Harvey M. Friedman, M.D. (Division Chief)
Dr. Friedman is the Chief of the Infectious Diseases Division. One project examines the role of the herpes simplex virus complement receptor and Fc receptor in viral pathogenesis. Herpes simplex virus encodes glycoproteins that help the virus escape antibody- and complement-mediated attack. Herpes simplex virus glycoproteins gC functions as a receptor for complement component C3b. By binding C3b, gC acts to turn off complement activation. Herpes simplex virus glycoproteins gE and gI together function as a receptor for the Fc domain of IgG, and reduce the effectiveness of antibody in clearing virus infection. Current studies are aimed to determine whether blocking the function of these glycoproteins improves the ability of the host to clear herpes infection. Another project examines the role of herpes simplex virus glycoprotein gE in neuronal spread. This glycoprotein is essential for transport of virus within neurons. The mechanisms by which gE mediate neuronal spread are evaluated using mouse primary neurons in vitro and a mouse retinal eye infection model in vivo.
Judson KA, Lubinski JM, Jiang M, Chang Y, Eisenberg RJ, Cohen GH, Friedman HM. Blocking immune evasion as a novel approach for prevention and treatment of herpes simplex virus infection. J Virol 77:12639-12645, 2003.
Xiaoqing L, Lubinski JM, Friedman HM. Immunization Strategies to Block the Herpes Simplex Virus Type 1 IgG Fc Receptor. J. Virol 78:2562-2571, 2004.
Wang F, Tang W, McGraw HM, Bennett J, Enquist LW, Friedman HM. Herpes simplex virus type 1 glycoprotein E is required for axonal localization of capsid, tegument and membrane glycoproteins. J Virol 79:13362-72, 2005.
Hook LM, Lubinski JM, Jiang M, Pangburn MK, Friedman HM. Herpes simplex virus type 1 and 2 glycoprotein C prevents complement-mediated neutralization induced by natural IgM antibody. J Virol 80:4038-4046, 2006.