THE EXPRESSION OF THE PROTEINS OF EQUINE HERPESVIRUS-1 WHICH SHARE HOMOLOGY WITH HERPES-SIMPLEX VIRUS-1 GLYCOPROTEIN-H AND GLYCOPROTEIN-L

Several expression systems were used in studies aimed at characterizin g the equine herpesvirus 1 (EHV-1) glycoprotein H and L homologues of HSV-1 (EHV-1 gH and gL) and the products were compared to the authenti c proteins synthesized in virus infected cells. Using an in vitro tran scription/translation system two gH species were detected (an unproces sed 89 kDa and a processed 116 kDa product). Three low molecular weigh t proteins were found in the case of gL (21.8 kDa, 22.9 kDa and 26.9 k Da) and these showed a slight reduction in mobility on the addition of microsomal membranes to the reactions. A gL fusion protein was produc ed in pGEX-2T, expression being confirmed by Western blotting using a gl-specific antiserum raised against a peptide incorporating the 13 ca rboxyl terminal amino acids of the protein. A gH specific peptide anti serum precipitated both gH and two smaller proteins from EHV-1 infecte d cells thought to be two forms of gL. Insect cells infected with gH o r gL baculovirus recombinants were used to vaccinate C3H (H-2(k)) mice . Some protection against EHV-1 infection was conferred to the gH inoc ulated mice. The results will enable further studies on the importance of the gH and gL interaction in the pathogenesis of EHV-1 to be evalu ated and their potential in contributing to a subunit vaccine to be as sessed.