Anti-biofilm properties and immunological response of an immune molecule lectin isolated from shrimp Metapenaeus monoceros

Elumalai, Preetham; Rubeena, Abdul Salam; Vaseeharan, Baskaralingam; Chaurasia, Mukesh Kumar; Arockiaraj, Jesu; Olsen, Rolf Erik

doi:10.1016/j.fsi.2019.09.032

Cited by 13 publications

(3 citation statements)

References 64 publications

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“…The role of MaCTL in loach immunity was further confirmed by its antimicrobial activity, which directly inhibits the growth of three kinds of Gram‐ bacteria and one kind of Gram + bacteria. The antimicrobial activity has been reported for CTLs from other taxa of animals, such as the mammals (Mukherjee et al., 2014) and crustaceans (Preetham et al., 2019; Wang & Wang, 2013), but rarely for CTLs from fish. It is unclear whether most fish CTLs lack the antimicrobial activity or they have not been examined yet.…”

Section: Discussionmentioning

confidence: 99%

A C‐type lectin with antibacterial activity in weather loach, Misgurnus anguillicaudatus

Zhang

Yang

Zhang³

et al. 2020

Journal of Fish Diseases

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C‐type lectins are carbohydrate‐binding proteins that play important roles in immunity by serving as pattern recognition receptors. In the present study, a novel nattectin‐like C‐type lectin was obtained from the weather loach, Misgurnus anguillicaudatus, designated as MaCTL. MaCTL encodes a peptide with 165 amino acids, with a signal peptide and a single C‐type lectin domain (CTLD), containing a galactose‐specific QPD motif and a conserved Ca2+‐binding site. Transcripts of MaCTL were significantly upregulated after immune challenge with its pathogen A. hydrophila. In vitro assays with recombinant MaCTL protein revealed that it exhibited hemagglutinating and bacterial agglutinating activities, in a Ca2+‐dependent manner. MaCTL was found to bind to a wide range of bacteria, as well as bind to bacterial polysaccharides LPS and PGN. Moreover, MaCTL displayed antimicrobial activity by inhibiting the growth of bacteria. These results collectively suggest that MaCTL is involved in the antibacterial defence of weather loach.

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Section: Discussionmentioning

confidence: 99%

A C‐type lectin with antibacterial activity in weather loach, Misgurnus anguillicaudatus

Zhang

Yang

Zhang³

et al. 2020

Journal of Fish Diseases

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“…In environmental microbiology, biofilm formation is an important biological concept in which microbial cells conform to multicellular lifestyles by forming biofilms during which the bacterial cells are self‐immobilized in the extracellular polymeric matrix (Arunasri & Mohan, 2018). Biofilm arrangement is of significance in a few pathogenic microbes, especially aquatic organisms, conferring a particular advantage by expanding their capacity to hold on beneath antagonistic natural conditions (Preetham et al, 2019). Biofilm is also known as the microbial community on an organic matrix and attaches to surfaces.…”

Section: Formation Of Biofilmmentioning

confidence: 99%

Pathogenic bacterial toxins and virulence influences in cultivable fish

Sarkar

Issac

Raju

et al. 2021

Aquaculture Research

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Bacterial virulence factors play a major role in infection, which provides devastating effect on the aquaculture industry. Bacterial toxins are the major virulence factors that influence the roles of host cells and take control of living organisms’ vital processes to facilitate microbial infection. Various other bacterial virulent components such as adhesins, capsular polysaccharides, lipopolysaccharides, bacterial flagellum, pili and microbial siderophore provide a diverse effect in the microbial pathogenesis and express a variety of pathogenic molecules including aebABCEG, HutA, cpsD and pPHDD1. Bacterial protein secretion system secretes enzymes and toxins from bacterial cytoplasm to the host membrane targeting the immune cells and promoting biofilm formation. However, as they enter, the host body expresses various immune molecules that interact to utilize the pathogen recognition receptors. Toxins are powerful molecules formed by a broad range of bacterial pathogens attacking host cells and playing key roles in the dialogue between host and pathogen. They are important virulence factors that are often enough to decide the outcome of the infection. Hence, a detailed view on the virulence molecules majorly exotoxins from various bacterial pathogenic strains that are necessary to understand the pathogenesis. This review focuses on bacterial toxins and various other virulence factors, which influence the pathogenesis in fish.

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“…Many lectins possessing various carbohydrate specificities have been purified from the hemolymph of bivalve mollusks and characterized, with emphasis on their biological properties [ 13 , 14 ]. In invertebrates, hemolymph lectins play an important role in protection against many pathogens, microbes, and environmental changes [ 15 , 16 , 17 ]. Additionally, many hemolymph lectins exhibit anti-cancer properties against various cancer cell lines that express globotriaosylceramides on their cell surface [ 18 ].…”

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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Anti-biofilm properties and immunological response of an immune molecule lectin isolated from shrimp Metapenaeus monoceros

Cited by 13 publications

References 64 publications

A C‐type lectin with antibacterial activity in weather loach, Misgurnus anguillicaudatus

A C‐type lectin with antibacterial activity in weather loach, Misgurnus anguillicaudatus

Pathogenic bacterial toxins and virulence influences in cultivable fish

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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