Annexin A2 gene interacting with viral matrix protein to promote bovine ephemeral fever virus release

Chen, Lihui; Li, Xingyu; Wang, Hongmei; Hou, Peili; He, Hongbin

doi:10.4142/jvs.2020.21.e33

Cited by 8 publications

(3 citation statements)

References 49 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Cellular proteins that potentially interact with the 2A protein were identified in this analysis (Table 4). Based on the previous literatures, annexin A2 is closely related to viral pathogenicity and apoptosis [8][9][10]. We chose annexin A2 as the interaction protein with the 2A protein for further study.…”

Section: A-interacting Proteins Identified By His Pull-down Assay And...mentioning

confidence: 99%

Encephalomyocarditis Virus 2A Protein Inhibited Apoptosis by Interaction with Annexin A2 through JNK/c-Jun Pathway

Han

Liang

Tong

et al. 2022

Viruses

View full text Add to dashboard Cite

Encephalomyocarditis virus can cause myocarditis and encephalitis in pigs and other mammals, thus posing a potential threat to public health safety. The 2A protein is an important virulence factor of EMCV. Previous studies have shown that the 2A protein may be related to the inhibition of apoptosis by virus, but its specific molecular mechanism is not clear. In this study, the 2A protein was expressed in Escherichia coli in order to find interacting cell proteins. A pull down assay, coupled with mass spectrometry, revealed that the 2A protein possibly interacted with annexin A2. Co-immunoprecipitation assays and confocal imaging analysis further demonstrated that the 2A protein interacted with annexin A2 in cells. In reducing the expression of annexin A2 by siRNA, the ability of the 2A protein to inhibit apoptosis was weakened and the proliferation of EMCV was slowed down. These results suggest that annexin A2 is closely related to the inhibition of apoptosis by 2A. Furthermore, both RT-PCR and western blot results showed that the 2A protein requires annexin A2 interaction to inhibit apoptosis via JNK/c-Jun pathway. Taken together, our data indicate that the 2A protein inhibits apoptosis by interacting with annexin A2 via the JNK/c-Jun pathway. These findings provide insight into the molecular pathogenesis underlying EMCV infection.

show abstract

Section: A-interacting Proteins Identified By His Pull-down Assay And...mentioning

confidence: 99%

Encephalomyocarditis Virus 2A Protein Inhibited Apoptosis by Interaction with Annexin A2 through JNK/c-Jun Pathway

Han

Liang

Tong

et al. 2022

Viruses

View full text Add to dashboard Cite

show abstract

“…The membranes were incubated with appropriate primary antibodies diluted in TBST supplemented with 5% nonfat dry milk overnight at 4 • C, and then washed five times with TBST. Finally, the incubated membranes were treated with a horseradish peroxidase-conjugated secondary antibody for 2 h as previously described [48][49][50]. Protein bands were quantified and analyzed by densitometry using AlphaView software (version 3.4; ProteinSimple, Santa Clara, CA, USA).…”

Section: Namementioning

confidence: 99%

Induction of the Unfolded Protein Response during Bovine Alphaherpesvirus 1 Infection

Wang

et al. 2020

Viruses

Self Cite

View full text Add to dashboard Cite

Bovine herpesvirus 1 (BoHV-1) is an alphaherpesvirus that causes great economic losses in the cattle industry. Herpesvirus infection generally induces endoplasmic reticulum (ER) stress, and the unfolded protein response (UPR) in infected cells. However, it is not clear whether ER stress and UPR can be induced by BoHV-1 infection. Here, we found that ER stress induced by BoHV-1 infection could activate all three UPR sensors (the activating transcription factor 6 (ATF6), the inositol-requiring enzyme 1 (IRE1), and the protein kinase RNA-like ER kinase (PERK)) in MDBK cells. During BoHV-1 infection, the ATF6 pathway of UPR did not affect viral replication. However, both knockdown and specific chemical inhibition of PERK attenuated the BoHV-1 proliferation, and chemical inhibition of PERK significantly reduced the viral replication at the post-entry step of the BoHV-1 life cycle. Furthermore, knockdown of IRE1 inhibits BoHV-1 replication, indicating that the IRE1 pathway may promote viral replication. Further study revealed that BoHV-1 replication was enhanced by IRE1 RNase activity inhibition at the stage of virus post-entry in MDBK cells. Furthermore, IRE1 kinase activity inhibition and RNase activity enhancement decrease BoHV1 replication via affecting the virus post-entry step. Our study revealed that BoHV-1 infection activated all three UPR signaling pathways in MDBK cells, and BoHV-1-induced PERK and IRE1 pathways may promote viral replication. This study provides a new perspective for the interactions of BoHV-1 and UPR, which is helpful to further elucidate the mechanism of BoHV-1 pathogenesis.

show abstract

“…It has been reported that ANXA2 participates in the replication process of a variety of viruses. For examples, ANXA2 interacts with the matrix (M) protein of viruses (such as measles virus and bovine transient fever virus), which is located on the inner surface of the virus envelope and plays a role in the formation of viral particles, thereby contributing to the assembly and release of the virus [22,23]. ANXA2 also participates in Classic swine fever virus (CSFV) and Hepatitis C virus (HCV) production process by binding to the NS5A protein [24].…”

Section: Introductionmentioning

confidence: 99%

ANXA2 enhances virus replication through negatively regulating cGAS-STING and RLRs-mediated signal pathway

Huang

Xue

et al. 2021

Preprint

View full text Add to dashboard Cite

Host nucleic acid receptors can recognize the viral DNA or RNA upon virus infection, which further triggers multiple signal pathways to promote the translocation of the interferon regulatory factor 3 (IRF3) into nucleus and produce type I interferon (IFN), leading to the host antiviral response. Here, we report a novel negative regulator Annexin A2 (ANXA2) that regulates type I IFN production through multiple mechanisms. Ectopic expression of ANXA2 inhibited the production of type I IFN induced by DNA- and RNA viruses and enhanced virus replication, while knockout of ANXA2 expression enhanced the production of type I IFN and inhibited virus replication. Mechanistically, ANXA2 not only disrupted MDA5 recruiting MAVS, but also inhibited the interaction between MAVS and TRAF3 upon RNA virus infection. In addition, ANXA2 impacted the translocation of STING from endoplasmic reticulum to Golgi apparatus upon DNA virus infection. Interestingly, ANXA2 also inhibited IRF3 phosphorylation and nuclear translocation through competing with TANK-binds kinase 1 (TBK1) and inhibitor-κB kinase ε (IKKε) for binding to IRF3. Anxa2 deficiency in vivo increased the production of type I IFN, which resulted in suppression of encephalomyocarditis virus (EMCV) replication. Our findings reveal that ANXA2, as a negative regulator of type I IFN production, plays an important role in regulating the host antiviral responses.Author summaryAnnexin is a family of evolutionarily conserved multi-gene proteins, which are widely distributed in various tissues and cells of plants and animals. These proteins can reversibly bind to phospholipid membranes and to calcium ions (Ca2+). To date, several studies have confirmed that some members of the Annexin family regulate the antiviral innate immune response. Until now, regulation of the production of type I IFN by ANXA2 is not reported. In this study, ANXA2 were found to strongly inhibit the production of type I IFN, leading to increased virus replication while knockout of ANXA2 expression inhibited virus replication by increasing the amount of IFN. Compared with wild-type littermates, ANXA2 deficiency mice produced more type I IFN to inhibit virus replication. Our results provide methanistic insights into the novel role of ANXA2 in the antiviral innate immune responses.

show abstract

Annexin A2 gene interacting with viral matrix protein to promote bovine ephemeral fever virus release

Cited by 8 publications

References 49 publications

Encephalomyocarditis Virus 2A Protein Inhibited Apoptosis by Interaction with Annexin A2 through JNK/c-Jun Pathway

Encephalomyocarditis Virus 2A Protein Inhibited Apoptosis by Interaction with Annexin A2 through JNK/c-Jun Pathway

Induction of the Unfolded Protein Response during Bovine Alphaherpesvirus 1 Infection

ANXA2 enhances virus replication through negatively regulating cGAS-STING and RLRs-mediated signal pathway

Contact Info

Product

Resources

About