Lectin-dependent recognition of foreign cells by hemocytes of the mussel, Mytilus edulis |
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| Authors: | P Mullainadhan L Renwrantz |
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| Affiliation: | 1. Department of Entomology and Plant Pathology, Oklahoma State University, Stillwater, OK 74078, USA;2. Faculty of Life Science and Technology, Kunming University of Science and Technology, Kunming, Yunnan 650500, PR China;3. Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK 74078, USA;4. School of Life Sciences, Fudan University, Shanghai 200433, PR China;5. Division of Molecular Biology and Biochemistry, University of Missouri-Kansas City, Kansas City, MO 64110, USA;1. Department of Characterization, Quality and Security, Institute of Food Science Technology and Nutrition (ICTAN-CSIC), Jose Antonio Novais 10, Madrid 28040, Spain;2. Unit Service of Analytical Techniques, Instrumentation and Microbiology (USTA), Institute of Food Science Technology and Nutrition (ICTAN-CSIC), Madrid, Spain;1. College of Food and Biological Engineering, Jimei University, Xiamen, Fujian Province, 361021, China;2. Hefei National Laboratory for Physical Sciences at Microscale, CAS Key Laboratory of Innate Immunity and Chronic Disease, School of Life Sciences and Medical Center, University of Science & Technology of China, Hefei, Anhui Province, 230007, China;3. Fujian Collaborative Innovation Center for Exploitation and Utilization of Marine Biological Resources, Xiamen, Fujian Province, 361100, China;1. Department of Marine Life Sciences & Fish Vaccine Research Center, Jeju National University, Jeju Self-Governing Province, 63243, Republic of Korea;2. Department of Chemistry, University of Colombo, Colombo 03, Sri Lanka |
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| Abstract: | Phagocytosis of human erythrocytes (rbc) by hemocytes of the mussel Mytilus edulis was found to be influenced by four heterologous lectins. The effects were examined in the absence of Ca++ ions under three experimental conditions: when the lectins were bound to 1) both hemocytes and rbc, 2) only hemocytes, but not to rbc, and 3) only rbc, but not to hemocytes. The lectins used included: albumen gland agglutinin from Helix pomatia (HPA), wheat germ agglutinin (WGA), Ricinus-120 (Ric-120) and Concanavalin-A (Con A). HPA, WGA and Ric-120, for which both hemocytes and A-rbc possess receptors, strongly enhanced uptake of A-rbc. This lectin-mediated phagocytosis was abolished by addition of specific sugars either to lectin-pretreated rbc (HPA, WGA) or to a pretreated hemocyte monolayer (Ric-120); this indicated the stimulation of phagocytosis by the binding of lectin to carbohydrate determinants at the surface of hemocytes and target cells. On the other hand, HPA which binds to hemocytes, but not to O-rbc, did not influence phagocytosis of these rbc; and Con A which binds to A-rbc, but not to hemocytes, also failed to stimulate phagocytosis. These findings reveal the importance of carbohydrate determinants on the surface of hemocytes as well as on target cells in recognition and in lectin-mediated phagocytosis of foreign cells by Mytilus hemocytes. |
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