Hsp70 Inhibits the Replication of Fowl Adenovirus Serotype 4 by Suppressing Viral Hexon with the Assistance of DnaJC7

Cao, Jie; Liu, Shuhui; Li, Meng; Wang, Shuaiwen; Bi, Zhenwei; Fan, Wentao; Shi, Zhiyu; Song, Suquan; Yan, Liping

doi:10.1128/jvi.00807-22

Cited by 4 publications

(3 citation statements)

References 54 publications

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“…HSP70 is also involved in multiple stages of virus proliferation [55]. HSP70 was recently found to have important functions in different viruses [32,[55][56][57]. At present, HSP70 has been validated as a host antiviral target in dengue virus (DENV), bovine viral diarrhoea virus (BVDV), flavivirus, grass carp reovirus (GCRV) and respiratory syncytial virus (RSV) infections [33,52,56,58].…”

Section: Discussionmentioning

confidence: 99%

Drug screening identified that handelin inhibits feline calicivirus infection by inhibiting HSP70 expression in vitro

Yan,

Yang,

Jiao

et al. 2024

Journal of General Virology

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Feline calicivirus (FCV) is considered one of the major pathogens of cats worldwide and causes upper respiratory tract disease in all cats. In some cats, infection is by a highly virulent strain of FCV (vs.-FCV), which can cause severe and fatal systemic disease symptoms. At present, few antiviral drugs are approved for clinical treatment against FCV. Therefore, there is an imminent need for effective FCV antiviral agents. Here, we used observed a cytopathic effect (CPE) assay to screen 1746 traditional Chinese medicine monomer compounds and found one that can effectively inhibit FCV replication, namely, handelin, with an effective concentration (EC50) value of approximately 2.5 µM. Further study showed that handelin inhibits FCV replication via interference with heat shock protein 70 (HSP70), which is a crucial host factor and plays a positive role in regulating viral replication. Moreover, handelin and HSP70 inhibitors have broad-spectrum antiviral activity. These findings indicate that handelin is a potential candidate for the treatment of FCV infection and that HSP70 may be an important drug target.

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Section: Discussionmentioning

confidence: 99%

Drug screening identified that handelin inhibits feline calicivirus infection by inhibiting HSP70 expression in vitro

Yan,

Yang,

Jiao

et al. 2024

Journal of General Virology

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“…These chaperone proteins participate not only in cellular proteostasis, but also in response to stress conditions. Growing evidence has indicated that during virus infection, host cellular Hsc70 and/or Hsp70 proteins were suggested to be involved in virus infection through interactions with viral proteins (Mayer, 2005;Park et al, 2021), such as HCV (Chen et al, 2010), ZIKV (Pujhari et al, 2019), influenza A virus (Manzoor et al, 2014), transmissible gastroenteritis virus (TGEV) (Ji et al, 2023), fowl adenovirus serotype 4 (Cao et al, 2022), porcine reproductive and respiratory syndrome virus (PRRSV) (Wang et al, 2022), classical swine fever virus (Zhang et al, 2015), PEDV (Park et al, 2021), tombusvirus (Wang et al, 2009), reovirus (Ivanovic et al, 2007), adenovirus (Glotzer et al, 2000), polyomavirus (Chromy et al, 2003), and DENV (Taguwa et al, 2015). Hsp70s share at least two functional domains: a 45 kDa NBD at N-terminal and a 25 kDa SBD at C-terminal, and the two domains are mainly responsible for Hsp70s regulatory functions such as protein folding, assembly, transferring, degradation and protection of cell against stressors (Rosenzweig et al, 2019).…”

Section: Many Viruses Rely On Host Cells For Viral Replication and Pr...mentioning

confidence: 99%

Chaperones Hsc70 and Hsp70 play distinct roles in the replication of bocaparvovirus minute virus of canines

Guo,

Yan,

Sun

et al. 2024

Molecular Microbiology

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Minute virus of canines (MVC) belongs to the genus Bocaparvovirus (formerly Bocavirus) within the Parvoviridae family and causes serious respiratory and gastrointestinal symptoms in neonatal canines worldwide. A productive viral infection relies on the successful recruitment of host factors for various stages of the viral life cycle. However, little is known about the MVC‐host cell interactions. In this study, we identified that two cellular proteins (Hsc70 and Hsp70) interacted with NS1 and VP2 proteins of MVC, and both two domains of Hsc70/Hsp70 were mediated for their interactions. Functional studies revealed that Hsp70 was induced by MVC infection, knockdown of Hsc70 considerably suppressed MVC replication, whereas the replication was dramatically promoted by Hsp70 knockdown. It is interesting that low amounts of overexpressed Hsp70 enhanced viral protein expression and virus production, but high amounts of Hsp70 overexpression weakened them. Upon Hsp70 overexpressing, we observed that the ubiquitination of viral proteins changed with Hsp70 overexpression, and proteasome inhibitor (MG132) restored an accumulation of viral proteins. In addition, we verified that Hsp70 family inhibitors remarkably decreased MVC replication. Overall, we identified Hsc70 and Hsp70 as interactors of MVC NS1 and VP2 proteins and were involved in MVC replication, which may provide novel targets for anti‐MVC approach.

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“…Three main structural proteins, namely fiber, hexon, and penton base, constitute the capsid of FAdVs [ 5 , 6 ]. Hexon proteins play significant roles in the pathogenicity and replication of FAdV-4 [ 7 , 8 , 9 , 10 , 11 ]. The penton base is the vertex of the icosahedron on which two separate fiber proteins are anchored [ 4 ].…”

Section: Introductionmentioning

confidence: 99%

The Development of a Novel Fiber-2 Subunit Vaccine against Fowl Adenovirus Serotype 4 Formulated with Oil Adjuvants

Liu,

Wang

et al. 2024

Vaccines

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Hepatitis-hydropericardium syndrome (HHS), caused by fowl adenovirus serotype 4 (FAdV-4), has been widely spread across China, resulting in great financial losses in the poultry industry. Therefore, efficient vaccines against this disease urgently need to be developed. In our study, the fiber-2 and penton base proteins derived from the FAdV-4 JS strain were expressed in a prokaryotic system (E. coli) in a soluble form. Then, the efficacy of the two recombinant proteins formulated with cheap and widely used adjuvants (Marcol™ 52 white oil) were respectively tested, and the minimum immune doses and safety of the above proteins were also determined. It was indicated that the fiber-2 (20 µg/bird, 200 µg/bird) and penton base (200 µg/bird) could provide complete protection against the highly pathogenic FAdV-4 and suppress its replication and shedding. Unfortunately, only the fiber-2 protein could induce complete protection (10/10) at a low dose (10 µg/bird). In addition, we confirmed that the fiber-2 subunit vaccine formulated with oil adjuvants was safe for vaccinated chickens. Conclusively, all of our results suggest that we successfully prepared an efficient and cheap fiber-2 subunit vaccine with few side effects.

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Hsp70 Inhibits the Replication of Fowl Adenovirus Serotype 4 by Suppressing Viral Hexon with the Assistance of DnaJC7

Abstract: FAdV-4, as the main cause of HHS, has quickly spread all over the world in recent years, seriously threatening the poultry industry. The aim of this study was to identify the important host proteins that have the potential to regulate the life cycle of FAdV-4.

Cited by 4 publications

References 54 publications

Drug screening identified that handelin inhibits feline calicivirus infection by inhibiting HSP70 expression in vitro

Drug screening identified that handelin inhibits feline calicivirus infection by inhibiting HSP70 expression in vitro

Chaperones Hsc70 and Hsp70 play distinct roles in the replication of bocaparvovirus minute virus of canines

The Development of a Novel Fiber-2 Subunit Vaccine against Fowl Adenovirus Serotype 4 Formulated with Oil Adjuvants

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