Infectivity and glycoprotein processing of herpes simplex virus type 1 grown in a ricin-resistant cell line deficient in N-acetylglucosaminyl transferase I

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Abstract
The replication of herpes simplex virus 1 (HSV-1) and viral glycoprotein processing in RicR14 cells, a mutant ricin-resistant cell line defective in N-acetylglucosaminyl transferase I activity, was investigated. In these cells, HSV-1(MP) and (F) replicated to yields very similar to those in parental hamster kidney BHK cells. The kinetics of HSV-1 adsorption in mutant and in parent cells was also essentially identical. Progeny virions from ricin-resistant and wild-type cells displayed comparable specific infectivities. In the mutant cells the efficiency of plating of progeny virus from both RicR14 and BHK cells was reduced. HSV-1(MP) failed to induce syncytia in RicR14 cells either in a plaque assay or after a high-multiplicity infection. The fully glycosylated forms of glycoproteins (gB, gC and gD) were totally absent, and only the partially glycosylated precursors (pgC, pgD and a triplet in the gB-gA region) accumulated in HSV-1-infected ricin-resistant cells and in herpesvirions made in these cells. Analysis of pronase glycopeptides from cells labeled with [14C]glucosamine showed a strong decrease of sialylated complex-type oligosaccharides and a dramatic accumulation of the neutral mannose-rich chains. The latter chains predominate in partially glycosylated precursors; the complex acidic chains predominate in the fully processed forms of HSV glycoproteins. Evidently host-cell N-acetylglucosaminyl transferase I participates in the processing of HSV glycoproteins and infectivity of herpesvirions does not necessarily require the mature form of gB. The absence of HSV-1(MP)-induced fusion in RicR14 cells is discussed.