TY - JOUR
T1 - Herpes simplex virus IgG Fc receptors induced using recombinant adenovirus vectors expressing glycoproteins E and I
AU - Hanke, Tomas
AU - Graham, Frank L.
AU - Lulitanond, Viraphong
AU - Johnson, David C.
N1 - Funding Information:
We thank Margaret Frame, Nigel Stow, and Patricia Spear for gifts of monoclonal antibodies. John Rudy provided invaluable technical assistance. We are indebted to Harvey Friedman and Tony Minson for sharing unpublished results. Support for this research was provided by grants from the Medical Research Council of Canada and the National Cancer Institute of Canada. D.C.J. is a research scholar and F.L.G. IS a Terry Fox fellow of the National Cancer Institute of Canada.
PY - 1990/8
Y1 - 1990/8
N2 - Evidence has been presented that herpes simplex virus (HSV) immunoglobulin (IgG) Fc receptors are composed of a complex of two glycoproteins, gE and gl. In previous studies, cells infected with HSV-1 mutants lacking either gE or gl bound lower levels of soluble IgG than cells infected with wild-type viruses suggesting that both gE and gl were required for IgG binding. We have reevaluated the Fc receptor activity of these mutants using a more sensitive assay involving IgG-coated erythrocytes and have found that cells infected with a gE- mutant HSV-1 did not bind IgG-coated erythrocytes whereas cells infected with a gl- mutant retained some Fc binding activity. To further study HSV-induced Fc receptors recombinant adenovirus vectors expressing gE or gl were constructed. Cells expressing gE alone bound both soluble IgG and IgG-coated red cells, although the binding was consistently lower than that observed with HSV-infected cells or cells expressing both gE and gl. Cells expressing only gl were unable to bind either soluble IgG or IgG-coated erythrocytes. These results support the conclusion that both gE and gl are required for full Fc receptor activity, although gE alone can bind IgG to a lesser extent.
AB - Evidence has been presented that herpes simplex virus (HSV) immunoglobulin (IgG) Fc receptors are composed of a complex of two glycoproteins, gE and gl. In previous studies, cells infected with HSV-1 mutants lacking either gE or gl bound lower levels of soluble IgG than cells infected with wild-type viruses suggesting that both gE and gl were required for IgG binding. We have reevaluated the Fc receptor activity of these mutants using a more sensitive assay involving IgG-coated erythrocytes and have found that cells infected with a gE- mutant HSV-1 did not bind IgG-coated erythrocytes whereas cells infected with a gl- mutant retained some Fc binding activity. To further study HSV-induced Fc receptors recombinant adenovirus vectors expressing gE or gl were constructed. Cells expressing gE alone bound both soluble IgG and IgG-coated red cells, although the binding was consistently lower than that observed with HSV-infected cells or cells expressing both gE and gl. Cells expressing only gl were unable to bind either soluble IgG or IgG-coated erythrocytes. These results support the conclusion that both gE and gl are required for full Fc receptor activity, although gE alone can bind IgG to a lesser extent.
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U2 - 10.1016/0042-6822(90)90507-N
DO - 10.1016/0042-6822(90)90507-N
M3 - Article
C2 - 2164721
AN - SCOPUS:0025280274
SN - 0042-6822
VL - 177
SP - 437
EP - 444
JO - Virology
JF - Virology
IS - 2
ER -