Phosphorylation of the HTLV-1 matrix L-domain-containing protein by virus-associated ERK-2 kinase

L-domain-containing proteins from animal retroviruses play a critical role in the recruitment of the host cell endocytic machinery that is required for retroviruses budding. We recently demonstrated that phosphorylation of the p6 gag protein containing the L-domain of the human immunodeficiency viru...

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Veröffentlicht in:Virology (New York, N.Y.) Jg. 349; H. 2; S. 430 - 439
Hauptverfasser: Hémonnot, Bénédicte, Molle, Dorothée, Bardy, Martine, Gay, Bernard, Laune, Daniel, Devaux, Christian, Briant, Laurence
Format: Journal Article
Sprache:Englisch
Veröffentlicht: United States Elsevier Inc 05.06.2006
Schlagworte:
Amino Acid Sequence
Amino Acid Substitution
Budding
Cell Line
ERK-2
HTLV-1
Human immunodeficiency virus 1
Human T-lymphotropic virus 1
Human T-lymphotropic virus 1 - growth & development
Human T-lymphotropic virus 1 - metabolism
Humans
L-domain
Microscopy, Electron, Transmission
Mitogen-Activated Protein Kinase 1 - metabolism
Molecular Sequence Data
Mutagenesis, Site-Directed
Mutation, Missense
Phosphorylation
Protein Structure, Tertiary
Serine - metabolism
Viral Matrix Proteins - chemistry
Viral Matrix Proteins - metabolism
Virus Assembly
L-domain
ERK-2
Phosphorylation
MA
PKA
HRP
GST
HTLV-1
MAPK
Budding
ERK
ISSN:0042-6822, 1096-0341
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Zusammenfassung:L-domain-containing proteins from animal retroviruses play a critical role in the recruitment of the host cell endocytic machinery that is required for retroviruses budding. We recently demonstrated that phosphorylation of the p6 gag protein containing the L-domain of the human immunodeficiency virus type 1 regulates viral assembly and budding. Here, we investigated whether or not the L-domain-containing protein from another human retrovirus, namely the matrix protein of the human T-cell leukemia virus type 1, that contains the canonical PTAP and PPPY L-domain motifs, shares similar functional properties. We found that MA is phosphorylated at several sites. We identified one phosphorylated amino acid in the HTLV-1 MA protein as being S105, located in the close vicinity to the L-domain sequence. S105 phosphorylation was found to be mediated by the cellular kinase ERK-2 that is incorporated within HTLV-1 virus particles in an active form. Mutation of the ERK-2 target S105 residue into an alanine was found to decrease viral release and budding efficiency of the HTLV-1 ACH molecular clone from transfected cells. Our data thus support the postulate that phosphorylation of retroviral L-domain proteins is a common feature to retroviruses that participates in the regulation of viral budding.
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ISSN:0042-6822
1096-0341
DOI:10.1016/j.virol.2006.02.043