Annexin A2 binds to vimentin and contributes to porcine reproductive and respiratory syndrome virus multiplication

Chang, Xiao Bo; Yang, Yong; Gao, Jia Cong; Zhao, Kun; Guo, Jin; Ye, Chao; Jiang, Cheng Gang; Tian, Zhi Jun; Cai, X H; Tong, Guang Zhi; An, Tong Qing

doi:10.1186/s13567-018-0571-5

Cited by 22 publications

(16 citation statements)

References 43 publications

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“…Vimentin is an important cytoskeletal protein involved in many virus infections. Interaction of annexin A2 with vimentin has been reported to enhanced virus replication in porcine reproductive and respiratory‐syndrome virus and porcine cicovirus type 2 . Furthermore, it has been demonstrated by Co‐IP, confocal laser microscopy, and bioinformatics that vimentin interacts with B domain of annexin A2 to enhance porcine reproductive and respiratory syndrome viral growth …”

Section: Association Of Annexin A2 With Other Virus Interacting Proteinsmentioning

confidence: 99%

Annexin A2 extracellular translocation and virus interaction: A potential target for antivirus‐drug discovery

Aliyu

Ling

Hashim

et al. 2019

Reviews in Medical Virology

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Annexin A2 is a membrane scaffolding and binding protein, which mediated various cellular events. Its functions are generally affected by cellular localization. In the cytoplasm, they interacted with different phospholipid membranes in Ca 2+ -dependent manner and play vital roles including actin binding, remodeling and dynamics, cytoskeletal rearrangement, and lipid-raft microdomain formation. However, upon cell exposure to certain stimuli, annexin A2 translocates to the external leaflets of the plasma membrane where annexin A2 was recently reported to serve as a virus receptor, play an important role in the formation of virus replication complex, or implicated in virus assembly and budding. Here, we review some of annexin A2 roles in virus infections and the potentiality of targeting annexin A2 in the design of novel and promising antivirus agent that may have a broader consequence in virus therapy.

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Section: Association Of Annexin A2 With Other Virus Interacting Proteinsmentioning

confidence: 99%

Annexin A2 extracellular translocation and virus interaction: A potential target for antivirus‐drug discovery

Aliyu

Ling

Hashim

et al. 2019

Reviews in Medical Virology

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“…Virus titers were determined according to a previous report [32]. Briefly, MARC-145 cells, grown in 96-well plates, were infected with ten-fold serial dilution of samples.…”

Section: Virus Titrationmentioning

confidence: 99%

IFI16 Inhibits Porcine Reproductive and Respiratory Syndrome Virus 2 Replication in a MAVS-Dependent Manner in MARC-145 Cells

Chang

Shi

Zhang

et al. 2019

Viruses

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Porcine reproductive and respiratory syndrome virus (PRRSV) is a single-stranded positive-sense RNA virus, and the current strategies for controlling PRRSV are limited. Interferon gamma-inducible protein 16 (IFI16) has been reported to have a broader role in the regulation of the type I interferons (IFNs) response to RNA and DNA viruses. However, the function of IFI16 in PRRSV infection is unclear. Here, we revealed that IFI16 acts as a novel antiviral protein against PRRSV-2. IFI16 could be induced by interferon-beta (IFN-β). Overexpression of IFI16 could significantly suppress PRRSV-2 replication, and silencing the expression of endogenous IFI16 by small interfering RNAs led to the promotion of PRRSV-2 replication in MARC-145 cells. Additionally, IFI16 could promote mitochondrial antiviral signaling protein (MAVS)-mediated production of type I interferon and interact with MAVS. More importantly, IFI16 exerted anti-PRRSV effects in a MAVS-dependent manner. In conclusion, our data demonstrated that IFI16 has an inhibitory effect on PRRSV-2, and these findings contribute to understanding the role of cellular proteins in regulating PRRSV replication and may have implications for the future antiviral strategies.

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“…It was reported that vimentin was important for Epstein-Barr Virus LMP1-mediated Akt and ERK activation and transformation of rodent fibroblasts [30]. Cellular vimentin is also a specific host binding partner for 2C of FMDV [31], and Vimentin rearrangement plays a structural role in anchoring DENV2 to replication sites [32], and in facilitating efficient viral RNA replication with NS4A Protein [33], and in enhancing PRRSV growth by interacting with ANXA2 [34]. These results suggested that vimentin as intermediate filament in MDCK cells should be an important intracellular molecule for H9N2 virus entry and replication.…”

Section: Discussionmentioning

confidence: 99%

The molecular evolutionary characteristics of new isolated H9N2 AIV from East China and the function of vimentin on virus replication in MDCK cells

Zheng

Hao

et al. 2020

Virol J

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Background: The low pathogenic H9N2 AIV caused the serious impact on the poultry industry and public safety. Our purpose was to investigate the molecular evolutionary characteristics of the new isolated H9N2 virus and investigate the intracellular target protein of H9N2 AIV replication in sensitive cells. Methods: AIV A/chicken/Shandong/LY1/2017 (H9N2) was isolated from the cloaca of the healthy chicken in Shandong, and the full-length eight gene segments of this isolated H9N2 AIV were amplified by RT-PCR and analyzed. MDCK cells were used as the target cell model, and VOPBA assay and LC-MS/MS were carried out to identify the virus-binding protein of H9N2 AIV. MDCK cells were pre-treated with the special antibody and siRNA, and treated with H9N2 AIV to detect the virus replication. Additionally, Vimentin-pcDNA3.0 was successfully constructed, and transinfected into MDCK cells, and then H9N2 AIV mRNA was detected with RT-PCR. Results: Phylogenetic analysis revealed that HA, NA, PB2, PB1, PA, NP and M seven genes of the isolated H9N2 AIV were derived from A/Chicken/Shanghai/F/98, while NS gene was derived from A/Duck/Hong Kong/Y439/97. The cleavage site sequence of HA gene of the isolated H9N2 AIV was a PARSSR G pattern, and the left side sequence (224~229) of receptor binding site was NGQQGR pattern, which were similar to that of A/Chicken/Shanghai/F/98. Following VOPBA assay, we found one protein of about 50KDa binding to H9N2 AIV, and the results of LC-MS/MS analysis proved that vimentin was the vital protein binding to H9N2 AIV. The pre-incubation of the specific antibody and siRNA decreased the viral RNA level in MDCK cells treated with H9N2 AIV. Furthermore, we found that over-expressed vimentin increased H9N2 AIV replication in MDCK cells.

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Annexin A2 binds to vimentin and contributes to porcine reproductive and respiratory syndrome virus multiplication

Cited by 22 publications

References 43 publications

Annexin A2 extracellular translocation and virus interaction: A potential target for antivirus‐drug discovery

Annexin A2 extracellular translocation and virus interaction: A potential target for antivirus‐drug discovery

IFI16 Inhibits Porcine Reproductive and Respiratory Syndrome Virus 2 Replication in a MAVS-Dependent Manner in MARC-145 Cells

The molecular evolutionary characteristics of new isolated H9N2 AIV from East China and the function of vimentin on virus replication in MDCK cells

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