ArticlePLoS pathogens2021
Human parvovirus B19 interacts with globoside under acidic conditions as an essential step in endocytic trafficking.
Article in PLoS pathogens, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 25 citations in OpenAlex.
- Article
- Parvovirus B19 infection as a trigger of acute cholestasis in heterozygous genetic BSEP deficiency: a case report and review of the literature of acute parvovirus B19-related hepatitis.Internal and emergency medicine · 2026Review
- Transferrin receptor 1 binds human parvovirus B19 VP1u to facilitate entry.Nature communications · 2026Article
- Cellular determinants of parvovirus B19 susceptibility in the human placenta.PLoS pathogens · 2026Article
- Parvovirus B19 in Rheumatic Diseases.Microorganisms · 2024Review
- Globoside Is an Essential Intracellular Factor Required for Parvovirus B19 Endosomal Escape.Cells · 2024Article
- Distinct clinical features of transplanted children with Parvovirus B19 infection.Virology journal · 2024Article
- NS1-mediated enhancement of MVC transcription and replication promoted by KAT5/H4K12ac.Journal of virology · 2024Article
- On-column refolding and off-column assembly of parvovirus B19 virus-like particles from bacteria-expressed protein.Applied microbiology and biotechnology · 2024Article
- Feasibility of Domain Segmentation of B19V VP1u Using Intein Technology for Structural Studies.Protein and peptide letters · 2024Article
- Structural Shifts of the Parvovirus B19 Capsid Receptor-binding Domain: A Peptide Study.Protein and peptide letters · 2024Article
- For better or worse: crosstalk of parvovirus and host DNA damage response.Frontiers in immunology · 2024Review
- Non-Permissive Parvovirus B19 Infection: A Reservoir and Questionable Safety Concern in Mesenchymal Stem Cells.International journal of molecular sciences · 2023Article
- Globoside and the mucosal pH mediate parvovirus B19 entry through the epithelial barrier.PLoS pathogens · 2023Article
- Identification of AXL as a co-receptor for human parvovirus B19 infection of human erythroid progenitors.Science advances · 2023Article
- Nuclear entry and egress of parvoviruses.Molecular microbiology · 2022Review
- Structural Dynamics and Activity of B19V VP1u during the pHs of Cell Entry and Endosomal Trafficking.Viruses · 2022Article
- Prevalence, Cell Tropism, and Clinical Impact of Human Parvovirus Persistence in Adenomatous, Cancerous, Inflamed, and Healthy Intestinal Mucosa.Frontiers in microbiology · 2022Article
- Microbial lectome versus host glycolipidome: How pathogens exploit glycosphingolipids to invade, dupe or kill.Frontiers in microbiology · 2022Review
- Multiplicity of Glycosphingolipid-Enriched Microdomain-Driven Immune Signaling.International journal of molecular sciences · 2021Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The glycosphingolipid (GSL) globoside (Gb4) is essential for parvovirus B19 (B19V) infection. Historically considered the cellular receptor of B19V, the role of Gb4 and its interaction with B19V are controversial. In this study, we applied artificial viral particles, genetically modified cells, and specific competitors to address the interplay between the virus and the GSL. Our findings demonstrate that Gb4 is not involved in the binding or internalization process of the virus into permissive erythroid cells, a function that corresponds to the VP1u cognate receptor. However, Gb4 is essential at a post-internalization step before the delivery of the single-stranded viral DNA into the nucleus. In susceptible erythroid Gb4 knockout cells, incoming viruses were arrested in the endosomal compartment, showing no cytoplasmic spreading of capsids as observed in Gb4-expressing cells. Hemagglutination and binding assays revealed that pH acts as a switch to modulate the affinity between the virus and the GSL. Capsids interact with Gb4 exclusively under acidic conditions and dissociate at neutral pH. Inducing a specific Gb4-mediated attachment to permissive erythroid cells by acidification of the extracellular environment led to a non-infectious uptake of the virus, indicating that low pH-mediated binding to the GSL initiates active membrane processes resulting in vesicle formation. In summary, this study provides mechanistic insight into the interaction of B19V with Gb4. The strict pH-dependent binding to the ubiquitously expressed GSL prevents the redirection of the virus to nonpermissive tissues while promoting the interaction in acidic intracellular compartments as an essential step in infectious endocytic trafficking.
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