Mutation of a highly conserved isoleucine residue in loop 2 of several β-coronavirus macrodomains indicates that enhanced ADP-ribose binding is detrimental for replication.

doi:10.1128/jvi.01313-24

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Article

Mutation of a highly conserved isoleucine residue in loop 2 of several β-coronavirus macrodomains indicates that enhanced ADP-ribose binding is detrimental for replication.

Journal of virology - 19 Nov 2024

Kerr Catherine M, Pfannenstiel Jessica J, Alhammad Yousef M, O'Connor Joseph J, Ghimire Roshan, Shrestha Rakshya, Khattabi Reem, Saenjamsai Pradtahna, Parthasarathy Srivatsan, McDonald Peter R, Gao Philip, Johnson David K, More Sunil, Roy Anuradha, Channappanavar Rudragouda, Fehr Anthony R

Abstract excerpt

All coronaviruses (CoVs) encode for a conserved macrodomain (Mac1) located in non-structural protein 3. Mac1 is an ADP-ribosylhydrolase that binds and hydrolyzes mono-ADP-ribose from target proteins. Previous work has shown that Mac1 is important for virus replication and pathogenesis. Within Mac1, there are several regions that are highly conserved across CoVs, including the glycine-isoleucine-phenylalanine...

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PMID: 39387584
DOI: 10.1128/jvi.01313-24
PMCID: PMC11575489

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