Comparative study of potyvirid NIa proteases and their cleavage sites

Abstract

Nuclear inclusion a protease (NIaPro), a major protease of potyvirids, processes its cognate viral polyprotein at distinct cleavage sites. Although Potyviridae is the largest family of the realm Riboviria, the individual NIaPro enzymes and their cleavage sites are believed to be species-specific. In the present study, the NIaPro amino acid sequences of 165 potyvirids of 10 genera and their 1154 cleavage sites were compared to understand their genus/species-specificity and functional regulation. Of these, the NIaPro of macluraviruses, maintains a constant length of 217 amino acids, while those of other genera allow variation. In particular, poaceviruses exhibited a broad range of NIaPro amino acid sequence lengths. Alignment of 162 NIaPro amino acid sequences showed that the N- and C-terminal regions allow variations, while the central region, with the catalytic triad and S1 subsite, are highly conserved. NIaPro cleavage sites are composed of seven amino acids (heptapeptide) denoted as P6-P5-P4-P3-P2-P1/P1’. A survey of 1154 cleavage sites showed that the P1 position is predominantly occupied by Gln/Glu, as is seen in picornaviruses. The P6 (Glu), P4 (Val/Cys/Gln), P2 (His/Tyr/Leu), and P1’ (Ser/Ala/Gly/Met) positions are predominantly occupied by genus-specific residues, while P5 and P3 are not genus-specific. The 6K2-VPg and VPg-NIaPro junctions possess Glu at the P1 position in order to maintain latency.

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Acknowledgements

Author SNP thanks the Science and Engineering Research Board (SERB) for fellowship support.

Funding

This work was funded by the Science and Engineering Research Board (SERB), Government of India, under project no. CRG/2018/002106.

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SNP and TJ designed this study. Sequence retrieval and analysis were performed by SNP and RS. SNP wrote the manuscript, and RS and TJ edited the manuscript.

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Correspondence to Jebasingh Tennyson.

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Palani, S.N., Sankaranarayanan, R. & Tennyson, J. Comparative study of potyvirid NIa proteases and their cleavage sites. Arch Virol 166, 1141–1149 (2021). https://doi.org/10.1007/s00705-021-04997-0

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