Identification and characterization of pseudorabies virus glycoprotein gM as a nonessential virion component.
Sequence analysis within BamHI fragment 3 of the pseudorabies virus (PrV) genome revealed an open reading frame homologous to the UL10 gene of herpes simplex virus. A rabbit antiserum directed against a synthetic oligopeptide representing the carboxy-terminal 18 amino acids of the predicted UL10 product recognized a major 45-kDa protein in lysates of purified Pr virions. In addition, a second protein of 90 kDa which could represent a dimeric form was observed. Enzymatic deglycosylation showed that the PrV UL10 protein is N glycosylated. Therefore, it was designated PrV gM according to its homolog in herpes simplex virus. A PrV mutant lacking ca. 60% of UL10 coding sequences was able to productively replicate on noncomplementing cells, demonstrating that PrV gM is not required for viral replication in cell culture. However, infectivity of the mutant virus was reduced and penetration was delayed, indicating a modulatory role of PrV gM in the initiation of infection.
Dijkstra
J M
JM
Institute of Molecular and Cellular Virology, Friedrich Loeffler Institutes, Federal Research Centre for Virus Diseases of Animals, Germany.
Visser
N
N
Mettenleiter
T C
TC
Klupp
B G
BG
D000595:Amino Acid Sequence; D000818:Animals; D002874:Chromosome Mapping; D016679:Genome, Viral; D011558:Herpesvirus 1, Suid / Q000235:genetics* / Q000378:metabolism; D008562:Membrane Glycoproteins / Q000235:genetics; D008969:Molecular Sequence Data; D016366:Open Reading Frames / Q000235:genetics; D011817:Rabbits; D014759:Viral Envelope Proteins / Q000235:genetics*; D014771:Virion / Q000235:genetics* / Q000378:metabolism
D008562:Membrane Glycoproteins; D014759:Viral Envelope Proteins