GLYCOPROTEIN-H (GLL GP108) AND GLYCOPROTEIN-L FORM A FUNCTIONAL COMPLEX WHICH PLAYS A ROLE IN PENETRATION, BUT NOT IN ATTACHMENT, OF BOVINEHERPESVIRUS-1/

Citation
Sv. Littelvandenhurk et al., GLYCOPROTEIN-H (GLL GP108) AND GLYCOPROTEIN-L FORM A FUNCTIONAL COMPLEX WHICH PLAYS A ROLE IN PENETRATION, BUT NOT IN ATTACHMENT, OF BOVINEHERPESVIRUS-1/, Journal of General Virology, 77, 1996, pp. 1515-1520
Citations number
21
Categorie Soggetti
Virology,"Biothechnology & Applied Migrobiology
Journal title
ISSN journal
00221317
Volume
77
Year of publication
1996
Part
7
Pages
1515 - 1520
Database
ISI
SICI code
0022-1317(1996)77:<1515:G(GAGF>2.0.ZU;2-5
Abstract
The glycoproteins of bovine herpesvirus 1 (BHV-1) play important roles in the interactions between virions and target cells. A 108 kDa glyco protein, designated gII or gp108, has been identified by two different panels of monoclonal antibodies, The gII- and gp108-specific monoclon al antibodies were shown to react with the same protein, which was ide ntified by N-terminal sequencing as the homologue of herpes simplex vi rus type 1 (HSV-1) gH. When BHV-1 gH was purified by immunoadsorbent c hromatography, gL was co-purified. The gH-gL complex induced the produ ction of antibodies that neutralized virus infectivity and inhibited v irus penetration, Affinity-purified gH-gL did prevent penetration, but not attachment of BHV-1, which suggests that the gH-gL complex is ess ential for penetration of BHV-1 into susceptible cells.