Site directed mutagenesis of the carboxyl terminus of human cytomegalovirus glycoprotein B leads to attenuation of viral growth in cell culture.
A viable human cytomegalovirus (HCMV) mutant was generated harbouring a glycoprotein B (gB) in which the carboxyl-terminal amino acids DRLRHR (aa 885-900) were changed to AALREE. Characterization of the phenotype of the recombinant virus revealed significant reduction of infectious progeny release and only moderate reduction of viral DNA replication indicating its diminished specific infectivity. This observation was in line with immunogold labeling of extracellular virions demonstrating that the amount of gB protein was markedly reduced in the envelope of the mutant virus. Our results suggest that the conserved carboxyl-terminus of the gB molecule is critical for HCMV maturation.
Strive
T
T
Pest Animal Control CRC, CSIRO Sustainable Ecosystems, Canberra, Australia.
Gicklhorn
D
D
Wohlfahrt
M
M
Kolesnikova
L
L
Eickmann
M
M
Borst
E
E
Messerle
M
M
Radsak
K
K
D000222:Adaptation, Physiological; D002478:Cells, Cultured; D003587:Cytomegalovirus / Q000235:genetics* / Q000472:pathogenicity; D005347:Fibroblasts; D006801:Humans; D016297:Mutagenesis, Site-Directed; D009154:Mutation; D014759:Viral Envelope Proteins / Q000737:chemistry / Q000235:genetics* / Q000502:physiology; D014779:Virus Replication
D014759:Viral Envelope Proteins; C040495:glycoprotein B, Simplexvirus