Biological role of lectins: A review

Kumar, Kunal; Chandra, K Lalith Prakash; Sumanthi, J; Reddy, G. Sridhar; Shekar, P Chandra; Reddy, B Srikanth

doi:10.4103/0975-8844.99883

Cited by 60 publications

(32 citation statements)

References 15 publications

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“…Con A and UEA 1 has also been used as markers of parotid gland and mucoepidermoid carcinoma with either high or low/ intermediate grade of dysplasia respectively (Sobral et al, 2010). Jack fruit lectins (JFL) and peanut agglutinin (PNA) have been used for identification of various pathological stages of tumor progression in different oral mucosa lesions (Kumar et al, 2012). Above studies clearly suggest that lectins can be used to develop potential tools for cancer diagnosis and metastasis detection.…”

Section: Lectins For Identification Of Malignant Tumorsmentioning

confidence: 99%

Structure-function and application of plant lectins in disease biology and immunity

Mishra

Behura

Mawatwal

et al. 2019

Food and Chemical Toxicology

154

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A B S T R A C TLectins are proteins with a high degree of stereospecificity to recognize various sugar structures and form reversible linkages upon interaction with glyco-conjugate complexes. These are abundantly found in plants, animals and many other species and are known to agglutinate various blood groups of erythrocytes. Further, due to the unique carbohydrate recognition property, lectins have been extensively used in many biological functions that make use of protein-carbohydrate recognition like detection, isolation and characterization of glycoconjugates, histochemistry of cells and tissues, tumor cell recognition and many more. In this review, we have summarized the immunomodulatory effects of plant lectins and their effects against diseases, including antimicrobial action. We found that many plant lectins mediate its microbicidal activity by triggering host immune responses that result in the release of several cytokines followed by activation of effector mechanism. Moreover, certain lectins also enhance the phagocytic activity of macrophages during microbial infections. Lectins along with heat killed microbes can act as vaccine to provide long term protection from deadly microbes. Hence, lectin based therapy can be used as a better substitute to fight microbial diseases efficiently in future.

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Section: Lectins For Identification Of Malignant Tumorsmentioning

confidence: 99%

Structure-function and application of plant lectins in disease biology and immunity

Mishra

Behura

Mawatwal

et al. 2019

Food and Chemical Toxicology

154

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“…The omnipresence of lectins in biosphere plays a crucial role in diverse biological processes. Surprisingly due to their multifaceted properties, biological role of lectins is speculative (Kumar et al 2012) and they are a subject of intensive investigations (Lam & Ng 2011). They serve a role in various biological recognition phenomena including cell-cell interactions (Matsumura et al 2007), molecular markers of cell differentiation, drug targeting and pathological states (Hussain et al 1997;Singh et al 1999).…”

Section: Introductionmentioning

confidence: 99%

Antimicrobial activity and carbohydrate specificity of new mycelial lectins from Fusarium sp.

Singh

Thakur

2014

Biologia

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In the present study, ten Fusarium sp. were screened for the presence of lectins by hemagglutination assay using human and animal erythrocytes. Amongst them nine species, namely F. acuminatum, F. chlamydosporium, F. coeruleum, F. compactum, F. concolor, F. crookwellense, F. culmorum, F. decemcellulare and F. dimerum were found to possess lectin activity. Neuraminidase treatment to rabbit erythrocytes considerably augmented hemagglutination titre, but no such effect was observed with protease-treated erythrocytes. Lectins were tested for inhibition of hemagglutination activity against a panel of carbohydrates. Majority of the lectins were inhibited by L-fucose, D-galactose, bovine submaxillary mucin and dextran. γ-Globulin was inhibitory against lectins from F. acuminatum, F. chlamydosporium, F. compactum and F. culmorum at a concentration of >250 µg/mL, whereas bovine submaxillary mucin and porcine stomach mucin were observed to be strongest inhibitors of lectin from F. compactum with minimum inhibitory concentration of 7.18 µg/mL and 15.6 µg/mL, respectively. Most of the lectins displayed antimicrobial activity against Bacillus cereus, Escherichia coli, Staphylococcus aureus and Aspergillus niger. Lectins from F. chlamydosporium, F. culmorum and F. crookwellense have also exhibited antimicrobial activity against Candida albicans. These findings illustrate the significance of Fusarium sp. lectins in clinical applications.

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“…Según la clasificación de lectinas vegetales basada en análisis estructural y datos sobre homología secuencial evolucionaria, la lectina V-2 pertenece a la familia de lectinas de leguminosas o tipo L (Peumans et al, 2001;Kumar et al, 2012).…”

Section: Estudio De Homología Secuencial Y áRbol Filogenético De La Lunclassified

Determinación de la estructura primaria de la lectina V-2 de semillas de arveja (Pisum sativum L.) y su efecto antibacteriano en Staphylococcus aureus y Escherichia coli

Huambo

2017

Idesia

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Determinación de la estructura primaria de la lectina V-2 de semillas de arveja (Pisum sativum L.) y su efecto antibacteriano en Staphylococcus aureus y Escherichia coliDetermination of the primary structure of a lectin V-2 from pea (Pisum sativum L.) seeds and his antibacterial effect on Staphylococcus aureus and Escherichia coliAlberto Cáceres-Huambo 1 * RESUMENLa lectina V-2 aislada de semillas de Pisum sativum L. ("arveja") fue purificada mediante cromatografía de exclusión molecular en Sephadex G-75 y cromatografía líquida de alta precisión de fase reversa (HPLC). El análisis en SDS-PAGE de dos dimensiones demostró que la lectina es homogénea con un único spot proteico de ~ 14 kDa y un punto isoeléctrico de 7,5. Mediante espectrometría de masa (MALDI-TOF) fue confirmado el peso molecular de la lectina mostrando una masa de 14.662,0 Da. La secuencia completa de aminoácidos (estructura primaria) reveló que la lectina V-2 está compuesta de 128 aminoácidos. El estudio comparativo con otras lectinas, mostró que la lectina V-2 tiene mayor homología con la lectina de semillas de Cratylia mollis L.(91,4%), seguido por la lectina de semillas de Cratylia argentea (61,6%). De acuerdo al árbol filogenético, la lectina V-2 presenta una aproximación microevolutiva ~ 1.000 nucleótidos con la lectina de C. mollis. Asimismo, la lectina V-2 mostró acción antibacteriana sobre Escherichia coli y Staphylococcus aureus formando un halo inhibitorio de crecimiento en una concentración de 1 mg. Palabras clave: lectina, Pisum sativum, secuencia de aminoácidos, estructura primaria, efecto antibacteriano. ABSTRACT The lectin V-2 from Pisum sativum L. ("arveja") seeds was purified by Sephadex G-75 molecular exclusion chromatography and reverse phase high performance liquid chromatography (RP-HPLC). Two dimensional SDS-PAGE analyses demonstrated that

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Biological role of lectins: A review

Cited by 60 publications

References 15 publications

Structure-function and application of plant lectins in disease biology and immunity

Structure-function and application of plant lectins in disease biology and immunity

Antimicrobial activity and carbohydrate specificity of new mycelial lectins from Fusarium sp.

Determinación de la estructura primaria de la lectina V-2 de semillas de arveja (Pisum sativum L.) y su efecto antibacteriano en Staphylococcus aureus y Escherichia coli

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