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Updated: Feb 24, 2026

Methodology for the Efficient Generation of Fluorescently Tagged Vaccinia Virus Proteins
Published on: January 17, 2014
Cellular interactome analysis of vaccinia virus K7 protein identifies three transport machineries as binding partners
Ye Li1, Leiliang Zhang2, Youyang Ke3
1MOH Key Laboratory of Systems Biology of Pathogens, Institute of Pathogen Biology, Chinese Academy of Medical Sciences & Peking Union Medical College, Beijing, 100730, China.
Abstract:
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.
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