Epstein-Barr virus gp350/220 binding to the B lymphocyte C3d receptor mediates adsorption, capping, and endocytosis |
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| Authors: | J Tanner J Weis D Fearon Y Whang E Kieff |
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| Affiliation: | 1. Institute of Information Science, Beijing Jiaotong University, China;2. Beijing Key Laboratory of Advanced Information Science and Network Technology, China;3. Department of Computer Science, Beijing Jiaotong University, China;4. Department of Electrical & Computer Engineering, Rensselaer Polytechnic Institute, USA;1. Department of Pharmaceutics, School of Pharmacy, Shahid Beheshti University of Medical Sciences, Tehran, Iran;2. Nanotechnology Research Center, School of Pharmacy, Mashhad University of Medical Sciences, Mashhad, Iran;4. Biotechnology Research Center, Nanotechnology Research Center, School of Pharmacy, Mashhad University of Medical Sciences, Mashhad, Iran;1. National Laboratory of Pattern Recognition, Institute of Automation, Chinese Academy of Sciences, Beijing 100190, PR China;2. CAS Center for Excellence in Brain Science and Intelligence Technology, Chinese Academy of Sciences, Beijing 100190, PR China;3. University of Chinese Academy of Sciences, Beijing 100190, PR China;4. Department of Computer Science and Information Systems, Birkbeck College, London WC1E 7HX, United Kingdom |
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| Abstract: | The type 2 complement receptor, CR2, a B lymphocyte surface glycoprotein, is known to be a component of the EBV receptor. We now demonstrate that the major EBV outer membrane glycoprotein, gp350/220, is a highly specific ligand for CR2. EBV or beads coated with purified recombinant gp350/220 adsorb to normal B lymphocytes, cap with CR2, become endocytosed into vesicles, and are released into the cytoplasm. This is the first demonstration of herpesvirus glycoprotein-cell glycoprotein receptor interaction in viral adsorption and penetration. The capping of CR2 in response to virus, gp350/220-coated beads, or anti-CR2 monoclonal antibodies is associated with cocapping of surface immunoglobulin. Interaction between CR2 and surface immunoglobulin may be important in modulating the B cell activation that normally follows EBV infection or exposure to antigen. |
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