Characterisation and physical mapping of an HSV-1 glycoprotein of approximately 115 X 10(3) molecular weight.
A type-specific monoclonal antibody that efficiently neutralises HSV-1 immunoprecipitated a glycoprotein of slightly greater electrophoretic mobility than gB from HSV-1 infected cells. Pulse and pulse chase experiments indicate that this glycoprotein is distinct from HSV-1 glycoproteins gB, gC, gD, and gE. This was confirmed by the reactions of LP11 with a series of intertypic recombinants the results of which indicate that the LP11 target gene is located close to the HSV-1 thymidine kinase gene between map positions 0.28 and 0.31. In accordance with the presently agreed convention this glycoprotein should be designated gH-1, and it may correspond to the 110K glycoprotein described by S. D. Showalter, M. Zweig, and B. Hampar (1981), Infect. Immun. 34, 684-692. Antibody LP11 inhibits plaque formation when added to cell monolayers after infection suggesting that gH-1 may play a role in cell-to-cell spread of infectious virus.
D000911:Antibodies, Monoclonal; D000936:Antigen-Antibody Complex; D001483:Base Sequence; D004262:DNA Restriction Enzymes; D004279:DNA, Viral / Q000235:genetics; D004591:Electrophoresis, Polyacrylamide Gel; D005814:Genes, Viral; D008970:Molecular Weight; D011995:Recombination, Genetic; D018139:Simplexvirus / Q000235:genetics*; D014759:Viral Envelope Proteins; D014764:Viral Proteins / Q000235:genetics / Q000302:isolation & purification*
D000911:Antibodies, Monoclonal; D000936:Antigen-Antibody Complex; D004279:DNA, Viral; D014759:Viral Envelope Proteins; D014764:Viral Proteins; C044200:glycoprotein H, herpes simplex virus type 1; D004262:DNA Restriction Enzymes