Journal
MICROBIOLOGY AND IMMUNOLOGY
Volume 65, Issue 11, Pages 492-504Publisher
WILEY
DOI: 10.1111/1348-0421.12934
Keywords
bornavirus; bud23; chromosomal tethering; host-viral interaction; proximity-dependent biotinylation; RNA methyltransferase
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Funding
- Ministry of Education, Culture, Sports, Science and Technology (MEXT) KAKENHI [16H06429, 16K21723, 16H06430]
- Japan Society for the Promotion of Science (JSPS) KAKENHI [19K22530, 20H05682]
- JSPS Core-to-Core Program
- Joint Usage/Research Center Program on inFront, Kyoto University
- Grants-in-Aid for Scientific Research [19K22530, 20H05682, 16H06430] Funding Source: KAKEN
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BoDV-1 utilizes vRNPs to maintain nuclear infection by tethering them onto host chromosomes. TRMT112 interacts with BoDV-1 L at the RNA-dependent RNA polymerase domain, along with BUD23, mediating the chromosomal tethering of BoDV-1 vRNPs.
Persistent intranuclear infection is an uncommon infection strategy among RNA viruses. However, Borna disease virus 1 (BoDV-1), a nonsegmented, negative-strand RNA virus, maintains viral infection in the cell nucleus by forming structured aggregates of viral ribonucleoproteins (vRNPs), and by tethering these vRNPs onto the host chromosomes. To better understand the nuclear infection strategy of BoDV-1, we determined the host protein interactors of the BoDV-1 large (L) protein. By proximity-dependent biotinylation, we identified several nuclear host proteins interacting with BoDV-1 L, one of which is TRMT112, a partner of several methyltransferases (MTases). TRMT112 binds with BoDV-1 L at the RNA-dependent RNA polymerase domain, together with BUD23, an 18S ribosomal RNA MTase and 40S ribosomal maturation factor. We then discovered that BUD23-TRMT112 mediates the chromosomal tethering of BoDV-1 vRNPs, and that the MTase activity is necessary in the tethering process. These findings provide us a better understanding on how nuclear host proteins assist the chromosomal tethering of BoDV-1, as well as new prospects of host-viral interactions for intranuclear infection strategy of orthobornaviruses.
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