Binding chicken Anx2 is beneficial for infection with infectious bursal disease virus

Ren, Xiangang; Zhang, Lizhou; Gao, Yulong; Gao, Honglei; Wang, Yongqiang; Liu, Changjun; Cui, Hongyu; Zhang, Yanping; Jiang, Lili; Qi, Xiaole; Wang, Xiaomei

doi:10.1016/j.virusres.2015.07.024

Cited by 6 publications

(5 citation statements)

References 32 publications

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“…Consequently, ANXA2 itself is found in a wide variety of cells and tissues and is a key host factor involved in many diverse cellular processes, including vesicle trafficking [ 31 ], membrane fusion [ 32 ], and exocytosis [ 33 ]. ANXA2 has been found to be involved in various viral infections, including cytomegalovirus [ 34 ], hepatitis C virus [ 17 ], and infectious bursal disease virus [ 35 ]. ANXA2 also has an important role during human immunodeficiency virus (HIV) type 1 entry, assembly, and budding [ 36 ].…”

Section: Discussionmentioning

confidence: 99%

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

Chang

Yang

Gao

et al. 2018

Vet Res

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Porcine reproductive and respiratory syndrome virus (PRRSV) is an important globally distributed and highly contagious pathogen that has restricted cell tropism in vivo and in vitro. In the present study, we found that annexin A2 (ANXA2) is upregulated expressed in porcine alveolar macrophages infected with PRRSV. Additionally, PRRSV replication was significantly suppressed after reducing ANXA2 expression in Marc-145 cells using siRNA. Bioinformatics analysis indicated that ANXA2 may be relevant to vimentin, a cellular cytoskeleton component that is thought to be involved in the infectivity and replication of PRRSV. Co-immunoprecipitation assays and confocal analysis confirmed that ANXA2 interacts with vimentin, with further experiments indicating that the B domain (109–174 aa) of ANXA2 contributes to this interaction. Importantly, neither ANXA2 nor vimentin alone could bind to PRRSV and only in the presence of ANXA2 could vimentin interact with the N protein of PRRSV. No binding to the GP2, GP3, GP5, nor M proteins of PRRSV was observed. In conclusion, ANXA2 can interact with vimentin and enhance PRRSV growth. This contributes to the regulation of PRRSV replication in infected cells and may have implications for the future antiviral strategies.

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Section: Discussionmentioning

confidence: 99%

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

Chang

Yang

Gao

et al. 2018

Vet Res

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“…The alpha 4 beta 1 integrin is another putative receptor, was verified by Delgui et al on BALB/c 3 T3 cells [7]. In addition, using a virus overlay protein-binding assay (VOPBA) with DF-1 cells, Ren et al demonstrated that chicken annexin A2 is positively related to viral infection [8]. All of these proteins have been found to promote viral infection.…”

Section: Introductionmentioning

confidence: 92%

HSC70 is required for infectious bursal disease virus (IBDV) infection in DF-1 cells

Chen

Qin

Qian

et al. 2020

Virol J

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Background Infectious bursal disease (IBD) is a highly contagious infectious disease that causes severe immunosuppression and damage to the bursa of Fabricius in chickens. Several proteins involved in IBD virus (IBDV) infection, such as surface immunoglobulin M, integrin, annexin A2 and chicken heat shock protein 90, have been identified. However, the main protein that plays key roles in virus infection has not yet been confirmed. Methods DF-1 cell line was transfected with the pcDNA-VP2 plasmid and analyzed by immunofluorescence assay. The proteins reacted with VP2 of IBDV in DF-1 cells were pulldown with the monoclonal antibody and identified by mass spectrometry. Heat shock cognate protein 70 (HSC70), one of these proteins, was selected to be investigated in the function in IBDV infection by specific antibody and its inhibitor. Results The DF-1 cell line was transfected with the pcDNA-VP2 plasmid, and expression of IBDV VP2 in DF-1 cells was confirmed by immunofluorescence assays. Heat shock cognate protein 70 (HSC70) was one of the proteins identified by coimmunoprecipitation using a monoclonal antibody (2H11) against VP2 and mass spectrometry analysis. IBDV infection in DF-1 cells was strongly inhibited by both an anti-HSC70 antibody and a HSC70 inhibitor (VER155008). Conclusion These results suggest that HSC70 may be an essential factor for IBDV infection.

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“…Several characteristics of cell entry by IBDV have been elucidated ( Qin and Zheng, 2017 ). Cellular factors for virus attachment include Hsp90 located on the cell surface ( Lin et al, 2007 ), the membrane protein Annexin II ( Ren et al, 2015 ), the integrin α4/β1 (potentially through an integrin-interacting motif in VP2; Delgui et al, 2009 ) and surface immunoglobulin M ( Luo et al, 2010 ). Cellular internalization of IBDV occurs by endocytosis that is clathrin-independent but requires c-Src tyrosine kinase and the actin cytoskeleton as is observed during macropinocytosis ( Yip et al, 2012 ; Gimenez et al, 2015 ; Ye et al, 2017 ).…”

Section: Molecular Mechanism Of Cell Entry By Birnavirusesmentioning

confidence: 99%

Mechanisms of Cell Entry by dsRNA Viruses: Insights for Efficient Delivery of dsRNA and Tools for Improved RNAi-Based Pest Control

et al. 2021

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While RNAi is often heralded as a promising new strategy for insect pest control, a major obstacle that still remains is the efficient delivery of dsRNA molecules within the cells of the targeted insects. However, it seems overlooked that dsRNA viruses already have developed efficient strategies for transport of dsRNA molecules across tissue barriers and cellular membranes. Besides protecting their dsRNA genomes in a protective shell, dsRNA viruses also display outer capsid layers that incorporate sophisticated mechanisms to disrupt the plasma membrane layer and to translocate core particles (with linear dsRNA genome fragments) within the cytoplasm. Because of the perceived efficiency of the translocation mechanism, it is well worth analyzing in detail the molecular processes that are used to achieve this feat. In this review, the mechanism of cell entry by dsRNA viruses belonging to the Reoviridae family is discussed in detail. Because of the large amount of progress in mammalian versus insect models, the mechanism of infections of reoviruses in mammals (orthoreoviruses, rotaviruses, orbiviruses) will be treated as a point of reference against which infections of reoviruses in insects (orbiviruses in midges, plant viruses in hemipterans, insect-specific cypoviruses in lepidopterans) will be compared. The goal of this discussion is to uncover the basic principles by which dsRNA viruses cross tissue barriers and translocate their cargo to the cellular cytoplasm; such knowledge subsequently can be incorporated into the design of dsRNA virus-based viral-like particles for optimal delivery of RNAi triggers in targeted insect pests.

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Binding chicken Anx2 is beneficial for infection with infectious bursal disease virus

Cited by 6 publications

References 32 publications

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

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

HSC70 is required for infectious bursal disease virus (IBDV) infection in DF-1 cells

Mechanisms of Cell Entry by dsRNA Viruses: Insights for Efficient Delivery of dsRNA and Tools for Improved RNAi-Based Pest Control

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