AI Article Synopsis
- - The West Nile virus (WNV) subtype Kunjin, prevalent in Australia, has been studied, particularly the classical strain OR393, which contains two virus types: small plaque-forming (SP) and large plaque-forming (LP).
- - Differences in amino acids at specific positions in the E protein between SP and LP influence their growth rates and the ability to form plaques, with SP growing slightly faster and being glycosylated while LP is not.
- - The study reveals that small changes in the E protein can significantly alter the virulence of the virus, indicating that the LP variant exhibits enhanced neuroinvasive potential compared to SP and that the amino acid Phe in LP can mutate to Ser, aiding the
Article Abstract
The West Nile virus (WNV) subtype Kunjin virus (WNV) is endemic to Australia. Here, we characterized the classical WNV strain, OR393. The original OR393 strain contained two types of viruses: small plaque-forming virus (SP) and large plaque-forming virus (LP). The amino acid residues at positions 156 and 332 in the E protein (E and E) of SP were Ser and Lys (E), respectively, whereas those in LP were Phe and Thr (E). SP grew slightly faster than LP in vitro. The E protein of SP was N-glycosylated, whereas that of LP was not. Analysis using two recombinant single-mutant LP viruses, rKUNV-LP-E and rKUNV-LP-E, indicated that E enlarged plaques formed by LP, but E potently reduced them, regardless of the amino acid at E. rKUNV-LP-E showed significantly higher neuroinvasive ability than LP, SP, and rKUNV-LP-E. Our results indicate that the low-pathogenic classical WNV can easily change its pathogenicity through only a few amino acid substitutions in the E protein. It was also found that Phe at E of the rKUNV-LP-E was easily changed to Ser during replication in vitro and in vivo, suggesting that E is advantageous for the propagation of WNV in mammalian cells.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11359920 | PMC |
| http://dx.doi.org/10.3390/v16081237 | DOI Listing |
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