Epstein-Barr Virus Recombinant Lacking Expression of Glycoprotein gp150 Infects B Cells Normally but Is Enhanced for Infection of Epithelial Cells

AUTOR(ES)

Borza, Corina M.

FONTE

American Society for Microbiology

RESUMO

Glycoprotein gp150 is a highly glycosylated protein encoded by the BDLF3 open reading frame of Epstein-Barr virus (EBV). It does not have a homolog in the alpha- and betaherpesviruses, and its function is not known. To determine whether the protein is essential for replication of EBV in vitro, a recombinant virus which lacked its expression was made. The recombinant virus had no defects in assembly, egress, binding, or infectivity for B cells or epithelial cells. Infection of epithelial cells was, however, enhanced. The glycoprotein was sensitive to digestion with a glycoprotease that digests sialomucins, but no adhesion to cells that express selectins that bind to sialomucin ligands could be detected.

Documentos Relacionados

• Epstein-Barr Virus Lacking Glycoprotein gp42 Can Bind to B Cells but Is Not Able To Infect
• Glycoprotein 110, the Epstein-Barr virus homolog of herpes simplex virus glycoprotein B, is essential for Epstein-Barr virus replication in vivo.
• Glycoprotein gp110 of Epstein–Barr virus determines viral tropism and efficiency of infection
• Epstein-Barr Virus gH Is Essential for Penetration of B Cells but Also Plays a Role in Attachment of Virus to Epithelial Cells
• Epstein-Barr virus enters B cells and epithelial cells by different routes.