The leader peptide of Theiler's murine encephalomyelitis virus is a zinc-binding protein.
The leader (L) peptide is located in the amino-terminal part of the polyprotein of members of the Cardiovirus (which includes Theiler's murine encephalomyelitis virus) and Aphthovirus genera of picornaviruses. Although the function of L is unknown, strain DA of Theiler's murine encephalomyelitis virus with a mutation of L produces a cell-specific restricted infection. We now report that the DA L peptide is a metalloprotein and that zinc binds to a Cys-His motif that is conserved among cardioviruses.
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002352:Carrier Proteins / Q000096:biosynthesis / Q000302:isolation & purification / Q000378:metabolism*; D002460:Cell Line; D017124:Conserved Sequence; D006224:Cricetinae; D007668:Kidney; D008969:Molecular Sequence Data; D016296:Mutagenesis; D021382:Protein Sorting Signals / Q000096:biosynthesis / Q000302:isolation & purification / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis / Q000302:isolation & purification / Q000378:metabolism; D017384:Sequence Deletion; D017945:Theilovirus / Q000235:genetics / Q000378:metabolism*; D015032:Zinc / Q000378:metabolism
D002352:Carrier Proteins; D021382:Protein Sorting Signals; D011993:Recombinant Fusion Proteins; C017800:zinc-binding protein; D015032:Zinc