a gammaherpesvirus complement regulatory protein promotes initiation of infection by activation of protein kinase aktpkbgammaherpesvirus补充监管蛋白促进通过激活蛋白激酶aktpkb感染起始.pdfVIP

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a gammaherpesvirus complement regulatory protein promotes initiation of infection by activation of protein kinase aktpkbgammaherpesvirus补充监管蛋白促进通过激活蛋白激酶aktpkb感染起始.pdf

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a gammaherpesvirus complement regulatory protein promotes initiation of infection by activation of protein kinase aktpkbgammaherpesvirus补充监管蛋白促进通过激活蛋白激酶aktpkb感染起始

A Gammaherpesvirus Complement Regulatory Protein Promotes Initiation of Infection by Activation of Protein Kinase Akt/PKB 1 2 3 4 1 Beatrix Steer , Barbara Adler , Stipan Jonjic , James P. Stewart , Heiko Adler * ¨ 1The Institute of Molecular Immunology, Clinical Cooperation Group Hematopoietic Cell Transplantation, Helmholtz Zentrum Munchen - German Research Center for Environmental Health, Munich, Germany, 2 Max von Pettenkofer-Institute, Ludwig-Maximilians-University Munich, Munich, Germany, 3 Department of Histology and Embryology, Faculty of Medicine, University of Rijeka, Rijeka, Croatia, 4 Centre for Comparative Infectious Diseases, Department of Medical Microbiology, University of Liverpool, Liverpool, United Kingdom Abstract Background: Viruses have evolved to evade the host’s complement system. The open reading frames 4 (ORF4) of gammaherpesviruses encode homologs of regulators of complement activation (RCA) proteins, which inhibit complement activation at the level of C3 and C4 deposition. Besides complement regulation, these proteins are involved in heparan sulfate and glycosaminoglycan binding, and in case of MHV-68, also in viral DNA synthesis in macrophages. Methodology/Principal Findings: Here, we made use of MHV-68 to study the role of ORF4 during infection of fibroblasts. While attachment and penetration of virions lacking the RCA protein were not affected, we observed a delayed delivery of the viral genome to the nucleus of infected cells. Analysis of the phosphorylation status of a variety of kinases revealed a significant reduction in phosphorylation of the protein ki