Structural and nonstructural proteins of Senecavirus A: Recent research advances, and lessons learned from those of other picornaviruses

Wang, Qianqian; Meng, Hailan; Ge, Dong; Shan, Hu; Geri, Letu; Liu, Fuxiao

doi:10.1016/j.virol.2023.06.004

Cited by 11 publications

(4 citation statements)

References 112 publications

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“…Studies on enteroviruses and apthoviruses have demonstrated that 3CD pro can cleave at VP2-VP3 and VP3-P1 more effectively than 3C [56,57]. SVV 3C protease cleaves the P1 polypeptide to provide VP0, VP1, and VP3 [58]. Most 3C proteases cleave at single sites such as (Q|G), (Q|S), (Q|R), (E|Q), and (E|G) [7] (see Table 1 for example).…”

Section: Viral Polyprotein Processing and Substrate Recognitionmentioning

confidence: 99%

“…CVB-3C activates caspase-9-based apoptosis through caspase 3 activation [127]. 3C is essential for SVV-mediated apoptosis following caspase 3, while HAV 3C Seneca Valley Virus 3C (SVV 3C) cleaves eukaryotic initiation factors (eIFs) eIF4AI and eIF4G1, while PV, CVB, and HRV 3C proteases cleave eIF5B [18,58,63,93,113]. eIF4AI inhibition alters eIF4AII protein expression [114].…”

Section: C-promoted Apoptosis For Virus Releasementioning

confidence: 99%

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Picornavirus 3C Proteins Intervene in Host Cell Processes through Proteolysis and Interactions with RNA

Mondal,

Sarvari,

Boehr

2023

Viruses

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The Picornaviridae family comprises a large group of non-enveloped viruses with enormous impact on human and animal health. The picornaviral genome contains one open reading frame encoding a single polyprotein that can be processed by viral proteases. The picornaviral 3C proteases share similar three-dimensional structures and play a significant role in the viral life cycle and virus–host interactions. Picornaviral 3C proteins also have conserved RNA-binding activities that contribute to the assembly of the viral RNA replication complex. The 3C protease is important for regulating the host cell response through the cleavage of critical host cell proteins, acting to selectively ‘hijack’ host factors involved in gene expression, promoting picornavirus replication, and inactivating key factors in innate immunity signaling pathways. The protease and RNA-binding activities of 3C are involved in viral polyprotein processing and the initiation of viral RNA synthesis. Most importantly, 3C modifies critical molecules in host organelles and maintains virus infection by subtly subverting host cell death through the blocking of transcription, translation, and nucleocytoplasmic trafficking to modulate cell physiology for viral replication. Here, we discuss the molecular mechanisms through which 3C mediates physiological processes involved in promoting virus infection, replication, and release.

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Section: Viral Polyprotein Processing and Substrate Recognitionmentioning

confidence: 99%

Section: C-promoted Apoptosis For Virus Releasementioning

confidence: 99%

Picornavirus 3C Proteins Intervene in Host Cell Processes through Proteolysis and Interactions with RNA

Mondal,

Sarvari,

Boehr

2023

Viruses

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“…Among the SVA structural proteins, the VP1, VP2, and VP3 proteins are exposed on the virion surface and are responsible for stimulating host immune responses and binding to host receptors, while VP4 is located internally and interacts with internal nucleic acids (Strauss et al, 2018 ). In addition, VP2 is crucial for determining the cell tropism of SVA (Wang et al, 2023 ) and mediating virus binding to the cell receptor anthrax toxin receptor 1 (ANTXR1) (Miles et al, 2017 ). Although VP2 is the major structural protein that induces neutralizing antibodies (Dvorak et al, 2016 ; Maggioli et al, 2018 ; Wen et al, 2022 ), few neutralizing epitopes have been identified.…”

Section: Introductionmentioning

confidence: 99%

Identification of a linear B-cell epitope on the “puff” loop of the Senecavirus A VP2 protein involved in receptor binding

Zhou,

Sun,

et al. 2024

Front. Microbiol.

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Senecavirus A (SVA) is an important emerging swine pathogen that causes vesicular lesions in swine and acute death in newborn piglets. VP2 plays a significant role in the production of antibodies, which can be used in development of diagnostic tools and vaccines. Herein, the aim of the current study was to identify B-cell epitopes (BCEs) of SVA for generation of epitope-based SVA marker vaccine. Three monoclonal antibodies (mAbs), named 2E4, 1B8, and 2C7, against the SVA VP2 protein were obtained, and two novel linear BCEs, 177SLGTYYR183 and 266SPYFNGL272, were identified by peptide scanning. The epitope 177SLGTYYR183 was recognized by the mAb 1B8 and was fully exposed on the VP2 surface, and alanine scanning analysis revealed that it contained a high continuity of key amino acids. Importantly, we confirmed that 177SLGTYYR183 locates on “the puff” region within the VP2 EF loop, and contains three key amino acid residues involved in receptor binding. Moreover, a single mutation, Y182A, blocked the interaction of the mutant virus with the mAb 1B8, indicating that this mutation is the pivotal point for antibody recognition. In summary, the BCEs that identified in this study could be used to develop diagnostic tools and an epitope-based SVA marker vaccine.

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“…Their 60 copies form an icosahedral capsid with the typical architecture of picornavirus. The other proteins are non-structural proteins, involved in viral genome replication, host cell metabolism, and immune evasion ( 13 ). Mutual replication between genome and antigenome is catalyzed by a picornavirus-encoded RNA-dependent RNA polymerase (RdRp), also termed 3D polymerase ( 14 ).…”

Section: Introductionmentioning

confidence: 99%

RNA recombination: non-negligible factor for preventing emergence or reemergence of Senecavirus A

Li,

Liu,

Zhang

et al. 2024

Front. Vet. Sci.

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Structural and nonstructural proteins of Senecavirus A: Recent research advances, and lessons learned from those of other picornaviruses

Cited by 11 publications

References 112 publications

Picornavirus 3C Proteins Intervene in Host Cell Processes through Proteolysis and Interactions with RNA

Picornavirus 3C Proteins Intervene in Host Cell Processes through Proteolysis and Interactions with RNA

Identification of a linear B-cell epitope on the “puff” loop of the Senecavirus A VP2 protein involved in receptor binding

RNA recombination: non-negligible factor for preventing emergence or reemergence of Senecavirus A

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