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