathogen recognition, inflammatory reactions, participating in various hemocyte functions (e.g., agglutination), phagocytic reactions, among others. Lectins can also control cell proliferation, protein folding, RNA splicing, and trafficking of molecules. Due to their reported biological and pharmaceutical activities, lectins have attracted the attention of scientists and industries (i.e., food, biomedical, and pharmaceutical industries). Therefore, this review aims to update current information on lectins from marine organisms, their characterization, extraction, and biofunctionalities.

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“…Lectins are proteins that possess at least one carbohydrate recognition domain (CRD), which specifically and reversibly binds to oligosaccharides (glycans) of glycoconjugates (glycoproteins, glycolipids, and proteoglycans). There is considerable interest in glycobiology relating to marine organisms and, in recent years, many lectins from marine invertebrates have been identified, including mollusks [ 1 , 2 , 3 , 4 , 5 , 6 , 7 ]. Invertebrates, unlike vertebrates, lack antibody-mediated humoral immunity in their systems [ 8 , 9 ]; however, invertebrates do possess innate immunity: the host defense of mollusks and other invertebrates against pathogenic infection solely depends on various pattern recognition receptors (PRRs), which bind conserved pathogen-associated molecular pattern molecules (PAMPs) expressed among the array of carbohydrate components on the surfaces of microorganisms.…”

Section: Introductionmentioning

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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Antimicrobial properties and immune-related gene expression of a C-type lectin isolated from Pinctada fucata martensii

Cited by 26 publications

References 47 publications

Immune characterization and expression analysis of a goose-type lysozyme gene from Pinctada fucata martensii

Immune characterization and expression analysis of a goose-type lysozyme gene from Pinctada fucata martensii

An Update of Lectins from Marine Organisms: Characterization, Extraction Methodology, and Potential Biofunctional Applications

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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