American Society for Microbiology, Journal of Virology, 2(96), 2022
DOI: 10.1128/jvi.01704-21
Full text: Unavailable
Herpesvirus UL34 homologs contain conserved amino-terminal domains that mediate vesicle formation through interactions with UL31 homologs during primary envelopment. UL34 homologs also comprise other domains adjacent to their membrane-anchoring regions, which differ in length, are variable in herpesviruses, and do not form distinguished secondary structures.