title: Multifunctional role of β-1, 3 glucan binding protein purified from the haemocytes of blue swimmer crab Portunus pelagicus and in vitro antibacterial activity of its reaction product.
abstract: β-1, 3 glucan binding protein (β-GBP) was isolated from the haemocytes of blue swimmer crab, Portunus pelagicus and purified by laminarin coupled Sephadex G-100 affinity column chromatography. The purified β-GBP has the molecular mass of 100 kDa, confirmed by SDS-PAGE. The X-ray diffraction analysis of purified β-GBP indicates the crystalline nature of the protein and also the presence of single peak confirming the existence of β-glucan molecule. The results of agglutination assay showed that the purified β-GBP had the ability to agglutinate with yeast cell, Saccharomyces cerevisiae and mammalian erythrocytes. β-GBP can agglutinate with yeast cells at the concentration of 50 μg/ml. The phagocytic and encapsulation activity of purified β-GBP from P. pelagicus was determined with yeast cell S. cerevisiae and sepharose bead suspension respectively. This reveals that, β-GBP have the ability to detect the pathogen associated molecular patterns (PAMP) found on the surface of fungi and bacteria. The recognition of invading foreign substances and in the involvement of functional activities induces the activation of prophenoloxidase. This revealed that β-GBP play a major role in the innate immune system of crustaceans by stimulating the prophenoloxidase system. Moreover, it was obvious to note that β-GBP reaction product exhibited antibacterial and antibiofilm activity against Gram positive and Gram negative bacteria. This study concludes the functional aspects of β-GBP purified from P. pelagicus and its vital role in the stimulation of prophenoloxidase cascade during the pathogenic infection.
authors.affiliation: Crustacean Molecular Biology and Genomics Lab, Department of Animal Health and Management, Alagappa University, Science Block 4th Floor, Burma Colony, Karaikudi 630004, Tamil Nadu, India.
authors.forename: Mahalingam
authors.initials: M
authors.lastname: Anjugam
authors.affiliation: Crustacean Molecular Biology and Genomics Lab, Department of Animal Health and Management, Alagappa University, Science Block 4th Floor, Burma Colony, Karaikudi 630004, Tamil Nadu, India.
authors.forename: Arokiadhas
authors.initials: A
authors.lastname: Iswarya
authors.affiliation: Crustacean Molecular Biology and Genomics Lab, Department of Animal Health and Management, Alagappa University, Science Block 4th Floor, Burma Colony, Karaikudi 630004, Tamil Nadu, India. Electronic address: vaseeharanb@gmail.com.
authors.forename: Baskaralingam
authors.initials: B
authors.lastname: Vaseeharan
mesh_terms: D000372:Agglutination Tests; D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry / Q000276:immunology / Q000302:isolation & purification; D060829:Arthropod Proteins / Q000737:chemistry / Q000276:immunology / Q000302:isolation & purification / Q000502:physiology; D001419:Bacteria / Q000254:growth & development / Q000378:metabolism; D003386:Brachyura / Q000276:immunology / Q000378:metabolism; D002352:Carrier Proteins / Q000737:chemistry / Q000276:immunology / Q000302:isolation & purification / Q000502:physiology; D004912:Erythrocytes / Q000502:physiology; D006434:Hemocytes / Q000276:immunology / Q000378:metabolism; D037102:Lectins / Q000737:chemistry / Q000276:immunology / Q000302:isolation & purification / Q000502:physiology; D014442:Monophenol Monooxygenase / Q000378:metabolism; D010587:Phagocytosis; D012441:Saccharomyces cerevisiae / Q000502:physiology
chemical_list: D000900:Anti-Bacterial Agents; D060829:Arthropod Proteins; D002352:Carrier Proteins; D037102:Lectins; C037937:glucan-binding proteins; D014442:Monophenol Monooxygenase
keywords: Agglutination; Antibiofilm activity; Prophenoloxidase; β-1, 3 glucan binding protein