Herpes simplex virus type 1 glycoprotein E is not indispensable for viral infectivity.
A mutant of the herpes simplex virus type 1 Angelotti was isolated in which 87% of the coding region of glycoprotein E (gE) was deleted and replaced by a functional neomycin resistance gene of the Tn5 transposon. The mutant was characterized by restriction enzyme analyses and Southern blotting. Western blotting of proteins and immunofluorescence assays revealed that gE was completely absent and that the Fc receptor was not expressed in cells infected with the mutant. The fact that this mutant was viable and that it replicated to a slightly lower titer than did the wild-type virus suggests that the presence of gE is not a prerequisite of viral infectivity in tissue culture.
D002460:Cell Line; D004262:DNA Restriction Enzymes; D004251:DNA Transposable Elements; D009154:Mutation; D018139:Simplexvirus / Q000235:genetics / Q000472:pathogenicity*; D014759:Viral Envelope Proteins / Q000235:genetics / Q000502:physiology*; D014774:Virulence
D004251:DNA Transposable Elements; D014759:Viral Envelope Proteins; C044768:glycoprotein E, herpes simplex virus type 1; D004262:DNA Restriction Enzymes