Work

Ectromelia virus BTB/kelch proteins, EVM150 and EVM167, interact with cullin-3-based ubiquitin ligases

Year: 2021

Type: article

Abstract: Cellular proteins containing BTB and kelch domains have been shown to function as adapters for the recruitment of substrates to cullin-3-based ubiquitin ligases. Poxviruses are the only family of viruses known to encode multiple BTB/kelch proteins, suggesting that poxviruses may modulate the ubiquitin pathway through interaction with cullin-3. Ectromelia virus encodes four BTB/kelch proteins and one BTB-only protein. Here we demonstrate that two of the ectromelia virus encoded BTB/kelch proteins, EVM150 and EVM167, interacted with cullin-3. Similar to cellular BTB proteins, the BTB domain of EVM150 and EVM167 was necessary and sufficient for cullin-3 interaction. During infection, EVM150 and EVM167 localized to discrete cytoplasmic regions, which co-localized with cullin-3. Furthermore, EVM150 and EVM167 co-localized and interacted with conjugated ubiquitin, as demonstrated by confocal microscopy and co-immunoprecipitation. Our findings suggest that the ectromelia virus encoded BTB/kelch proteins, EVM150 and EVM167, interact with cullin-3 potentially functioning to recruit unidentified substrates for ubiquitination.

Source: Carolina Digital Repository (University of North Carolina at Chapel Hill)

DOI: 10.17615/rb95-7988

Authors: Furukawa, Manabu, Barry, Michele, Xiong, Yue, Van Buuren, Nicholas, Garneau, Robyn, Campbell, Stephanie, Wilton, Brianne A.

Language: English

Topic: Poxvirus research and outbreaks

Subfield: Virology

Field: Immunology and Microbiology

Domain: Life Sciences

Open Access status: green

Funders: Howard Hughes Medical Institute, National Institutes of Health, Canadian Institutes of Health Research

Award: G9000263411

OpenAlex ID: W4298179856

FWCI:

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