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2024-4-22 13:32:05

Chan JJ, Tang YS, Lo CY, Shaw PC. Functional Importance of the Hydrophobic Residue 362 in Influenza A PB1 Subunit. Viruses. 2023 Jan 30;15(2):396
submited by kickingbird at Mar, 1, 2023 13:40 PM from Viruses. 2023 Jan 30;15(2):396

PB1, acting as the catalytic subunit of the influenza polymerase, has numerous sequentially and structurally conserved regions. It has been observed that the slight modification of residues in PB1 would greatly affect the polymerase activity and even host adaptation ability. Here, we identified a critical residue, 362M, on the polymerase activity and virus replication. By means of the minireplicon assay, we assured the importance of the hydrophobicity of PB1 362, and the possibility that the size and charge of the side chain might directly interfere with the polymerase function. We also proposed a hydrophobic core between the PA-arch and the PB1 β-hairpin motifs and showed the importance of the core to the polymerase function.

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