Physico-Chemical Characterization Of A Naturally Occurring Agglutinin In The Hemolymph Of The Larva Of Red Palm Weevil, Rhynchophorus Ferrugineus
Main Article Content
Abstract
The hemolymph of most invertebrates contains naturally occurring hemagglutinins with diverse specificities for erythrocytes. A natural agglutinin with high affinity for rabbit erythrocytes was detected in the hemolymph of the larva of the red palm weevil, Rhynchophorus ferrugineus. The HA titer can be ranked as rabbit > guinea pig = dog = horse > human B > human O = buffalo > goat = pig > human A = rat = mice = cow erythrocytes. Maximum hemagglutinin activity with rabbit erythrocytes was observed at pH 7.5 and temperature 30°C to 40°C. The hemagglutinability was calcium dependent and reversibly sensitive to EDTA. The HA activity of the larval hemagglutinin was inhibited by the glycoproteins, Porcine stomach mucin = Fetuin > Bovine thyroglobulin > Transferrin = Apotransferrin > Bovine submaxillary mucin and sugars, N-acetyl mannosamine = melibiose = α-lactose > D-galactosamine > N-acetyl-D-galactosamine = N-acetyl neuraminic acid. Reduction in HA titer with the sialidase treated rabbit erythrocytes revealed the sialic acid specificity of the agglutinin. Presence of a single agglutinin and its proteinaceous nature were unveiled by cross adsorption studies and treatment with denaturing agents respectively. Therefore, the preliminary description of the hemolymph agglutinin would offer ways to perform lectin purification from Rhynchophorus ferrugineus, the red palm weevil.
Downloads
Article Details
This work is licensed under a Creative Commons Attribution 4.0 International License.
References
Amirante, G. A. (1976). Production of heteroagglutinins in hemocytes of Leucophaea maderae, L. Experientia, 32 (4): 526-528.
Anderson, R. S., Day, N. K. B. & GOOD R. A. (1972). Specific hemagglutinin and a modulator of complement in cockroach hemolymph. Infect. Immunol., 5 (1): 55-59.
Ayaad, T. H. (2004). Isolation, characterization and N-terminal aminoacid sequence of lectin from plasma of Schistocerca gregaria. Efflatounia, 4: 9-22.
Basil Rose, M. R., Ravindranath, M. H. & Mercy, P. D. (2014). Physico-chemical characterization of a natural agglutinin from the hemolymph of a millipede Thyropygus descriptus. ISJ, 11 (1): 331-336.
Chai, L. Q., Tian, Y. Y., Yang, D. T., Wang, J. X. & Zhao, X. F. (2008). Molecular cloning and characterization of a C-type lectin from the cotton bollworm, Helicoverpa armigera. Dev. Comp. Immunol., 32 (1): 71-83.
Drif, L. & Brehelin, M. (1989). Agglutinin mediated immune recognition in Locusta migratoria (Insecta). J. Insect Physiol., 35: 729-736.
Fries, C. R. (1984). Protein hemolymph factors and their roles in invertebrate mechanisms: a review. In: Invertebrate blood, cells and serum factors. Vol. 6, (Cheng T.C., ed.), Plenum press, New York, 49-109.
Goldstein, I. J. & Hayes, C. E. (1978). The lectins: carbohydrate-binding of plants and animals. Adv. Carbohydr. Chem. Biochem., 35: 127-340.
Grubhoffer, L. & Matha, V. (1991). Characteristics of a new L-fucose and N-acetyl D-galactosamine specific lectin from the integument of Gallaria mellonella larva. Comp. Biochem. Physiol., 100 (1): 73-76.
Hakomori, S. (1973). Glycolipids of tumor cell membrane. Adv. Cancer. Res., 18: 265-315.
Hall, J. L. & Rowlands, D. T. (1974). Heterogeneity of lobster agglutinins. I. Purification and physicochemical characterization. Biochemistry, 13: 821–827.
Hapner, K. D. & Jermyn, M. A. (1981), Hemagglutinin activity in the hemolymph of Teleogryllus commodus (Walker). Insect Biochem., 11 (3): 287-295.
Ingram, G. A. & Molyneux, D. H. (1990). Lectins (hemagglutinins) in the hemolymph of Glossina fuscipes fuscipes: isolation, partial characterization, selected physico-chemical properties and carbohydrate-binding specificities. Insect Biochem., 20 (1): 13-27.
Jayalakshmi, M. (2005). Coconut pest Oryctes rhinoceros lectin: Nature, purification and ecophysiological significance. Ph. D. Thesis, Manonmanium Sundaranar University, Tirunelveli, India.
Kabir, S. R.., Islam, M. F., Alom, M. J., Zubair, M. A. & Absar, N. (2012). Purification, characterization of a snake guard seeds lectin with antitumor activity against Ehrlich ascites carcinoma cells in vivo in mice. Protein peptide. Lett., 19 (3): 360-368.
Kubo, T. & Natori, S. (1987). Purification and some properties of a lectin from the hemolymph of Periplaneta americana (American cockroach). Eur. J. Biochem., 168: 75-82.
Learnal-Sudhakar, G. R. (2014). Purification and characterization of three novel lectins from the marine shrimp Alpheus digitalis complex, the clam Villorita cyprinoids and the insect Dragon fly (nymph) Bradinopyga geminata. Ph.D. Thesis, Manonmanium Sundharanar University, Tirunelveli, India.
Mercy, P. D. & Ravindranath, M. H. (1992). An agglutinin with unique specificity for N-glycolyl sialic acid residues of thyroglobulin in the hemolymph of a marine crab Scylla serrata (Forskal). Experientia, 48 (5): 498-500.
Mercy, P. D. & Ravindranath, M. H. (1993). Purification and characterization of N-glycolyl neuraminic acid-specific lectin from Scylla serrata. Eur. J. Biochem., 215 (5): 697-704.
Minnick, M. F., Rupp, R. A. & Spence, K. D. (1986). A bacterial-induced lectin which triggers hemocyte coagulation in Manduca sexta. Biochem. Biophys. Res. Communications, 137 (2): 729-735.
Mohamed, H. A., Ingram, G. A. & Molyneux, D. H. (1992). Carbohydrate-binding specificities of anti-erythrocyte lectins (hemagglutinins) in Anopheles gambiae gut extracts and hemolymph. Med. Vet. Entomol., 6 (3): 217-224.
Molyneux, D. H., Takle, G., Ibrahim, A. B. & INGRAM, D. (1986). Insect immunity to Trypanosomatidae. Symp. Zool. Soc. London, 56: 117-144.
Naeen, A., Haque, S. & Khan, R. H. (2007). Purification and characterization of a novel beta-D-galactosides-specific lectin from Clitoria ternatea. Protein J., 26 (6): 403-413.
Nalini, M. & Kim Y. (2007). Biochemical characterization of C-type lectin in the diamondback moth, Plutella Xylostella (Yponomeutidae: Lepidoptera). J. Asia-Pacific Entomol., 10 (3): 229-237.
Paulova, M., Ticha, M., Entlicher, G., Kostir, J. V. & Kocourek. (1971). Studies on phytohemagglutinins: IX Metal content and activity of the hemagglutinin from the lentil (Lens esculenta moench). Biochemi. Biophysi. Acta, General Subjects, 252 (2): 388-395.
Pendland, J. C. & Boucius, D. G. (1986). Characteristics of a galactose-binding hemagglutinin (lectin) from hemolymph of Spodoptera exigua larvae. Dev. Comp. Immunol., 10: 477-487.
Pereira, M. E. A., Andrade, A. F. B. & Ribeiro, J. M. C. (1981). Lectins of distinct specificity in Rhodnius prolixus interact selectively with Trypanosoma cruzi. Science, 211: 597-599.
Qadir, S., Wani, I. H., Rafiq, S., Ganie, S. A., Masood, A. & Hamin, R. (2013). Evaluation of antimicrobial activity of a lectin isolated and purified from Indigofera heterantha. Adv. Biosci. Biotechnol., 4 (11) : 999.
Rananavare, H. D., Shantaram, K., Harwalkar, M. R. & Rahalkar, G. W. (1975). Methods for the laboratory rearing of red palm weevil, Rhynchophorus ferrugineus Oliv. J. Plantation Crops, 3 (2): 65-678.
Ravindranath, M. H. & Paulson, J. C. (1987). O-acetyl sialic acid specific lectin from the crab Cancer antennarius. Enzymol., 138: 520-527.
Richards, E. H., Ratcliffe, N. A. & Renwrantz, L. (1988), Isolation and characterization of a serum lectin from the giant stick insect, Extatosoma tiaratum. Insect. Biochem., 18: 691-700.
Stebbins, M. R. & HAPNER, K. D. (1985). Preparation and properties of hemagglutinin from hemolymph of Acrididae (grasshoppers). Insect. Biochem., 15: 451-462.
Tamilarasan, K., Annapoorani, A., Manikandan, R. & Janarthana, S. (2021). Isolation, characterization of galactose-specific lectin from Odoiporus longicollis and its antibacterial and anticancer activities’, International journal of Biological macromolecules, 183: 1119-1135.
Tian, Y. Y., Liu, Y., Zhao, X. F. & WANG, J. X. (2009). Characterization of a C-type lectin from the cotton bollworm, Helicoverpa armigera. Dev. Comp. Immunol., 33: 772-779.
Ugwu, S. O. & Apte, S. P. (2004). The effect of buffers on protein conformational stability. Pharma. Technol., 28 (3): 86–108.
Uhlenbruck, G. & Rothe, A. (1974). Biological alternations of membrane-bound glycoproteins by neuraminidase treatment. Behring Inst. Mitt. No. 55: 177-185.
Utarabhand, P. & Akkayanont, P. (1995). Purification of a lectin from Parkia javanica beans. Phytochem., 38 (2): 281-285.
Vasta, G. R., Quesenberry, M., Ahmed, H. & O'leary, Y, N. (1999). C-type lectins and galectins mediate innate and adaptive immune functions: their roles in the complement activation pathway. Dev. Comp. Immunol., 23 (4-5): 401-420.