Retrieval of human cytomegalovirus glycoprotein B from the infected cell surface for virus envelopment

• Published in: Archives of virology Vol. 141; no. 3-4; pp. 557 - 572
• Main Authors: RADSAK, K, EICKMANN, M, MOCKENHAUPT, T, BOGNER, E, KERN, H, EIS-HÜBINGER, A, RESCHKE, M
• Format: Journal Article
• Language: English
• Published: Wien Springer 01-01-1996; New York, NY
• Subjects: Biological and medical sciences; Biological Transport; Biotin - metabolism; Cell Line; Cytomegalovirus - metabolism; Cytomegalovirus - physiology; Cytomegalovirus - ultrastructure; Fundamental and applied biological sciences. Psychology; Humans; Microbiology; Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains; Viral Envelope Proteins - metabolism; Virion - metabolism; Virology; Virus Assembly; Virus; Intracellular transport; Molecular processing; Herpesviridae; Virus replication cycle; Glycoproteins; Infected cell; Betaherpesvirinae; Virus envelope; Cell surface; Human cytomegalovirus
• ISSN: 0304-8608; 1432-8798
• DOI: 10.1007/BF01718317

Surface biotinylation of human cytomegalovirus (HCMV)-infected fibroblasts under pulse-chase conditions was used to define the cellular route of the dominant viral envelope glycoprotein gB into the cytoplasmic compartment of viral maturational envelopment. The results showed that a major fraction of gB was re-internalized from the infected cell surface prior to incorporation into the viral envelope. Viral particles carrying biotinylated gB were subsequently released into the culture medium. Viral release appeared to be inhibited in the presence of gB-specific antibody or when infected cultures were incubated at room temperature, but was not reduced by inhibitors of cellular glycoprotein transport. To our knowledge this is the first report describing that HCMV gB is retrieved from the infected cell surface prior to viral envelopment.