Immunological properties of an N-terminal fragment of herpes simplex virus type 1 glycoprotein D expressed in Escherichia coli

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Abstract
Summary The N-terminal fragment, comprising residues −5 to 55 of herpes simplex virus type 1 glycoprotein D was expressed as a β-galactosidase fusion protein inEscherichia coli. This gD-fusion protein reacts with monoclonal antibody LP14 directed against glycoprotein D of HSV. Antisera obtained after immunization of rabbits with purified gD-fusion protein react with HSV-1 gD in a Western blot and with N-terminal synthetic peptides of gD. In addition, these antisera are able to neutralize viral infectivity in vitro.