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Merck
CN
  • Phosphoproteomic analysis reveals Smad protein family activation following Rift Valley fever virus infection.

Phosphoproteomic analysis reveals Smad protein family activation following Rift Valley fever virus infection.

PloS one (2018-02-07)
Cynthia de la Fuente, Chelsea Pinkham, Deemah Dabbagh, Brett Beitzel, Aura Garrison, Gustavo Palacios, Kimberley Alex Hodge, Emanuel F Petricoin, Connie Schmaljohn, Catherine E Campbell, Aarthi Narayanan, Kylene Kehn-Hall
摘要

Rift Valley fever virus (RVFV) infects both ruminants and humans leading to a wide variance of pathologies dependent on host background and age. Utilizing a targeted reverse phase protein array (RPPA) to define changes in signaling cascades after in vitro infection of human cells with virulent and attenuated RVFV strains, we observed high phosphorylation of Smad transcription factors. This evolutionarily conserved family is phosphorylated by and transduces the activation of TGF-β superfamily receptors. Moreover, we observed that phosphorylation of Smad proteins required active RVFV replication and loss of NSs impaired this activation, further corroborating the RPPA results. Gene promoter analysis of transcripts altered after RVFV infection identified 913 genes that contained a Smad-response element. Functional annotation of these potential Smad-regulated genes clustered in axonal guidance, hepatic fibrosis and cell signaling pathways involved in cellular adhesion/migration, calcium influx, and cytoskeletal reorganization. Furthermore, chromatin immunoprecipitation confirmed the presence of a Smad complex on the interleukin 1 receptor type 2 (IL1R2) promoter, which acts as a decoy receptor for IL-1 activation.

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Sigma-Aldrich
抗磷酸组蛋白H3(Ser10)抗体,有丝分裂标记, Upstate®, from rabbit
Sigma-Aldrich
抗-Beclin-1 兔抗, affinity isolated antibody, buffered aqueous solution
Sigma-Aldrich
Anti-phospho-Histone H3 (Ser28) Antibody, from rabbit, purified by affinity chromatography