ArticleJournal of virology2009
Molecular chaperone BiP interacts with Borna disease virus glycoprotein at the cell surface.
Article in Journal of virology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
What it found
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Who cites it
38 citing papers in PubMed.
- GRP78 promotes rabies virus entry through interacting with viral receptors.Journal of virology · 2026Article
- Heat shock proteins at the crossroads of endosomal trafficking pathways.Cell biology and toxicology · 2025Review
- Hepatitis E Virus: What More Do We Need to Know?Medicina (Kaunas, Lithuania) · 2024Review
- GRP78 recognizes EV-F 3D protein and activates NF-κB to repress virus replication by interacting with CHUK/IKBKB.Journal of virology · 2024Article
- Endoplasmic reticulum stress triggers unfolded protein response as an antiviral strategy of teleost erythrocytes.Frontiers in immunology · 2024Article
- HSPA5 Promotes Attachment and Internalization of Porcine Epidemic Diarrhea Virus through Interaction with the Spike Protein and the Endo-/Lysosomal Pathway.Journal of virology · 2023Article
- New progresses on cell surface protein HSPA5/BiP/GRP78 in cancers and COVID-19.Frontiers in immunology · 2023Review
- Mycoplasma hyopneumoniae membrane protein Mhp271 interacts with host UPR protein GRP78 to facilitate infection.Molecular microbiology · 2022Article
- Vulnerability of The Male Reproductive System to SARS-CoV-2 Invasion: Potential Role for The Endoplasmic Reticulum Chaperone Grp78/HSPA5/BiP.Cell journal · 2022Article
- Potential to Eradicate Cancer Stemness by Targeting Cell Surface GRP78.Biomolecules · 2022Review
- Cellular stress modulates severity of the inflammatory response in lungsFrontiers in immunology · 2022Article
- The interaction of heat shock proteins with cellular membranes: a historical perspective.Cell stress & chaperones · 2021Review
- Human heat shock cognate protein (HSC70/HSPA8) interacts with negatively charged phospholipids by a different mechanism than other HSP70s and brings HSP90 into membranes.Cell stress & chaperones · 2021Article
- Is There any Alternative Receptor for SARS-CoV-2?Cell journal · 2021Article
- In silico identification of available drugs targeting cell surface BiP to disrupt SARS-CoV-2 binding and replication: Drug repurposing approach.European journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences · 2021Article
- Review
- Optimal Expression of the Envelope Glycoprotein of Orthobornaviruses Determines the Production of Mature Virus Particles.Journal of virology · 2021Article
- Interaction of HSPA5 (Grp78, BIP) with negatively charged phospholipid membranes via oligomerization involving the N-terminal end domain.Cell stress & chaperones · 2020Article
- GRP78 targeting: Hitting two birds with a stone.Life sciences · 2020Review
- The Role of Molecular Chaperones in Virus Infection and Implications for Understanding and Treating COVID-19.Journal of clinical medicine · 2020Review
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Borna disease virus (BDV) is characterized by highly neurotropic infection. BDV enters its target cells using virus surface glycoprotein (G), but the cellular molecules mediating this process remain to be elucidated. We demonstrate here that the N-terminal product of G, GP1, interacts with the 78-kDa chaperone protein BiP. BiP was found at the surface of BDV-permissive cells, and anti-BiP antibody reduced BDV infection as well as GP1 binding to the cell surface. We also reveal that BiP localizes at the synapse of neurons. These results indicate that BiP may participate in the cell surface association of BDV.
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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.