Structural highlights
Function
S4YYB7_USUV Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.[ARBA:ARBA00003504] Serine protease subunit NS2B: Required cofactor for the serine protease function of NS3.[PROSITE-ProRule:PRU00859]
Publication Abstract from PubMed
The mosquito-borne flavivirus Usutu virus (USUV) has recently emerged in birds and humans in Europe. Symptoms of a USUV infection resemble those of West Nile virus (WNV); further, the close antigenic relationship of domain III (DIII) of the USUV and WNV envelope (E) proteins has prevented the development of a reliable serological test to distinguish USUV from WNV. To begin to address this deficiency, we identified ten different sequence groups of DIII from 253 complete and 80 partial USUV genome sequences. We solved the DIII structures of four groups, including that of the outlying CAR-1969 strain, which shows an atypical DIII structure. Structural comparisons of the USUV DIII groups and the DIII of WNV bound to the neutralizing antibody E16 revealed why the E16 failed to neutralize all USUV strains tested except for USUV CAR-1969. The analyses allowed predictions to be made to engineer an antibody specific for USUV CAR-1969.
Structural and antigenic investigation of Usutu virus envelope protein domain III.,Josephine Schoenenwald AK, Pletzer M, Skern T Virology. 2020 Sep 28;551:46-57. doi: 10.1016/j.virol.2020.09.002. PMID:33011522[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Josephine Schoenenwald AK, Pletzer M, Skern T. Structural and antigenic investigation of Usutu virus envelope protein domain III. Virology. 2020 Sep 28;551:46-57. doi: 10.1016/j.virol.2020.09.002. PMID:33011522 doi:http://dx.doi.org/10.1016/j.virol.2020.09.002
