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Purification and functional characterization of lectin with phenoloxidase activity from the hemolymph of cockroach, Periplaneta americana
Author(s) -
Arumugam Ganesh,
Sreeramulu Bhuvaragavan,
Paulchamy Ramaraj,
Thangavel Sakthivel,
Sundaram Janarthanan
Publication year - 2017
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.21390
Subject(s) - lectin , hemolymph , biology , biochemistry , hemocyanin , periplaneta , ficolin , affinity chromatography , c type lectin , agglutinin , snake venom , masp1 , hemagglutination , cockroach , mannan binding lectin , venom , enzyme , antibody , serine protease , protease , ecology , immunology
Lectins also identified as hemagglutinins are multivalent proteins and on account of their fine sugar‐binding specificity play an important role in immune system of invertebrates. The present study was carried out on the hemolymph lectin of cockroach, Periplaneta americana with appropriate screening and purification to understand its molecular as well as functional nature. The lectin from the hemolymph was purified using ion‐exchange chromatography. The approximate molecular weight of purified lectin was 340kDa as determined by FPLC analysis. Rabbit erythrocytes were highly agglutinated with purified lectin from the hemolymph of P. americana . The hemagglutination activity (HA) of lectin was specifically inhibited by fucose. Glycoproteins also inhibited the HA activity of lectin. The amino acid sequences of the purified lectin revealed homology with amino acid sequences of allergen proteins from P. americana . Purified lectin showed the highest phenoloxidase activity against dopamine. The activators such as exogenous proteases and LPS from Escherichia coli and Salmonella minnesota significantly enhanced the PO activity of the purified lectin. Besides, the presence of copper and hemocyanin conserved domain in the purified lectin provided a new facet that insects belonging to the ancient clade such as cockroaches retained some traces of evolutionary resemblance in possessing lectin of ancient origin.