Proteins Specified by Herpesvirus Saimiri: Purification and Properties of a Single Polypeptide which Elicits Virus-neutralizing Antibody

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Abstract
A virus-specified polypeptide of 160,000 MW (160K) was purified > 1000-fold from the soluble proteins present in the culture medium of owl monkey kidney cells productively infected with herpesvirus saimiri (HVS). Purified preparations of the 160K polypeptide gave rise to high titer precipitating and neutralizing antibodies in immunized rabbits, which cross-neutralized independent isolates of HVS (neutralization rate contstants, k, 3.8-4.8)and specifically precipitated the 160K polypeptide from extracts of cells infected with the homologous or heterologous strains of this virus. Antiserum to the 160K polypeptide of HVS also gave low (k = 0.02) levels of neutralization of the related herpesvirus ateles. Purified preparations of the 160K polypeptide were capable of removing most or all of the neutralizing antibody sera of squirrel monkeys with naturally acquired antibodies to HVS. The 160K polypeptide was previously shown to form part of the surface of enveloped virus particles. However, it is shown here that the 160K polypeptide is not extensively glycosylated in infected cells. The majority of glucosamine incorporation specific to HVS-infected cells was into 8 regions with apparent MW of 170K-220K, 125K-145K, 115K-120K, 83K-88K, 65K-75K, 52K-58K, 25K-27K and 12.5-13K. Although alternative cleaved or glycosylated forms of the 160K polypeptide may also be present on the virus particle or precipitating antibody to 160K and virus-neutralizing antibodies may not be identical, the inability to detect precipitating antibody to virus-induced proteins or glycoproteins other than the 160K polypeptide and the high titer of neutralizing antibody present in this serum provide reasonable evidence that it is the antibodies which react with the 160K polypeptide that are responsible for virus neutralization.

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