ArticleVeterinary research2018
Annexin A2 binds to vimentin and contributes to porcine reproductive and respiratory syndrome virus multiplication.
Article in Veterinary research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 25 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
25 citing papers in PubMed, 45 citations in OpenAlex.
- Crosstalk between vimentin and keratins in viral infection: Implications across the viral life cycle.Virulence · 2026Review
- ANXA2 suppresses antiviral immunity by impeding STING Golgi translocation and disrupting the TBK1/IKKε-IRF3 axis.Journal of virology · 2026Article
- Annexin A2 negatively regulates IFN-β production through targeting the RLR signaling pathway.Journal of virology · 2026Article
- Nuclear factor IC promoting porcine reproductive and respiratory syndrome virus (PRRSV) replication and suppressing type I interferon transcription.BMC veterinary research · 2026Article
- Ipriflavone Inhibits Porcine Reproductive and Respiratory Syndrome Virus Infection via RIG-I/IRF3-Mediated Interferon Signaling.Animals : an open access journal from MDPI · 2025Article
- Strategies and scheming: the war between PRRSV and host cells.Virology journal · 2025Review
- Annexin A2 Contributes to Release of Extracellular Vimentin in Response to Inflammation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Article
- Molecular breeding of pigs in the genome editing era.Genetics, selection, evolution : GSE · 2025Review
- Article
- Knockdown of annexin A2 enhances the host cell apoptosis induced byFrontiers in veterinary science · 2025Article
- Calycosin inhibits porcine reproductive and respiratory syndrome virus replication and activates RIG-I/IRF3 signaling pathway.Frontiers in veterinary science · 2025Article
- Annexin A2: A Double-Edged Sword in Pathogen Infection.Pathogens (Basel, Switzerland) · 2024Review
- FADD promotes type I interferon production to suppress porcine reproductive and respiratory syndrome virus infection.Frontiers in veterinary science · 2024Article
- Candidate proteins interacting with cytoskeleton in cells from the basal airway epitheliumFrontiers in molecular biosciences · 2024Article
- Review
- Extracellular Vimentin as a Target Against SARS-CoV-2 Host Cell Invasion.Small (Weinheim an der Bergstrasse, Germany) · 2022Article
- Article
- Reappraising host cellular factors involved in attachment and entry to develop antiviral strategies against porcine reproductive and respiratory syndrome virus.Frontiers in microbiology · 2022Review
- Extracellular vimentin as a target against SARS-CoV-2 host cell invasion.bioRxiv : the preprint server for biology · 2021Article
- Mechanical and Non-Mechanical Functions of Filamentous and Non-Filamentous Vimentin.BioEssays : news and reviews in molecular, cellular and developmental biology · 2020Review
Corrections and comments
- Erratum issued
Authors and funding
11 authors at 2 institutions in 1 country.
Funding
Abstract
Porcine reproductive and respiratory syndrome virus (PRRSV) is an important globally distributed and highly contagious pathogen that has restricted cell tropism in vivo and in vitro. In the present study, we found that annexin A2 (ANXA2) is upregulated expressed in porcine alveolar macrophages infected with PRRSV. Additionally, PRRSV replication was significantly suppressed after reducing ANXA2 expression in Marc-145 cells using siRNA. Bioinformatics analysis indicated that ANXA2 may be relevant to vimentin, a cellular cytoskeleton component that is thought to be involved in the infectivity and replication of PRRSV. Co-immunoprecipitation assays and confocal analysis confirmed that ANXA2 interacts with vimentin, with further experiments indicating that the B domain (109-174 aa) of ANXA2 contributes to this interaction. Importantly, neither ANXA2 nor vimentin alone could bind to PRRSV and only in the presence of ANXA2 could vimentin interact with the N protein of PRRSV. No binding to the GP2, GP3, GP5, nor M proteins of PRRSV was observed. In conclusion, ANXA2 can interact with vimentin and enhance PRRSV growth. This contributes to the regulation of PRRSV replication in infected cells and may have implications for the future antiviral strategies.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.