Critical role of G3BP1 in bovine parainfluenza virus type 3 (BPIV3)-inhibition of stress granules formation and viral replication

Front Immunol. 2024 Apr 16:15:1358036. doi: 10.3389/fimmu.2024.1358036. eCollection 2024.

Abstract

Background: It remains unclear whether BPIV3 infection leads to stress granules formation and whether G3BP1 plays a role in this process and in viral replication. This study aims to clarify the association between BPIV3 and stress granules, explore the effect of G3BP1 on BPIV3 replication, and provide significant insights into the mechanisms by which BPIV3 evades the host's antiviral immunity to support its own survival.

Methods: Here, we use Immunofluorescence staining to observe the effect of BPIV3 infection on the assembly of stress granules. Meanwhile, the expression changes of eIF2α and G3BP1 were determined. Overexpression or siRNA silencing of intracellular G3BP1 levels was examined for its regulatory control of BPIV3 replication.

Results: We identify that the BPIV3 infection elicited phosphorylation of the eIF2α protein. However, it did not induce the assembly of stress granules; rather, it inhibited the formation of stress granules and downregulated the expression of G3BP1. G3BP1 overexpression facilitated the formation of stress granules within cells and hindered viral replication, while G3BP1 knockdown enhanced BPIV3 expression.

Conclusion: This study suggest that G3BP1 plays a crucial role in BPIV3 suppressing stress granule formation and viral replication.

Keywords: BPIV3; G3BP1; inhibition; stress granules; viral replication.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cattle
  • Cell Line
  • Cytoplasmic Granules / metabolism
  • DNA Helicases* / genetics
  • DNA Helicases* / metabolism
  • Eukaryotic Initiation Factor-2 / metabolism
  • Host-Pathogen Interactions / immunology
  • Phosphorylation
  • Poly-ADP-Ribose Binding Proteins* / genetics
  • Poly-ADP-Ribose Binding Proteins* / metabolism
  • RNA Helicases* / genetics
  • RNA Helicases* / metabolism
  • RNA Recognition Motif Proteins* / metabolism
  • Respirovirus Infections / immunology
  • Respirovirus Infections / metabolism
  • Stress Granules* / metabolism
  • Virus Replication*

Substances

  • Poly-ADP-Ribose Binding Proteins
  • RNA Recognition Motif Proteins
  • DNA Helicases
  • RNA Helicases
  • Eukaryotic Initiation Factor-2

Grants and funding

The author(s) declare financial support was received for the research, authorship, and/or publication of this article. Financial support for this study was provided by grants from the National Science and Technology Support Project (2012BAD12B03-3, 2012BAD12B05-2), Natural Science Foundation of Heilongjiang Province (LH2022C037, LH2023C023) and the Science and Technology Planning Project of Heilongjiang Province (GC12B303). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.