Binding of the human cytomegalovirus (HCMV) tegument protein UL69 to UAP56/URH49 is not required for efficient replication of HCMV.
The human cytomegalovirus (HCMV) tegument protein UL69 is important for efficient viral replication at low multiplicities of infection. Several molecular mechanisms by which UL69 contributes to HCMV replication have been proposed, including UL69's ability to interact with the mRNA export factors UAP56 and URH49 to facilitate the shuttling of viral mRNAs from the nuclei of infected cells. Using a UL69 viral mutant that is unable to bind UAP56 and URH49, we demonstrated that UL69's interaction with UAP56 or URH49 does not contribute to the growth phenotype associated with the UL69 deletion mutant.
Kronemann
Daniel
D
Department of Microbiology, University of Minnesota, 420 Delaware St. SE, 1060 Mayo Building, MMC196, Minneapolis, MN 55455, USA.
Hagemeier
Stacy R
SR
Cygnar
Dan
D
Phillips
Stacia
S
Bresnahan
Wade A
WA
D000818:Animals; D002460:Cell Line; D003587:Cytomegalovirus / Q000502:physiology*; D053487:DEAD-box RNA Helicases / Q000378:metabolism*; D017353:Gene Deletion; D054884:Host-Pathogen Interactions; D006801:Humans; D051379:Mice; D050505:Mutant Proteins / Q000378:metabolism; D011485:Protein Binding; D015534:Trans-Activators / Q000235:genetics / Q000378:metabolism*; D014779:Virus Replication
D050505:Mutant Proteins; D015534:Trans-Activators; C446019:pUL69 protein, Human herpesvirus 5; C498428:DDX39A protein, human; C487886:DDX39B protein, human; D053487:DEAD-box RNA Helicases