Abstract
The Tyr-X-X-Leu (YxxL) motif of the vaccinia virus F13L protein was examined for late (L) domain activity. The ability of an F13L deletion virus to form plaques was restored by PCR products containing single alanine substitutions within the motif and a YAAL construct but not by constructs lacking both the Y and L residues. Recombinant viruses possessing alanine substitutions in place of the tyrosine or the leucine residue in the YxxL motif demonstrated small, asymmetrical plaques. RNA interference-dependent depletion of Alix and TSG101 (host proteins involved in L domain-dependent protein trafficking) diminished extracellular enveloped virion production to various degrees, suggesting that the YxxL motif is a genuine L domain.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Amino Acid Motifs / genetics
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Amino Acid Substitution
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Animals
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Calcium-Binding Proteins / deficiency
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Calcium-Binding Proteins / metabolism
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Carrier Proteins / metabolism
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Cell Cycle Proteins / metabolism
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Cell Line
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DNA-Binding Proteins / deficiency
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DNA-Binding Proteins / metabolism
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Endosomal Sorting Complexes Required for Transport
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Humans
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Membrane Proteins / genetics
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Membrane Proteins / metabolism*
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Protein Structure, Tertiary / genetics
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Protein Transport / genetics
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Transcription Factors / deficiency
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Transcription Factors / metabolism
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Vaccinia virus / genetics
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Vaccinia virus / metabolism*
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Viral Envelope Proteins / genetics
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Viral Envelope Proteins / metabolism*
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Virion / genetics
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Virion / metabolism*
Substances
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Calcium-Binding Proteins
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Carrier Proteins
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Cell Cycle Proteins
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DNA-Binding Proteins
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Endosomal Sorting Complexes Required for Transport
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Membrane Proteins
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PDCD6IP protein, human
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Transcription Factors
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Tsg101 protein
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Viral Envelope Proteins
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p37 protein, Vaccinia virus