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TRIM52 inhibits Japanese Encephalitis Virus replication by degrading the viral NS2A

View Article: PubMed Central - PubMed

ABSTRACT

The members of tripartite-motif containing (TRIM) protein participate in various cellular processes and play an important role in host antiviral function. TRIM proteins exert their antiviral activity either directly by degrading viral proteins through their E3 ligase activity, or indirectly by promoting host innate immunity. This study demonstrated for the first time that TRIM52 is a novel antiviral TRIM protein against Japanese encephalitis virus (JEV) infection. Overexpression of TRIM52 restricted JEV replication in BHK-21 and 293T cells. In addition, JEV nonstructural protein 2A (NS2A) is a protein that interacts with TRIM52. Their interaction degraded NS2A in a proteasome-dependent manner via the E3 ligase activity of TRIM52. Thus, TRIM52 is a novel antiviral TRIM protein, and it exerted antiviral activity against JEV infection by targeting and degrading viral NS2A.

No MeSH data available.


In vivo self-ubiquitination of TRIM52.(a) Plasmids expressing Flag-tagged TRIM52 or empty vector were co-transfected with or without HA-tagged ubiquitin in 293T cells. The cells were harvested at 30 hpt, and then subjected to an in vivo ubiquitination assay. (b) The 293T cells were co-transfected with Flag-tagged full length TRIM52, RING domain deleted TRIM52 (TRIM52-dR), and empty vector with or without HA-tagged ubiquitin. The cells were collected at 30 hpt for ubiquitination assay. HC, heavy chain of antibody.
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f3: In vivo self-ubiquitination of TRIM52.(a) Plasmids expressing Flag-tagged TRIM52 or empty vector were co-transfected with or without HA-tagged ubiquitin in 293T cells. The cells were harvested at 30 hpt, and then subjected to an in vivo ubiquitination assay. (b) The 293T cells were co-transfected with Flag-tagged full length TRIM52, RING domain deleted TRIM52 (TRIM52-dR), and empty vector with or without HA-tagged ubiquitin. The cells were collected at 30 hpt for ubiquitination assay. HC, heavy chain of antibody.

Mentions: We performed an in vivo ubiquitylation assay in 293T cells to evaluate the E3 ubiquitin ligase activity of the RING finger domain of TRIM52. The 293T cells were co-transfected with Flag-tagged TRIM52 with or without HA-tagged ubiquitin. The cells were collected at 30 hpt; subsequently, the cell lysate was precipitated with anti-Flag affinity gel, and then analyzed by Western blot using the indicated antibodies to detect ubiquitylated TRIM52. Figure 3a shows that poly-ubiquitylated TRIM52 was detected only when Flag-tagged TRIM52 was co-expressed with HA-tagged ubiquitin.


TRIM52 inhibits Japanese Encephalitis Virus replication by degrading the viral NS2A
In vivo self-ubiquitination of TRIM52.(a) Plasmids expressing Flag-tagged TRIM52 or empty vector were co-transfected with or without HA-tagged ubiquitin in 293T cells. The cells were harvested at 30 hpt, and then subjected to an in vivo ubiquitination assay. (b) The 293T cells were co-transfected with Flag-tagged full length TRIM52, RING domain deleted TRIM52 (TRIM52-dR), and empty vector with or without HA-tagged ubiquitin. The cells were collected at 30 hpt for ubiquitination assay. HC, heavy chain of antibody.
© Copyright Policy - open-access
Related In: Results  -  Collection

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getmorefigures.php?uid=PMC5035999&req=5

f3: In vivo self-ubiquitination of TRIM52.(a) Plasmids expressing Flag-tagged TRIM52 or empty vector were co-transfected with or without HA-tagged ubiquitin in 293T cells. The cells were harvested at 30 hpt, and then subjected to an in vivo ubiquitination assay. (b) The 293T cells were co-transfected with Flag-tagged full length TRIM52, RING domain deleted TRIM52 (TRIM52-dR), and empty vector with or without HA-tagged ubiquitin. The cells were collected at 30 hpt for ubiquitination assay. HC, heavy chain of antibody.
Mentions: We performed an in vivo ubiquitylation assay in 293T cells to evaluate the E3 ubiquitin ligase activity of the RING finger domain of TRIM52. The 293T cells were co-transfected with Flag-tagged TRIM52 with or without HA-tagged ubiquitin. The cells were collected at 30 hpt; subsequently, the cell lysate was precipitated with anti-Flag affinity gel, and then analyzed by Western blot using the indicated antibodies to detect ubiquitylated TRIM52. Figure 3a shows that poly-ubiquitylated TRIM52 was detected only when Flag-tagged TRIM52 was co-expressed with HA-tagged ubiquitin.

View Article: PubMed Central - PubMed

ABSTRACT

The members of tripartite-motif containing (TRIM) protein participate in various cellular processes and play an important role in host antiviral function. TRIM proteins exert their antiviral activity either directly by degrading viral proteins through their E3 ligase activity, or indirectly by promoting host innate immunity. This study demonstrated for the first time that TRIM52 is a novel antiviral TRIM protein against Japanese encephalitis virus (JEV) infection. Overexpression of TRIM52 restricted JEV replication in BHK-21 and 293T cells. In addition, JEV nonstructural protein 2A (NS2A) is a protein that interacts with TRIM52. Their interaction degraded NS2A in a proteasome-dependent manner via the E3 ligase activity of TRIM52. Thus, TRIM52 is a novel antiviral TRIM protein, and it exerted antiviral activity against JEV infection by targeting and degrading viral NS2A.

No MeSH data available.