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
Hauptverfasser: KOCKEN, C. H. M, GEERLIGS, H. J, BOS, C. A, AG, B, WEIJER, W. J, DRIJFHOUT, J. W, WELLING, G. W, WELLING-WESTER, S
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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.
ISSN:0304-8608
1432-8798
DOI:10.1007/BF01311098