Immunological properties of an N-terminal fragment of herpes simplex virus type 1 glycoprotein D expressed in Escherichia coli (brief report)
The N-terminal fragment, comprising residues -5 to 55 of herpes simplex virus type 1 glycoprotein D was expressed as a beta-galactosidase fusion protein in Escherichia coli. This gD-fusion protein reacts with monoclonal antibody LP 14 directed against glycoprotein D of HSV. Antisera obtained after i...
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Veröffentlicht in: | Archives of virology 1988-01, Vol.103 (3-4), p.267-274 |
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Hauptverfasser: | , , , , , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | The N-terminal fragment, comprising residues -5 to 55 of herpes simplex virus type 1 glycoprotein D was expressed as a beta-galactosidase fusion protein in Escherichia coli. This gD-fusion protein reacts with monoclonal antibody LP 14 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. |
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ISSN: | 0304-8608 1432-8798 |
DOI: | 10.1007/BF01311098 |