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Updated: Jun 13, 2026
08:40
Production of Pseudotyped Particles to Study Highly Pathogenic Coronaviruses in a Biosafety Level 2 Setting
Published on: March 1, 2019
Transferrin receptor 1 binds human parvovirus B19 VP1u to facilitate entry
Hyunwook Lee1, Jan Bieri2, Nicolas Ammann2,3
1The Hormel Institute, University of Minnesota, Austin, MN, USA.
Nature Communications
|June 11, 2026
Summary
Human parvovirus B19 uses transferrin receptor 1 (TfR1) to enter erythroid progenitor cells. This discovery identifies the virus
Area of Science:
- Virology
- Cell Biology
- Structural Biology
Background:
- Human parvovirus B19 (B19V) specifically infects erythroid progenitor cells.
- The VP1 unique domain (VP1u) of B19V mediates cell entry via an unknown receptor (VP1uR).
Purpose of the Study:
- Identify the cellular receptor (VP1uR) for B19V uptake.
- Characterize the interaction between B19V VP1u and its receptor.
Main Methods:
- Proximity labeling in erythroid cells.
- Co-localization studies.
- Antibody blocking assays.
- Direct binding assays.
- Cryo-electron microscopy (cryo-EM) structure determination.
Main Results:
- Transferrin receptor 1 (TfR1/CD71) was identified as a key protein interacting with B19V VP1u.
- VP1u and TfR1 co-localize on the erythroid cell surface.
- Anti-TfR1 antibody OKT9 inhibited B19V uptake and infection but not initial binding.
- Cryo-EM revealed the structure of the TfR1-VP1u complex, pinpointing the binding site.
Conclusions:
- Transferrin receptor 1 (TfR1) is the previously unknown receptor (VP1uR) for human parvovirus B19.
- TfR1 mediates the uptake of B19V into erythroid progenitor cells.
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