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The Molecular Basis for Erns Dimerization in Classical Swine Fever Virus
Manjula Mischler1, Gregor Meyers1
1Institut für Immunologie, Friedrich-Loeffler-Institut, Südufer 10, Insel Riems, 17493 Greifswald, Germany.
Viruses
|November 27, 2021
Summary
Classical swine fever virus (CSFV) virulence relies on the Erns glycoprotein
Area of Science:
- * Virology
- * Molecular Biology
- * Swine Health
Background:
- * Classical swine fever virus (CSFV) is a significant swine pathogen.
- * The Erns glycoprotein's RNase activity is crucial for CSFV virulence.
- * Erns forms homodimers via disulfide bonds, involving cysteine 171, which is essential for virulence, not viability.
Purpose of the Study:
- * To investigate the structural requirements for Erns homodimerization.
- * To understand the role of specific cysteine residues in CSFV Erns dimerization and virulence.
Main Methods:
- * Site-directed mutagenesis to alter cysteine residues in Erns.
- * Crosslinking experiments to assess protein interactions.
- * Analysis of viral pseudorevertants and their virulence.
Main Results:
- * CSFV Erns dimerization is not essential for viral viability but critical for virulence.
- * Mutant Erns lacking cysteine 171 can still interact transiently.
- * Disulfide-linked dimer formation primarily occurs between cysteine residues at similar helical positions.
Conclusions:
- * The ectodomain integrity of Erns is important for efficient dimer formation.
- * Specific cysteine substitutions can restore Erns dimerization and partially CSFV virulence.
- * Dimerization of Erns is a key determinant of CSFV virulence.
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