CSFV proliferation is associated with GBF1 and Rab2

Liang, Wan; Zheng, Minping; Bao, Changlei; Zhang, Yanming

doi:10.1007/s12038-016-9659-0

Cited by 26 publications

(20 citation statements)

References 40 publications

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“…Several viruses of the Picornaviridae , Coronaviridae , and Flaviviridae families rely on GBF1 for their replication (Belov et al, ; Carpp, Rogers, Moritz, & Aitchison, ; Goueslain et al, ; Lanke et al, ; Liang, Zheng, Bao, & Zhang, ; Qin et al, ; van der Linden et al, ; Verheije et al, ; Wang, Du, & Jin, ). However, it has been shown that GBF1 is not involved in the formation of poliovirus, mouse hepatitis coronavirus, and HCV replication complexes but rather in their maturation or activity (Belov et al, ; Goueslain et al, ; Verheije et al, ).…”

Section: Resultsmentioning

confidence: 99%

“…GBF1 also participates in Golgi morphogenesis and lipid droplet metabolism (Jackson & Bouvet, ). In addition, GBF1 is hijacked by several positive‐strand RNA viruses including Picornaviridae , Coronaviridae , and Flaviviridae members for their replication (Belov et al, ; Carpp et al, ; Goueslain et al, ; Lanke et al, ; Liang et al, ; Qin et al, ; van der Linden et al, ; Verheije et al, ; Wang et al, ). For instance, GBF1 was shown to interact with poliovirus and coxsackievirus B3 (CVB3) non‐structural protein 3A (Wessels et al, ; Wessels et al, ).…”

Section: Discussionmentioning

confidence: 99%

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Identification of GBF1 as a cellular factor required for hepatitis E virus RNA replication

Farhat

Ankavay

Lebsir

et al. 2017

Cellular Microbiology

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The hepatitis E virus (HEV) genome is a single-stranded, positive-sense RNA that encodes three proteins including the ORF1 replicase. Mechanisms of HEV replication in host cells are unclear, and only a few cellular factors involved in this step have been identified so far. Here, we used brefeldin A (BFA) that blocks the activity of the cellular Arf guanine nucleotide exchange factors GBF1, BIG1, and BIG2, which play a major role in reshuffling of cellular membranes. We showed that BFA inhibits HEV replication in a dose-dependent manner. The use of siRNA and Golgicide A identified GBF1 as a host factor critically involved in HEV replication. Experiments using cells expressing a mutation in the catalytic domain of GBF1 and overexpression of wild type GBF1 or a BFA-resistant GBF1 mutant rescuing HEV replication in BFA-treated cells, confirmed that GBF1 is the only BFA-sensitive factor required for HEV replication. We demonstrated that GBF1 is likely required for the activity of HEV replication complexes. However, GBF1 does not colocalise with the ORF1 protein, and its subcellular distribution is unmodified upon infection or overexpression of viral proteins, indicating that GBF1 is likely not recruited to replication sites.Together, our results suggest that HEV replication involves GBF1-regulated mechanisms.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Identification of GBF1 as a cellular factor required for hepatitis E virus RNA replication

Farhat

Ankavay

Lebsir

et al. 2017

Cellular Microbiology

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“…This result suggests that AIF1 has a positive effect on CSFV Shimen infection in macrophages. Many cytokines of host maybe affect CSFV replication (Liang et al, 2016), and we considered AIF1-mediated microenvironment in PAM 3D4/21 cells contributed to CSFV Shimen infection. However, more detailed studies are required to consider this finding, and whether the AIF1 could inhibit other viruses also needs further investigations.…”

Section: Discussionmentioning

confidence: 99%

AIF1 was identified as an up-regulated gene contributing to CSFV Shimen infection in porcine alveolar macrophage 3D4/21 cells

Gong

You

et al. 2020

PeerJ

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Classical swine fever (CSF) is a disease that is characterized by diffuse hemorrhaging, high fever, and high mortality rates. The pro-inflammatory characteristics of allograft inflammatory factor 1 (AIF1) have been well documented; however, insufficient attention has been given to porcine AIF1. In the present study, AIF1 was identified as a key player contributing to CSFV Shimen infection in porcine alveolar macrophage (PAM) 3D4/21 cell line. Our evaluation showed that AIF1 mRNA and protein are expressed at a time-dependent high level in CSFV Shimen-infected PAM 3D4/21 cells. The transcription and translation of IL6 were also significantly upregulated in infected PAM 3D4/21 cells. By utilizing overexpression RNAs approach, we showed that the cellular AIF1 induced an increased IL6 in PAM 3D4/21 cells. Furthermore, silencing of AIF1 suppressed CSFV Shimen-induced IL6 production in PAM 3D4/21 cells and also inhibited CSFV replication, whereas overexpression of recombinant AIF1 was beneficial for the replication of CSFV Shimen and promoting IL6 production in CSFV Shimen-infected PAM 3D4/21 cells. It is suggested CSFV Shimen induced IL6 in PAM 3D4/21 cells via AIF1 activation, which help clarify the AIF1-related inflammatory processes that occur on CSFV Shimen infected macrophages.

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“…In the case of influenza (61, 62) and vesicular stomatitis viruses (VSV) (63, 64) the COPI/Arf1 complex seems to play a role in their entry process. Moreover, for VSV as well as for hepatitis C virus (65–67), mouse hepatitis coronavirus (68), chikungunya virus (69), poliovirus (57, 58, 70), coxsackievirus (71) and classical swine fever virus (72), COPI/Arf1 has been shown to be necessary for genome replication as well as for viral protein expression. COPI/Arf1 has also been shown to be critical for viral particle assembly of influenza and the Chandipura virus (62, 73).…”

Section: Discussionmentioning

confidence: 99%

The guanine nucleotide exchange factor GBF1 participates in rotavirus replication

Martínez

Arnoldi

Schraner

et al. 2019

Preprint

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19Cellular and viral factors participate in the replication cycle of rotavirus. We report that the 20 guanine nucleotide exchange factor GBF1, which activates the small GTPase Arf1 to induce 21 COPI transport processes, is required for rotavirus replication since knocking down GBF1 22 3 IMPORTANCE 40 Rotavirus, a member of the family Reoviridae, is the major cause of severe diarrhea in 41 children and young animals worldwide. Despite the significant advances in the 42 characterization of the biology of this virus, the mechanisms involved in morphogenesis of 43 the virus particle are still poorly understood. In this work, we show that the guanine 44 nucleotide exchange factor GBF1, relevant for the COPI/Arf1-mediated cellular vesicular 45 transport, participates in the replication cycle of the virus, influencing the correct processing 46 of viral glycoproteins VP7 and NSP4, and the assembly of the virus surface proteins VP7 47 59 Rotaviruses, members of the family Reoviridae, are non-enveloped particles formed by three 60 concentric layers of proteins that surround the eleven genome segments of double-stranded 61 RNA (dsRNA). The innermost layer is composed of the core-shell proteinVP2 that encloses 62 the replication intermediates, composed of the RNA dependent RNA polymerase VP1, and 63 the guanylyl-methyl transferase, VP3. The intermediate layer is formed by VP6 that 64 surrounds the VP2 layer to form double-layered particles (DLPs). Finally, the addition of the 65 glycoprotein VP7 and the spike protein VP4 onto the DLPs forms the infectious triple-layered 66 particles (TLPs) (1, 2). 67 The replication of rotavirus occurs in cytoplasmic non-membranous electron-dense 68 inclusions termed viroplasms composed of NSP2, NSP5, VP1, VP2, VP6 and host 69 components (1, 3). The replication and packaging of the viral genome into newly synthesized 70DLPs take place in these inclusions (4), which then bud into the lumen of the endoplasmic 71 reticulum (ER) through membrane sites modified by the presence of NSP4 (5, 6). NSP4 is a 72 transmembrane ER glycoprotein with two N-linked high mannose glycosylated chains (7) 73 that play a crucial role in the last steps of rotavirus assembly. It has been shown that the 74 cytoplasm oriented-terminus of NSP4 associates with VP4 (8), and binds the VP6 on DLPs 75 acting as a receptor for these particles to mediate their budding into the ER (9, 10). Moreover, 76 NSP4 has been shown to also interact with VP7 through its N-terminus oriented to the ER 77 lumen (11, 12). It has been proposed that these interactions drive the incorporation of the 78 outer layer proteins into the transitory lipid envelope that DLPs acquire during ER membrane 79 budding; this envelope is removed in the lumen of the ER by an unknown process in which 80 NSP4 is eliminated while VP4 and VP7 are assembled to produce the final infectious TLPs 81 All rights reserved. No reuse allowed without permission.The copyright holder for this preprint (which was not peer-reviewed) is the author/funder. . https://doi.org/10.110...

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CSFV proliferation is associated with GBF1 and Rab2

Cited by 26 publications

References 40 publications

Identification of GBF1 as a cellular factor required for hepatitis E virus RNA replication

Identification of GBF1 as a cellular factor required for hepatitis E virus RNA replication

AIF1 was identified as an up-regulated gene contributing to CSFV Shimen infection in porcine alveolar macrophage 3D4/21 cells

The guanine nucleotide exchange factor GBF1 participates in rotavirus replication

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