Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
6138687 | Virology | 2016 | 5 Pages |
Abstract
Human herpesvirus 6 (HHV-6) glycoprotein B (gB) is an abundantly expressed viral glycoprotein required for viral entry and cell fusion, and is highly conserved among herpesviruses. The present study examined the function of HHV-6 gB cytoplasmic tail domain (CTD). A gB CTD deletion mutant was constructed which, in contrast to its revertant, could not be reconstituted. Moreover, deletion of gB cytoplasmic tail impaired the intracellular transport of gB protein to the trans-Golgi network (TGN). Taken together, these results suggest that gB CTD is critical for HHV-6 propagation and important for intracellular transportation.
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Authors
Nora F. Mahmoud, Chyntia Jasirwan, Satoshi Kanemoto, Aika Wakata, Bochao Wang, Yuuki Hata, Satoshi Nagamata, Akiko Kawabata, Huamin Tang, Yasuko Mori,