Effect of specific amino acid substitutions in the putative fusion peptide of structural glycoprotein E2 on Classical Swine Fever Virus replication

Abstract E2, along with Erns and E1, is an envelope glycoprotein of Classical Swine Fever Virus (CSFV). E2 is involved in several virus functions: cell attachment, host range susceptibility and virulence in natural hosts. Here we evaluate the role of a specific E2 region,818 CPIGWTGVIEC828 , contain...

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Bibliographic Details
Published in:	Virology (New York, N.Y.) Vol. 456; pp. 121 - 130
Main Authors:	Fernández-Sainz, I.J, Largo, E, Gladue, D.P, Fletcher, P, O’Donnell, V, Holinka, L.G, Carey, L.B, Lu, X, Nieva, J.L, Borca, M.V
Format:	Journal Article
Language:	English
Published:	United States Elsevier Inc 01-05-2014
Subjects:	60 APPLIED LIFE SCIENCES AMINO ACID SEQUENCE Amino Acid Substitution AMINO ACIDS Animals Cell Line Cell Membrane - metabolism Classical swine fever Classical Swine Fever Virus Classical swine fever virus - genetics Classical swine fever virus - physiology COMPARATIVE EVALUATIONS CSFV FEVER Fusion peptide GENETICS GLYCOPROTEINS HARBORS HOST IN VITRO Infectious Disease LIPIDS Liposomes - metabolism MEMBRANES Models, Molecular Mutant Proteins - chemistry Mutant Proteins - genetics Mutant Proteins - metabolism PEPTIDES Pestivirus PLANT GROWTH Protein Conformation RESIDUES Reverse Genetics SWINE Viral Envelope Proteins - chemistry Viral Envelope Proteins - genetics Viral Envelope Proteins - metabolism VIRULENCE Virus Internalization VIRUSES Pestivirus Classical swine fever Fusion peptide Classical Swine Fever Virus CSFV
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Summary:	Abstract E2, along with Erns and E1, is an envelope glycoprotein of Classical Swine Fever Virus (CSFV). E2 is involved in several virus functions: cell attachment, host range susceptibility and virulence in natural hosts. Here we evaluate the role of a specific E2 region,818 CPIGWTGVIEC828 , containing a putative fusion peptide (FP) sequence. Reverse genetics utilizing a full-length infectious clone of the highly virulent CSFV strain Brescia (BICv) was used to evaluate how individual amino acid substitutions within this region of E2 may affect replication of BICv. A synthetic peptide representing the complete E2 FP amino acid sequence adopted a β-type extended conformation in membrane mimetics, penetrated into model membranes, and perturbed lipid bilayer integrity in vitro . Similar peptides harboring amino acid substitutions adopted comparable conformations but exhibited different membrane activities. Therefore, a preliminary characterization of the putative FP818 CPIGWTGVIEC828 indicates a membrane fusion activity and a critical role in virus replication.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0042-6822 1096-0341
DOI:	10.1016/j.virol.2014.03.005