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New research reveals cell proteins that drive severe viral infections

Phys · · 694 words · By Ingrid Söderbergh

Researchers at Umeå University identified two human cell proteins, NUP98 and NUP153, that are crucial for the replication of various viruses, including TBEV, West Nile, and dengue. The findings suggest that targeting these host cell proteins could provide a new strategy for developing antiviral drugs, as the proteins regulate viral replication and protein expression. The study also identified a small peptide that can block NUP98's binding to viral RNA, leading to reduced viral replication.

open_in_new Read the original article: https://phys.org/news/2026-04-reveals-cell-proteins-severe-viral.html

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fact_checkFact-Check Results

13 claims extracted and verified against multiple sources including cross-references, web search, and Wikipedia.

check_circle Corroborated 7
schedule Pending 3
help Insufficient Evidence 2
info Single Source 1
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“Researchers at Umeå University have identified two human cell proteins, NUP98 and NUP153, that play a crucial role in how viruses such as tick-borne encephalitis virus (TBEV), West Nile virus, and dengue virus replicate in the body.”
CORROBORATED
Multiple web search results report that researchers at Umeå University identified NUP98 and NUP153 as key proteins involved in the replication of TBEV, West Nile virus, and dengue virus. This is reported across different search snippets referencing the same research findings.
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web search NEUTRAL — Researchers at Umeå University have identified two human cell proteins, NUP98 and NUP153, that play a crucial role in how viruses such as tick-borne encephalitis virus (TBEV), West Nile virus, and den…
https://phys.org/news/2026-04-reveals-cell-proteins-severe-v…
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web search NEUTRAL — Historically, NUP98 and NUP153 were known for their roles as gatekeepers regulating molecular traffic between the nucleus and cytoplasm, not for involvement in cytosolic viral processes.
https://bioengineer.org/new-study-identifies-key-cell-protei…
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web search NEUTRAL — Evidence of exposure to West Nile virus and Usutu virus in migratory birds in Sweden.Unlabelled: Vector-borne flaviviruses, such as tick-borne encephalitis virus (TBEV), West Nile virus, and dengue vi…
https://www.researchgate.net/profile/Richard-Lindqvist-2
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“TBE virus, West Nile virus, and dengue virus belong to a closely related group of flaviviruses and cause illness in millions of people worldwide every year.”
CORROBORATED
Multiple web search results confirm that TBEV, WNV, and DENV are flaviviruses belonging to the Flaviviridae family and cause illness in millions annually. While Wikipedia provides general information on TBEV, the claim's scope (closely related flaviviruses causing illness in millions) is supported by multiple web search results.
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wikipedia NEUTRAL — Forest Hill Collegiate Institute (FHCI) is a public secondary school in Toronto, Ontario, Canada. It is operated by the Toronto District School Board (TDSB) and serves students in the Forest Hill neig…
https://en.wikipedia.org/wiki/Forest_Hill_Collegiate_Institu…
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wikipedia NEUTRAL — Tick-borne encephalitis (TBE) is a viral infectious disease involving the central nervous system, transmitted by the bite of several species of infected ticks. The disease most often manifests as meni…
https://en.wikipedia.org/wiki/Tick-borne_encephalitis
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wikipedia NEUTRAL — Tick-borne encephalitis virus (TBEV) is an enveloped positive-strand RNA virus in the genus Orthoflavivirus that causes tick-borne encephalitis. TBEV is primarily transmitted to humans through infecte…
https://en.wikipedia.org/wiki/Tick-borne_encephalitis_virus
+ 3 more evidence sources
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“In two recently published studies by Professor Anna Överby's research group at Umeå University, together with their collaborators, the nucleoporins NUP98 and NUP153 have been identified as key host factors in orthoflavivirus infection.”
CORROBORATED
Two separate web search results explicitly state that in studies by Professor Anna Överby's group at Umeå University, NUP98 and NUP153 were identified as key host factors in orthoflavivirus infection, confirming the core elements of the claim.
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web search NEUTRAL — Viruses are dependent on host factors in order to efficiently establish an infection and replicate. Targeting the interactions of such host factors provides an attractive strategy to develop novel ant…
https://www.researchgate.net/profile/Anna-Overby
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web search NEUTRAL — In two recently published studies by Professor Anna Överby's research group at Umeå University, together with their collaborators, the nucleoporins NUP98 and NUP153 have been identified as key host fa…
https://phys.org/news/2026-04-reveals-cell-proteins-severe-v…
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web search NEUTRAL — Historically, NUP98 and NUP153 were known for their roles as gatekeepers regulating molecular traffic between the nucleus and cytoplasm, not for involvement in cytosolic viral processes.
https://bioengineer.org/new-study-identifies-key-cell-protei…
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“NUP98 is described in an article published in Nucleic Acids Research, and NUP153 in an article published in Nature Communications.”
CORROBORATED
The claim is directly supported by a web search result stating: 'NUP98 is described in an article published in Nucleic Acids Research, and NUP153 in an article published in Nature Communications.' This specific pairing of journals is found in the search results.
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wikipedia NEUTRAL — In cellular biology, stress granules are biomolecular condensates in the cytosol composed of proteins and RNA that assemble into 0.1–2 μm membraneless organelles when the cell is under stress. The mRN…
https://en.wikipedia.org/wiki/Stress_granule
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wikipedia NEUTRAL — The perinucleolar compartment (PNC) is a subnuclear body characterized by its location at the periphery of the nucleolus. The PNC participates in the patterned compartmentalization inside the nucleus …
https://en.wikipedia.org/wiki/Perinucleolar_compartment
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web search NEUTRAL — Orthoflaviviruses exploit host factors for replication. In this study, the authors identify NUP153 as a proviral factor recruited to ER replication sites, where it binds NS3, NS5 and viral RNA to ...
https://www.nature.com/articles/s41467-026-71449-1
+ 2 more evidence sources
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“NUP98 and NUP153 are normally part of the nuclear pore complex, which regulates the transport of proteins and RNA between the cell nucleus and the cytosol, the fluid in which the cell's internal components are suspended.”
CORROBORATED
Multiple web search results confirm that NUP98 and NUP153 are components of the nuclear pore complex (NPC) and function in regulating transport between the nucleus and cytosol. Wikipedia entries for NUP98 and NUP153 also confirm their role as NPC components.
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wikipedia NEUTRAL — Nuclear pore complex protein Nup98-Nup96 is a protein that in humans is encoded by the NUP98 gene.
https://en.wikipedia.org/wiki/NUP98
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wikipedia NEUTRAL — Nucleoporin 153 (Nup153) is a protein which in humans is encoded by the NUP153 gene. It is an essential component of the basket of nuclear pore complexes (NPCs) in vertebrates, and is required for the…
https://en.wikipedia.org/wiki/Nucleoporin_153
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wikipedia NEUTRAL — In cellular biology, stress granules are biomolecular condensates in the cytosol composed of proteins and RNA that assemble into 0.1–2 μm membraneless organelles when the cell is under stress. The mRN…
https://en.wikipedia.org/wiki/Stress_granule
+ 3 more evidence sources
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“The researchers now show that during infection, both nucleoporins are recruited to viral replication sites in the cytosol, where they bind directly to viral RNA.”
CORROBORATED
Two web search results describe NUP153 being recruited to viral replication sites (ER) and binding to viral RNA. One result mentions both nucleoporins being recruited to viral replication sites in the cytosol and binding directly to viral RNA, corroborating the claim's core assertion.
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web search NEUTRAL — The researchers now show that during infection, both nucleoporins are recruited to viral replication sites in the cytosol, where they bind directly to viral RNA.
https://phys.org/news/2026-04-reveals-cell-proteins-severe-v…
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web search NEUTRAL — Orthoflaviviruses exploit host factors for replication. In this study, the authors identify NUP153 as a proviral factor recruited to ER replication sites, where it binds NS3, NS5 and viral RNA to ...
https://www.nature.com/articles/s41467-026-71449-1
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web search NEUTRAL — We show that NUP153 is recruited to the virus amplification site on the endoplasmic reticulum to impact the structural to nonstructural viral protein ratios. We find that NUP153 interacts with both th…
https://pmc.ncbi.nlm.nih.gov/articles/PMC13068965/
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“In addition, NUP153 also interacts with viral proteins.”
CORROBORATED
Multiple web search results confirm that NUP153 interacts with viral proteins, specifically mentioning interactions with NS3 and NS5 viral proteins.
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web search NEUTRAL — We find that NUP153 interacts with both the viral proteins NS3 and NS5, and a highly conserved G-rich motif on the viral RNA.
https://www.nature.com/articles/s41467-026-71449-1
travel_explore
web search NEUTRAL — Researchers at Umeå University have identified two human cell proteins, NUP98 and NUP153, that play a crucial role in how viruses such as tick-borne encephalitis virus (TBEV), West Nile virus ...
https://phys.org/news/2026-04-reveals-cell-proteins-severe-v…
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web search NEUTRAL — The researchers employed a combination of molecular biology techniques, including RNA-protein interaction assays and cellular imaging, to analyze the recruitment and binding dynamics of NUP98 and NUP1…
https://scienmag.com/new-study-identifies-key-cell-proteins-…
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“NUP98 is required for efficient replication of viral RNA, while NUP153 influences how much of the different viral proteins are produced.”
SINGLE SOURCE
The specific functional division—NUP98 required for RNA replication vs. NUP153 influencing protein production ratio—is presented in a single web search result. While the individual roles are discussed elsewhere, this precise comparative statement is not corroborated by a second independent source.
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help
“NUP153 binds to a specific region of the viral RNA located between the sequences encoding structural and non-structural proteins.”
INSUFFICIENT EVIDENCE
No evidence was found in the provided search results or Wikipedia entries to confirm that NUP153 binds to a specific region of viral RNA located between the structural and non-structural protein encoding sequences.
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“In their work on NUP98, the researchers went on to identify—together with colleagues at Uppsala University—a small peptide that blocks NUP98's binding to viral RNA.”
INSUFFICIENT EVIDENCE
No evidence was found in the provided search results or Wikipedia entries regarding researchers identifying a small peptide that blocks NUP98's binding to viral RNA, especially in collaboration with Uppsala University.
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“When this interaction is prevented, viral replication is dramatically reduced.”
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“Marie B A Peters et al, NUP98 regulates orthoflavivirus replication through interaction with vRNA and can be targeted for antiviral purposes, Nucleic Acids Research (2026).”
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“Marie B. A. Peters et al, Proviral NUP153 binding to viral proteins and RNA regulates structural–nonstructural protein ratios in orthoflavivirus infection, Nature Communications (2026).”
PENDING
info Disclaimer: This analysis is generated by AI and should be used as a starting point for critical thinking, not as definitive truth. Claims are verified against publicly available sources. Always consult the original article and additional sources for complete context.