L-domain flanking sequences are important for host interactions and efficient budding of vesicular stomatitis virus recombinants.
Vesicular stomatitis virus (VSV) possesses a PPPY and a PSAP motif within the matrix (M) protein. The PPPY motif has significant L-domain activity in BHK-21 cells, whereas the PSAP motif does not. Since the core PSAP motif alone is insufficient to provide L-domain activity, we modified upstream or downstream amino acids flanking the PSAP core motif to determine their effect on L-domain activity. VSV recombinants were recovered that contained single or multiple amino acid mutations in upstream or downstream sequences flanking the PSAP core. Recombinant viruses were examined for growth kinetics, budding efficiency, and functional interactions with host proteins. We demonstrate that the composition of amino acids surrounding the L-domain core motifs are critical for efficient L-domain activity and for interactions with host proteins in the context of a VSV infection.
Irie
Takashi
T
Department of Pathobiology, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, 19104, USA.
Harty
Ronald N
RN
D000595:Amino Acid Sequence / Q000502:physiology; D000818:Animals; D002460:Cell Line; D006801:Humans; D008969:Molecular Sequence Data; D009154:Mutation; D017434:Protein Structure, Tertiary / Q000235:genetics*; D016865:Reassortant Viruses / Q000235:genetics / Q000502:physiology*; D011995:Recombination, Genetic; D018353:Rhabdoviridae Infections / Q000821:virology*; D016415:Sequence Alignment; D014721:Vesicular stomatitis Indiana virus / Q000235:genetics / Q000502:physiology*; D014763:Viral Matrix Proteins / Q000235:genetics*; D014779:Virus Replication
C094460:M protein, Vesicular stomatitis virus; D014763:Viral Matrix Proteins