Host protein ABCE1 interacts with the viral phosphoprotein and promotes rabies virus replication

Liu, Xing; Zhang, Jiwen; Li, Fang; Hagoss, Yibrah Tekle; Tesfagaber, Weldu; Wang, Lulu; Wang, Zilong; Zhao, Dongming; Bu, Zhigao

doi:10.1016/j.bsheal.2020.07.011

Cited by 6 publications

(9 citation statements)

References 32 publications

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“…We performed FLAG tag–based immunoprecipitation of lysates of HEK293T cells transfected with plasmids expressing either N- or C-terminally FLAG-tagged M protein (M-NF or M-CF, respectively) and identified host proteins that interacted with the M proteins by using mass spectrometry (MS) ( Fig. 1 A ) as described previously ( 28 ). Proteins were detected in lysates of cells transfected with the plasmid expressing FLAG-tagged M proteins but not in those of cells transfected with the control plasmid ( Fig.…”

Section: Resultsmentioning

confidence: 99%

The ATPase ATP6V1A facilitates rabies virus replication by promoting virion uncoating and interacting with the viral matrix protein

Liu

Zhang

et al. 2021

Journal of Biological Chemistry

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Rabies virus (RABV) matrix protein (M) plays crucial roles in viral transcription, replication, assembly, and budding; however, its function during the early stage of virus replication remains unknown. Here, we mapped the protein interactome between RABV M and human host factors using a proteomic approach, finding a link to the V-type proton ATPase (V-ATPase) catalytic subunit A (ATP6V1A) which is located in the endosomes where RABV first enters. By downregulating or upregulating ATP6V1A expression in HEK293T cells, we found that ATP6V1A facilitated RABV replication. We further found that ATP6V1A was involved in the dissociation of incoming viral M proteins during viral uncoating. Co-immunoprecipitation demonstrated that M interacted with the full length or middle domain of ATP6V1A, which was dependent on the lysine residue at position 256 and the glutamic acid residue at position 279. RABV growth and uncoating in ATP6V1A-depleted cells was restored by trans-complementation with the full length or interaction domain of ATP6V1A. Moreover, stably overexpressed ATP6V1A enhanced RABV growth in Vero cells which are used for the production of rabies vaccine. Our findings identify a new partner for RABV M proteins and establish a new role of ATP6V1A by promoting virion uncoating during RABV replication.

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Section: Resultsmentioning

confidence: 99%

The ATPase ATP6V1A facilitates rabies virus replication by promoting virion uncoating and interacting with the viral matrix protein

Liu

Zhang

et al. 2021

Journal of Biological Chemistry

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“…Phage display assay, Co-IP, Pull-down assay [63] P (P3 Isoform) RABV (Ni strain) MT Colocalization, dSTORM [56] P RABV (HEP-Flury, CVS-11 strains) HSP90AA1/Cdc37 Co-IP, colocalization [87] P RABV (street strain 8743THA) JAK1 Protein complementation assay [55] P, P5 isoform RABV (HEP-Flury, CVS-11 strains) BECN1 Co-IP, Colocalization [64,65] P RABV (ERA strain) ABCE1 Pull-down assay, Co-IP [67] P RABV (CVS-B2c, DRV-Mexico) IIGP1 Co-IP, Colocalization [76] 238 Iran. Biomed.…”

Section: Discussionmentioning

confidence: 99%

“…Inactivation of ABCE1 inhibits RABV replication significantly, but its overexpression enhances the viral replication. Thus, this binding positively regulates virus progeny [67] . On the other hand, P and ABCE1 are both associated with the IFN signaling.…”

Section: Iran Biomed J 25 (4): 226-242 233mentioning

confidence: 97%

“…P5-BECN1 interaction promotes RABV selfreplication [64] . ABCE1 (RNase L inhibitor) is another host interactor of RABV (ERA strain) P [67] . This protein acts as a RNase L inhibitor to promote RNA stability [68,69] .…”

Section: Iran Biomed J 25 (4): 226-242 233mentioning

confidence: 99%

“…ABCE1 inhibits RNase L activation in the mentioned signaling. It is speculated that P benefits from this ABCE1 function to protect RABV RNA from degradation [67] . Further studies are needed to demonstrate this issue.…”

Section: Iran Biomed J 25 (4): 226-242 233mentioning

confidence: 99%

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Rabies Infection: An Overview of Lyssavirus-Host Protein Interactions

Zandi

Goshadrou

Meyfour

et al. 2021

ibj

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List of Abbreviations: 2-5A, 2',5'-oligoadenylate; ABLV, Australian bat lyssavirus; AKT, protein kinase B; AMPK, AMP-activated protein kinase; ATP6V1A, V type proton ATPase catalytic subunit A; CASP, caspase; Cco1, cytochrome c oxidase subunit 1; CCT, T-complex protein 1; CNS, central nervous system; Co-IP, co-immunoprecipitation; CVS, challenge virus standard; DLC1, dynein light chain 1; DUVV, Duvenhage lyssavirus; EBLV-1,2, European bat lyssaviruses type 1 and 2; eIF3h, eukaryotic translation initiation factor 3, subunit h; ESCRT, endosomal sorting complexes required for transport; FAK, focal adhesion kinase; G, glycoprotein;

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hnRNPA1 impedes snakehead vesiculovirus replication via competitively disrupting viral phosphoprotein-nucleoprotein interaction and degrading viral phosphoprotein

Liu

Qin

et al. 2023

Virulence

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Heterogeneous nuclear ribonucleoprotein A1 (hnRNPA1) plays an important role in regulating the replication of many viruses. However, it remains elusive whether and how hnRNPA1 regulates fish virus replication. In this study, the effects of twelve hnRNPs on the replication of snakehead vesiculovirus (SHVV) were screened. Three hnRNPs, one of which was hnRNPA1, were identified as anti-SHVV factors. Further verification showed that knockdown of hnRNPA1 promoted, while overexpression of hnRNPA1 inhibited, SHVV replication. SHVV infection reduced the expression level of hnRNPA1 and induced the nucleocytoplasmic shuttling of hnRNPA1. Besides, we found that hnRNPA1 interacted with the viral phosphoprotein (P) via its glycine-rich domain, but not with the viral nucleoprotein (N) or large protein (L). The hnRNPA1-P interaction competitively disrupted the viral P-N interaction. Moreover, we found that overexpression of hnRNPA1 enhanced the polyubiquitination of the P protein and degraded it through proteasomal and lysosomal pathways. This study will help understanding the function of hnRNPA1 in the replication of single-stranded negative-sense RNA viruses and providing a novel antiviral target against fish rhabdoviruses.

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Host protein ABCE1 interacts with the viral phosphoprotein and promotes rabies virus replication

Cited by 6 publications

References 32 publications

The ATPase ATP6V1A facilitates rabies virus replication by promoting virion uncoating and interacting with the viral matrix protein

The ATPase ATP6V1A facilitates rabies virus replication by promoting virion uncoating and interacting with the viral matrix protein

Rabies Infection: An Overview of Lyssavirus-Host Protein Interactions

hnRNPA1 impedes snakehead vesiculovirus replication via competitively disrupting viral phosphoprotein-nucleoprotein interaction and degrading viral phosphoprotein

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