The nuclear inclusion a (NIa) protease of turnip mosaic virus (TuMV) cleaves amyloid-β

Hye Eun Han, Saravanan Sellamuthu, Bae Hyun Shin, Yong Jae Lee, Sungmin Song, Ji Seon Seo, In Sun Baek, Jeomil Bae, Hannah Kim, Yung Joon Yoo, Yong Keun Jung, Woo Keun Song, Pyung Lim Han, Woo Jin Park

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12 Scopus citations


Background:The nuclear inclusion a (NIa) protease of turnip mosaic virus (TuMV) is responsible for the processing of the viral polyprotein into functional proteins. NIa was previously shown to possess a relatively strict substrate specificity with a preference for Val-Xaa-His-Gln ↓, with the scissile bond located after Gln. The presence of the same consensus sequence, Val12-His-His-Gln15, near the presumptive α-secretase cleavage site of the amyloid-β (Aβ) peptide led us to hypothesize that NIa could possess activity against Aβ. Methodology/Principal Findings: Western blotting results showed that oligomeric as well as monomeric forms of Aβ can be degraded by NIa in vitro. The specific cleavage of Aβ was further confirmed by mass spectrometry analysis. NIa was shown to exist predominantly in the cytoplasm as observed by immunofluorescence microscopy. The overexpression of NIa in B103 neuroblastoma cells resulted in a significant reduction in cell death caused by both intracellularly generated and exogenously added Aβ. Moreover, lentiviral-mediated expression of NIa in APPsw/PS1 transgenic mice significantly reduced the levels of Aβ and plaques in the brain. Conclusions/Significance: These results indicate that the degradation of Aβ in the cytoplasm could be a novel strategy to control the levels of Aβ, plaque formation, and the associated cell death.

Original languageEnglish
Article numbere15645
JournalPLoS ONE
Issue number12
StatePublished - 2010


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