Skip to content
Open access

Enteroviruses antagonize the host restriction factor ABL2 via proteasomal degradation to facilitate viral replication

Aug 2026 · Virologica Sinica · Vol 41, pp. 855 - 867 · 0 citations · 39 references
Medicine

TL;DR

This study reveals a post-translational mechanism by which enteroviruses evade host antiviral defenses, providing a rationale for therapeutic development against enteroviral diseases.

Abstract

Enteroviruses, including Coxsackievirus B3 (CVB3), are significant human pathogens that cause severe diseases, such as viral myocarditis, pancreatitis, and encephalitis. ABL proto-oncogene 2 (ABL2), a non-receptor tyrosine-protein kinase, regulates diverse physiological processes and participates in virus infection; however, its role in enterovirus infection remains uncharacterized. Here, we demonstrate a novel host-virus interaction: enteroviruses degrade ABL2 via the ubiquitin-proteasome system through their non-structural protein 2B. Furthermore, ABL2 functions as an antiviral restriction factor during enterovirus infection, specifically inhibiting the early stages of viral replication. Mechanistically, ABL2 directly interacts with RAC1, a Rho family GTPase, and downregulates RAC1 protein levels, thereby suppressing RAC1-dependent activation of the PI3K/AKT signaling pathway. In summary, our study reveals a post-translational mechanism by which enteroviruses evade host antiviral defenses, providing a rationale for therapeutic development against enteroviral diseases.

Read PDF

Similar papers

Open access Aug 2026

Carboxypeptidase A6 contributes to bovine enterovirus F production through apoptosis-associated PI3K/AKT/FOXO1 signaling

A genome-wide CRISPR/Cas9 loss-of-function screen in Madin–Darby bovine kidney cells identifies CPA6 as a previously unrecognized host factor for BEV-F infection, support a model in which CPA6 is functionally associated with PI3K/AKT/FOXO1 signaling related to apoptosis, and suggest that carboxypeptidase-associated pat...

Yuanchen Geng, Hao Yang, Qimeng Wu et al. · 0 citations
Open access Oct 2026

The Golgi-resident protein ACBD3 facilitates the interaction between enteroviral 3A proteins and Exportin-1.

Enteroviruses are among the most common viral pathogens in humans, causing illnesses ranging from the common cold to severe and sometimes life-threatening diseases such as acute haemorrhagic conjunctivitis or poliomyelitis. To replicate efficiently within host cells, enteroviruses hijack several host factors, including...

Vladimira Horova, Michala Zgarbová, M. Klíma et al. · 0 citations
Open access Sep 2026

LY6E regulates Pseudorabies virus early infection via impairing viral internalization

This study identifies LY6E as a previously unrecognized host restriction factor for PRV and highlights the role of surface proteins in controling viral entry, which broadens the antiviral spectrum of LY6E to DNA viruses, beyond its previously reported host–viral interaction in RNA viruses.

Tanveer Ali Fazlani, Tian-Xing Cao, Yi-Chao Wang et al. · 0 citations
Review Open access Oct 2026

Enterovirus 2B protein: From viroporin to membrane stress sensor, mechanistic principles of multi-pathway regulation

ABSTRACT Enterovirus 2B is a highly conserved, functionally versatile, nonstructural protein. The classic viroporin model, which restricts its role to ion channel formation, cannot account for its interactions with host factors such as Bcl-2-associated X protein, interleukin enhancer-binding factor 2, and karyopherin s...

Zeng-Jun Ji, Yi-Kun Chen, Hong-Xing Shen · 0 citations
Review Open access Sep 2026

Molecular Mechanisms Between Canine Parvovirus 2 and Host Interactions: From Viruses to Innate Immune Signaling Pathways

This review summarizes the innate immunity evasion tactics employed by CPV-2, focusing on the interactions of various viral proteins and host signaling pathways, and identifies the key mechanisms underlying the defective TLR activation.

Guan-Yu Zhao, Xin-Ying Yang, Yue-Hua Li et al. · 0 citations

We use cookies to run the site and, with your consent, for analytics and to show ads. See our Cookie Policy.