Mechanism and Complex Roles of HSC70 in Viral Infections

Wang, Zeng; Li, Yongtao; Yang, Xia; Zhao, Jingpeng; Cheng, Yuhua; Wang, Jianke

doi:10.3389/fmicb.2020.01577

Cited by 30 publications

(29 citation statements)

References 88 publications

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“…During the assembly and budding process, M protein is performing a dominant aspect in retaining the S protein by its interaction. It interacts with N protein, assists in RNA packaging and functions in viral immunoevasion [74] , [75] . The envelope (E) protein is a smallest single-pass type ΙΙΙ transmembrane protein (8 kDa), consists of approximately 76–109 aa that are prevailing in tiny amounts on the viral envelope [76] , as shown in Fig.…”

Section: Genome and Structure Of Sars-cov-2mentioning

confidence: 99%

COVID-19: A review of newly formed viral clades, pathophysiology, therapeutic strategies and current vaccination tasks

Murugan

Ramamoorthy

Kuppuswamy

et al. 2021

International Journal of Biological Macromolecules

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Today, the world population is facing an existential threat by an invisible enemy known as severe acute respiratory syndrome coronavirus 2 (SARS-COV-2) or COVID-19. It is highly contagious and has infected a larger fraction of human population across the globe on various routes of transmission. The detailed knowledge of the SARS-CoV-2 structure and clinical aspects offers an important insight into the evolution of infection, disease progression and helps in executing the different therapies effectively. Herein, we have discussed in detail about the genome structure of SARS-CoV-2 and its role in the proteomic rational spread of different muted species and pathogenesis in infecting the host cells. The mechanisms behind the viral outbreak and its immune response, the availability of existing diagnostics techniques, the treatment efficacy of repurposed drugs and the emerging vaccine trials for the SARS-CoV-2 outbreak also have been highlighted. Furthermore, the possible antiviral effects of various herbal products and their extracted molecules in inhibiting SARS-CoV-2 replication and cellular entry are also reported. Finally, we conclude our opinion on current challenges involved in the drug development, bulk production of drug/vaccines and their storage requirements, logistical procedures and limitations related to dosage trials for larger population.

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Section: Genome and Structure Of Sars-cov-2mentioning

confidence: 99%

COVID-19: A review of newly formed viral clades, pathophysiology, therapeutic strategies and current vaccination tasks

Murugan

Ramamoorthy

Kuppuswamy

et al. 2021

International Journal of Biological Macromolecules

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“…In the metabolic pathway of antigen processing and presentation, HSP70 is closely related to virus-induced host immune response through presenting antigenic peptides by MHC-II to CD4 + T cells (Auger et al, 1996). HSP70 assists in the release and recycle of clathrin to form the endosome, preparing for membrane fusion and transporting exogenous cargos to the subcellular sites, and it is no doubt to play an integral role in virus invasion (Wang et al, 2020). In the protein interaction sub-network, the protein directly interacting with HSP70 was GAK (cyclin G-associated kinase; Figure 7b and Table 6).…”

Section: Discussionmentioning

confidence: 99%

Transcriptome analysis reveals immune‐related differentially expressed genes in the hepatopancreas and gills of Penaeus vannamei after Vibrio anguillarum infection

Song

Soomro

et al. 2021

Aquaculture Research

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Penaeus vannamei is one of the commercially important aquaculture species in the world but sensitive to Vibrio anguillarum infection. To understand the immune response of P. vannamei against V. anguillarum infection, the transcriptomes of hepatopancreas and gills of P. vannamei were analysed before and after V. anguillarum infection. Total 6213 differentially expressed genes (DEGs) were obtained from the hepatopancreas, and 3780 were obtained from the gills. The DEGs of interest were screened to construct a heat map. The reliability and accuracy of the transcriptome data were verified using RT‐qPCR. HSP70 and ARF6 were found highly expressed in both hepatopancreas and gills, while MLC2s encoded by two different gene sequences were found to be expressed in hepatopancreas and gills. Six immune‐related DEGs were identified from the protein–protein interaction (PPI) network including the HSP70, ARF6 and MLC2s. The sub‐network of PPI was constructed to explore the mode of interaction of immune‐related DEGs with their neighbouring proteins. Based on the result of PPI network, we infer that phosphorylated MLC2‐1 conducts signal transduction to induce leukocyte transendothelial migration in P. vannamei gills tissue while MLC2‐2 plays a role in immunity of V. anguillarum infection not only through activating signal transduction to mediate immune responses but also through the formation of phagosomes in hepatopancreas tissue. HSP70 is associated with the transporting exogenous cargos through presenting antigenic peptides in the process of V. anguillarum infection in P. vannamei. ARF6 interacts with Rab proteins to regulate phagolysosome formation by regulating GTPase activity in P. vannamei gills tissue. In hepatopancreas tissue, ARF6 plays a role in immunity by interacting with cytohesin. This study will contribute to further exploring the immune mechanism of P. vannamei to V. anguillarum infection.

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“…The initially low affinity increases significantly after ATP is hydrolyzed to ADP by the cochaperone HSP40. Finally, with the help of nucleotide exchange factors, ADP dissociates to reset the cycle [15]. The most important functions of the HSP70 isoforms are presented in Table 1.…”

Section: Characteristics Of Selected Hsp's 21 Hsp70mentioning

confidence: 99%

Role of Heat Shock Proteins (HSP70 and HSP90) in Viral Infection

Lubkowska

Pluta

Strońska

et al. 2021

IJMS

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Heat shock proteins (HSPs) are a large group of chaperones found in most eukaryotes and bacteria. They are responsible for the correct protein folding, protection of the cell against stressors, presenting immune and inflammatory cytokines; furthermore, they are important factors in regulating cell differentiation, survival and death. Although the biological function of HSPs is to maintain cell homeostasis, some of them can be used by viruses both to fold their proteins and increase the chances of survival in unfavorable host conditions. Folding viral proteins as well as replicating many different viruses are carried out by, among others, proteins from the HSP70 and HSP90 families. In some cases, the HSP70 family proteins directly interact with viral polymerase to enhance viral replication or they can facilitate the formation of a viral replication complex and/or maintain the stability of complex proteins. It is known that HSP90 is important for the expression of viral genes at both the transcriptional and the translational levels. Both of these HSPs can form a complex with HSP90 and, consequently, facilitate the entry of the virus into the cell. Current studies have shown the biological significance of HSPs in the course of infection SARS-CoV-2. A comprehensive understanding of chaperone use during viral infection will provide new insight into viral replication mechanisms and therapeutic potential. The aim of this study is to describe the molecular basis of HSP70 and HSP90 participation in some viral infections and the potential use of these proteins in antiviral therapy.

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Mechanism and Complex Roles of HSC70 in Viral Infections

Cited by 30 publications

References 88 publications

COVID-19: A review of newly formed viral clades, pathophysiology, therapeutic strategies and current vaccination tasks

COVID-19: A review of newly formed viral clades, pathophysiology, therapeutic strategies and current vaccination tasks

Transcriptome analysis reveals immune‐related differentially expressed genes in the hepatopancreas and gills of Penaeus vannamei after Vibrio anguillarum infection

Role of Heat Shock Proteins (HSP70 and HSP90) in Viral Infection

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