Core Protein of Pestiviruses Is Processed at the C Terminus by Signal Peptide Peptidase

• DOI: 10.1128/jvi.80.4.1915-1921.2006
• Publication Date: 2006-01-26T18:02:43Z
• Authors: Manuela Heimann; Gleyder Roman Sosa; Bruno Martoglio; Heinz-Jürgen Thiel; Till Rümenapf
• Keywords: Cleavage (geology); C-terminus; Alanine; Signal peptidase

The core protein of pestiviruses is released from the polyprotein by viral and cellular proteinases. Here we report on an additional intramembrane proteolytic step that generates C terminus protein. C-terminal processing classical swine fever virus (CSFV) was blocked inhibitor (Z-LL)(2)-ketone, which specific for signal peptide peptidase (SPP). same effect obtained overexpression dominant-negative SPP D(265)A mutant. presence (Z-LL)(2)-ketone reduced viability CSFV almost 100-fold in a concentration-dependent manner. Reduction also observed infection experiments using cell line inducibly expressed D(265)A. position cleavage determined sequencing purified virions. alanine(255) located hydrophobic center peptide. generation identical to scheme hepatitis viruses.