The high glycoprotein (gp300) of equine herpesvirus type 1 was found to have an , estimated by SDS-PAGE, of over 400000 and was confirmed as being a surface glycoprotein by I-labelling. In contrast to [H]glucosamine, gp300 showed very low levels of [H]mannose incoporation. The of gp300 showed no detectable change upon treatment of purified virus with -glycanase, and showed only a small change in virus-infected cells treated with tunicamycin. In addition, gp300 failed to bind the lectin concanavalin A. Taken together, these results indicate a lack of -linked carbohydrate on gp300. The major carbohydrate species were found to be composed primarily of -linked chains, as indicated by the sensitivity of the protein to monensin, to exoglycanase enzymes specific for sugars present in -linked chains and to mild alkaline borohydride treatment, which revealed three species of carbohydrate of of >10000, 2400 and 1100, respectively. Neuraminidase treatment and binding of lectin indicated the presence of α--acetylglucosamine and sialic acid as terminal sugars. Immunological cross-reactivity of gp300 with a high protein of equine herpesvirus type 4 was shown and it also exhibited a marked variation in the vaccine strain Rhinomune.


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