Key result
Three amino acid mutations in the capsid proteins Vp1 and Vp3 of Coxsackievirus B3 strain 28 were individually associated with increased viral stability at 37 °C.
Three specific amino acid mutations in the capsid proteins of Coxsackievirus B3 strain 28 increase its stability at 37 °C, though the less stable parental strain propagates better in receptor-rich cells.
These mutations enhance CVB3 stability at body temperature; hypothesis-generating for fitness trade-offs or pathogenesis in animal models.
Coxsackievirus B3 strain 28 (CVB3/28) is less stable at 37 °C than eight other CVB3 strains with which it has been compared, including four in this study. In a variant CVB3/28 population selected for increased stability at 37 °C, the capsid proteins of the stable variant differed from the parental CVB3/28 by two mutations in Vp1 and one mutation in Vp3, each of which resulted in altered protein sequences. Each of the amino acid changes was individually associated with a more stable virus. Competition between CVB3/28 and a more stable derivative of the strain showed that propagation of the less stable virus was favoured in receptor-rich HeLa cells.
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Carson et al. (2015) studied Coxsackievirus B3. Capsid amino acid mutations (Vp1 and Vp3) vs. Parental CVB3/28 strain was evaluated on Virus stability at 37 °C and propagation in HeLa cells. Three amino acid mutations in the capsid proteins Vp1 and Vp3 of Coxsackievirus B3 strain 28 were individually associated with increased viral stability at 37 °C.
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