Key result
Carboxy-terminal truncation of pestivirus E1 reduces Erns-E1 cleavage efficiency ~70% and increases uncleaved protein secretion.
Processing of the pestiviral glycoprotein precursor by SPase is ordered and depends on protein integrity for efficient cleavage.
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Highlights E1 C-terminus role in ordered SPase cleavage; leaves open relevance to pestivirus pathogenesis or interventions.
Mu et al. (2020) studied Pestivirus infection. E1 sequence truncation and mutation vs. Wild-type Erns-E1 was evaluated on Cleavage efficiency of Erns-E1 precursor. Carboxy-terminal truncation of the pestivirus E1 moiety reduced the cleavage efficiency of the Erns-E1 precursor to less than 30% of the wild-type level and increased secretion of uncleaved proteins.
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