Roles and Biomedical Applications of Haemolymph Lectin

Kamei, Rana; Devi, O. Sandhyarani; Singh, Sorokhaibam Jibankumar; Singh, Senjam Sunil

doi:10.2174/1389201021666200730123330

Cited by 4 publications

(4 citation statements)

References 59 publications

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“…The MBL in chickens can be activated when they are exposed to chicken diseases (135). Lectins are effective for invertebrate and vertebrate cancerous cells, prompting biochemists to use them in histochemical and cytochemical research (136,137) as well as in human medicine (138)…”

Section: Role Of Lectinsmentioning

confidence: 99%

Role of Lectin in the Response of Aedes aegypti Against Bt Toxin

et al. 2022

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Aedes aegypti is one of the world’s most dangerous mosquitoes, and a vector of diseases such as dengue fever, chikungunya virus, yellow fever, and Zika virus disease. Currently, a major global challenge is the scarcity of antiviral medicine and vaccine for arboviruses. Bacillus thuringiensis var israelensis (Bti) toxins are used as biological mosquito control agents. Endotoxins, including Cry4Aa, Cry4Ba, Cry10Aa, Cry11Aa, and Cyt1Aa, are toxic to mosquitoes. Insect eradication by Cry toxin relies primarily on the interaction of cry toxins with key toxin receptors, such as aminopeptidase (APN), alkaline phosphatase (ALP), cadherin (CAD), and ATP-binding cassette transporters. The carbohydrate recognition domains (CRDs) of lectins and domains II and III of Cry toxins share similar structural folds, suggesting that midgut proteins, such as C-type lectins (CTLs), may interfere with interactions among Cry toxins and receptors by binding to both and alter Cry toxicity. In the present review, we summarize the functional role of C-type lectins in Ae. aegypti mosquitoes and the mechanism underlying the alteration of Cry toxin activity by CTLs. Furthermore, we outline future research directions on elucidating the Bti resistance mechanism. This study provides a basis for understanding Bti resistance, which can be used to develop novel insecticides.

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Section: Role Of Lectinsmentioning

confidence: 99%

Role of Lectin in the Response of Aedes aegypti Against Bt Toxin

et al. 2022

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“…An agglutinin named limulin was discovered in Limulus polyphemus, a sialic acid-binding lectin, playing a role in the host defense mechanism. Indian variety horseshoe crab, Carcinoscorpius rotundacauda contains sialic acid-binding lectin carcinoscorpin, which acts as an opsonizing agent 43 . Venomous arthropods are a rich source of bioactive compounds.…”

Section: Bioactive Compounds From Marine Arthropodamentioning

confidence: 99%

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2022

IJPSR

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Marine environment is an exceptional storehouse of novel bioactive natural products that are mainly found in invertebrates such as sponges, arthropods, annelids, molluscs, etc. This diversity has been the source of unique chemical compounds. A large portion of these natural compounds has been extracted from marine invertebrates. Marine invertebrates are rich sources of bioactive compounds and their biotechnological potential attracts scientific and economic interest worldwide. Marine invertebrates are extremely diverse, largely productive, untapped oceanic resources with chemically unique bioactive compounds. Marine natural products are generally secondary metabolites. The number of natural products isolated from marine organisms increases rapidly. Isolated compounds from marine invertebrates have been shown pharmacological activities. They are helpful for the invention and discovery of bioactive compounds, primarily for deadly diseases like cancer, an Acquired immunodeficiency syndrome (AIDS), osteoporosis and so forth. So marine life is fascinating and has great potential for the development of drugs. The present review aims to know about the bioactive compounds produced by marine invertebrates and their use and application in the pharmaceutical field. INTRODUCTION:Marine environment is the largest aquatic ecosystem on the planet with high salt content and the most important source of biodiversity in the world 1 . Marine habitats offer diverse ecosystems and serve as an excellent source of natural bioactive molecules, novel compounds, secondary metabolites and enzymes. Marine natural products have attracted attention to biologists and chemists all over the world for the last five decades 2 .

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“…Additionally, many hemolymph lectins exhibit anti-cancer properties against various cancer cell lines that express globotriaosylceramides on their cell surface [ 18 ]. The vast array of hemolymph lectins with the ability to recognize and inhibit the growth of various harmful microbes and cancer cells has prompted biochemists to study them for use medicinally and as antibacterial agents [ 19 ].…”

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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Roles and Biomedical Applications of Haemolymph Lectin

Cited by 4 publications

References 59 publications

Role of Lectin in the Response of Aedes aegypti Against Bt Toxin

Role of Lectin in the Response of Aedes aegypti Against Bt Toxin

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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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