Cellular interactome analysis of vaccinia virus K7 protein identifies three transport machineries as binding partners for K7.
Identification of viral-host interacting proteins will contribute to understanding of how poxvirus exploits the host cellular machinery. The vaccinia virus gene K7R encodes a conserved protein K7 in most orthopoxviruses. To gain insight into the biology of K7, we investigated the cellular interactome of K7 by GST pulldown coupled with mass spectrometry. The top categories of identified proteins contained components of trafficking machineries. We selected key components of three transport machineries including coatomer, retromer, and CHEVI to further confirm their binding abilities to K7. Di-lysine motif of K7 is required for its interaction with coatomer, while C terminal leucines in K7 are critical for association of retromer. Our study uncovers the viral-host interactome of vaccinia K7 and reveals three host transport machineries as binding partners of K7, which might have important roles in poxvirus' life cycles.
['Li|Ye|Y|', 'Zhang|Leiliang|L|', 'Ke|Youyang|Y|']
D045744:Cell Line, Tumor D006367:HeLa Cells D054884:Host-Pathogen Interactions D006801:Humans D011485:Protein Binding D014615:Vaccinia D014616:Vaccinia virus D014764:Viral Proteins
Vaccinia virus K7 Coatomer Retromer CHEVI