ArticlemBio2026
The EP424R protein of African swine fever virus functions as a 2'-O-methyltransferase and plays an important role in viral replication.
Article in mBio, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
African swine fever (ASF) is a highly pathogenic infectious disease that poses a serious threat to the pig farming industry worldwide. Currently, there are no effective vaccines and drugs. The 5' cap structure of messenger RNAs (mRNAs) is a critical modification that is found in all eukaryotic organisms and many viruses. This modification improves mRNA stability by protecting it from cleavage by 5' to 3' exonuclease, thus facilitating efficient translation. The African swine fever virus (ASFV) NP868R protein (pNP868R) has 5'-triphosphatase (TPase), guanylyltransferase (GTase), and guanine-N7-methyltransferase (MTase) activities, endowing the viral transcripts with a 7-methylguanosine RNA cap (m IMPORTANCE: 2'-O-ribose methyltransferases (2'-O-MTases) play a vital role in cellular processes of eukaryotes and in the replication of many viruses. However, these enzymes in the African swine fever virus (ASFV) remain uncharacterized. Our study revealed that the EP424R protein (pEP424R) of ASFV exhibits 2'-O-MTase activity during viral replication and is crucial for ASFV replication. Notably, this function is partially dependent on its methyltransferase activity. These findings increase our understanding of the transcriptional capping mechanism of ASFV and provide new insights for developing antiviral drugs targeting African swine fever (ASF).
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