Disulfide Bonds and Membrane Topology of the Vaccinia Virus A17L Envelope Protein

AUTOR(ES)

Betakova, Tatiana

FONTE

American Society for Microbiology

RESUMO

The envelope protein encoded by the vaccinia virus A17L open reading frame is essential for virion assembly. Our mutagenesis studies indicated that cysteines 101 and 121 form an intramolecular disulfide bond and that cysteine 178 forms an intermolecular disulfide linking two A17L molecules. This arrangement of disulfide bonds has important implications for the topology of the A17L protein and supports a two-transmembrane model in which cysteines 101 and 121 are intraluminal and cysteine 178 is cytoplasmic. The structure of the A17L protein, however, was not dependent on these disulfide bonds, as a recombinant vaccinia virus with all three cysteine codons mutated to serines retained infectivity.

Documentos Relacionados

• Regulation of Vaccinia Virus Morphogenesis: Phosphorylation of the A14L and A17L Membrane Proteins and C-Terminal Truncation of the A17L Protein Are Dependent on the F10L Kinase
• The vaccinia virus 14-kilodalton fusion protein forms a stable complex with the processed protein encoded by the vaccinia virus A17L gene.
• Characterization of the Vaccinia Virus H3L Envelope Protein: Topology and Posttranslational Membrane Insertion via the C-Terminal Hydrophobic Tail
• Vaccinia Virus A28L Gene Encodes an Essential Protein Component of the Virion Membrane with Intramolecular Disulfide Bonds Formed by the Viral Cytoplasmic Redox Pathway
• Vaccinia virus A17L gene product is essential for an early step in virion morphogenesis.