Key result
Hexon R188I mutation alters proinflammatory cytokine expression and protein conformation in pathogenic FAdV-4.
Why the study?
The key determinants for the different virulence of FAdV-4 strains have not been fully elucidated.
The role of hexon amino acid 188 in FAdV-4 virulence depends on the strain's genetic background, with mutations inducing conformational changes and altering cytokine expression in pathogenic but not nonpathogenic strains.
Hexon aa188 may guide FAdV-4 attenuation; leaves open cross-strain validation before vaccine or control applications.
HHS induced by FAdV-4 has caused huge economic losses to the poultry industry. The key determinants for the different virulence of FAdV-4 have not been fully elucidated. Here, we investigated the role of hexon aa188 in FAdV-4 strains with different virulence and showed that the role of hexon aa188 varies in FAdV-4 strains with different genetic contents. The hexon R188 may be the key amino acid for causing inclusion body hepatitis by the pathogenic FAdV-4 strain, and induction of HHS by FAdV-4 may need other viral cofactors. Moreover, the hexon R188I mutation greatly affected the expression of proinflammatory cytokines induced by the pathogenic strain CH/HNJZ/2015, but no significant difference was observed between the nonpathogenic strain ON1 and ON1 with hexon I188R mutation. We found that hexon aa188 mutation induced conformational changes to hexon protein in CH/HNJZ/2015 but not in ON1, which might be the underlying reason for the changing virulence.
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Wang et al. (2022) studied Fowl Adenovirus Serotype 4 (FAdV-4) infection. Hexon aa188 mutation vs. Wild-type strains was evaluated on Virulence, inclusion body hepatitis, and proinflammatory cytokine expression. The hexon R188I mutation in the pathogenic FAdV-4 strain CH/HNJZ/2015 altered proinflammatory cytokine expression and hexon protein conformation, whereas the I188R mutation in the nonpathogenic ON1 strain did not.
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