Different evolutionary patterns of classical swine fever virus envelope proteins
2015
Li, Yan | Yang, Zexiao | Zhang, Mingwang
Classical swine fever virus (CSFV) is the causative agent of classical swine fever (CSF), which is a highly contagious disease of the domestic pig as well as wild boar. The proteins Erns, E1, and E2 are components of the viral envelope membrane. They are also implicated in virus attachment and entry, replication, and/or anti-immune response. Here, we studied the genetic variations of these envelope proteins in the evolution of CSFV. The results reveal that the envelope proteins underwent different evolutionary fates. In Erns and E1, but not E2, a number of amino acid sites experienced functional divergence. Furthermore, the diversification in Erns and E1 were generally episodic because the divergence-related changes of E1 have only occurred with the split between two major groups of CSFV and that of Erns have taken place with the division of one major group. The major divergence-related sites of Erns are located on one of the substrate-binding regions of RNase domain and C-terminal extension. These functional domains have been reported to block activation of the innate immune system and attachment and entry into host cells, respectively. Our results might shed some light on the divergent roles of the envelope proteins.
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