Alteration of a Second Putative Fusion Peptide of Structural Glycoprotein E2 of Classical Swine Fever Virus Alters Virus Replication and Virulence in Swine.

ABSTRACT: E2, the major envelope glycoprotein of classical swine fever virus (CSFV), is involved in several critical virus functions, including cell attachment, host range susceptibility, and virulence in natural hosts. Functional structural analysis of E2 based on a Wimley-White interfacial hydrophobicity distribution predicted the involvement of a loop (residues 864 to 881) stabilized by a disulfide bond (⁸⁶⁹CKWGGNWTCV⁸⁷⁸, named FPII) in establishing interactions with the host cell membrane. This loop further contains an ⁸⁷²GG⁸⁷³ dipeptide, as well as two aromatic residues (⁸⁷¹W and ⁸⁷⁵W) accessible to solvent. Reverse genetics utilizing a full-length infectious clone of the highly virulent CSFV strain Brescia (BICv) was used to eva

SUBMITTER: Holinka LG 

PROVIDER: S-EPMC5105664 | biostudies-literature | 2016 Nov

REPOSITORIES: biostudies-literature