The immune-evasive proline-283 substitution in influenza nucleoprotein increases aggregation propensity without altering the native structure.

ABSTRACT: Nucleoprotein (NP) is a key structural protein of influenza ribonucleoprotein complexes and is central to viral RNA packing and trafficking. NP also determines the sensitivity of influenza to myxovirus resistance protein 1 (MxA), an innate immunity factor that restricts influenza replication. A few critical MxA-resistant mutations have been identified in NP, including the highly conserved proline-283 substitution. This essential proline-283 substitution impairs influenza growth, a fitness defect that becomes particularly prominent at febrile temperature (39°C) when host chaperones are depleted. Here, we biophysically characterize proline-283 NP and serine-283 NP to test whether the fitness defect is caused by the proline-283 substitution introducing folding defects. We show that the prolin

SUBMITTER: Yoon J 

PROVIDER: S-EPMC11029814 | biostudies-literature | 2024 Apr

REPOSITORIES: biostudies-literature