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Showing 1–4 of 4 results

Advanced filters: Author: Ricardo Rajsbaum Clear advanced filters

TRIM7 ubiquitinates SARS-CoV-2 membrane protein to limit apoptosis and viral replication

TRIM7 acts as an antiviral factor during SARS-CoV-2 infection, by ubiquitinating the M protein on K14 and inhibiting caspase-6-dependent apoptosis. The natural K14 mutations in circulating strains support the physiological role of M ubiquitination.

Maria Gonzalez-Orozco
Hsiang-chi Tseng
Ricardo Rajsbaum
ResearchOpen Access30 Nov 2024
Nature Communications

Volume: 15, P: 1-16
Envelope protein ubiquitination drives entry and pathogenesis of Zika virus

The E3 ubiquitin ligase TRIM7 polyubiquitinates the envelope protein of Zika virus, adding Lys63-linked polyubiquitin chains that interact with the TIM1 receptor of host cells to enhance virus entry and replication.

Maria I. Giraldo
Hongjie Xia
Ricardo Rajsbaum
Research08 Jul 2020
Nature

Volume: 585, P: 414-419
An evolutionary NS1 mutation enhances Zika virus evasion of host interferon induction

The Asian lineage of Zika virus (ZIKV) has acquired a mutation in NS1 that enhances mosquito infection. Here, Xia et al. show that the same mutation interferes with interferon production through interaction with TBK1 and affects ZIKV replication in mice.

Hongjie Xia
Huanle Luo
Pei-Yong Shi
ResearchOpen Access29 Jan 2018
Nature Communications

Volume: 9, P: 1-13
Ubiquitination of SARS-CoV-2 ORF7a promotes antagonism of interferon response

Zengguo Cao
Hongjie Xia
Pei-Yong Shi
Correspondence20 Jan 2021
Cellular & Molecular Immunology

Volume: 18, P: 746-748