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TitleTransferrin receptor 1 binds human parvovirus B19 VP1u to facilitate entry.
Journal, issue, pagesNat Commun, Year 2026
Publish dateJun 11, 2026
AuthorsHyunwook Lee / Jan Bieri / Nicolas Ammann / Corinne Suter / Daniela Hunziker / Ajit K Singh / Carol M Bator / Susan L Hafenstein / Carlos Ros /
PubMed AbstractHuman parvovirus B19 (B19V) displays a strict tropism for erythroid progenitor cells, which is governed by the VP1 unique domain (VP1u). This domain mediates cell-specific uptake through interaction ...Human parvovirus B19 (B19V) displays a strict tropism for erythroid progenitor cells, which is governed by the VP1 unique domain (VP1u). This domain mediates cell-specific uptake through interaction with an unknown cellular receptor, termed VP1uR. Proximity labeling in permissive erythroid cells identifies transferrin receptor 1 (TfR1/CD71) as a predominant membrane protein associated with VP1u. VP1u constructs colocalize with TfR1 at the cell surface of erythroid cells. Incubation with anti-TfR1 antibody OKT9 abolishes binding and uptake of recombinant VP1u. While OKT9 efficiently inhibits B19V uptake and infection, it does not block virus binding to host cells. Direct binding assays confirm interaction of VP1u with human TfR1. Using cryo-EM we solved the 2.4 Å structure of the TfR1-VP1u complex, mapping the binding site. These findings establish TfR1 as the previously unknown receptor, VP1uR, required for B19V uptake.
External linksNat Commun / PubMed:42277060
MethodsEM (single particle)
Resolution2.4 Å
Structure data

75944

11qc

EMDB-75944, PDB-11qc:
Human transferrin receptor ectodomain
Method: EM (single particle) / Resolution: 2.4 Å

75980

11rn

EMDB-75980, PDB-11rn:
Complex of B19V VP1u RBD and human transferrin receptor ectodomain
Method: EM (single particle) / Resolution: 2.4 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • homo sapiens (human)
  • human parvovirus b19
KeywordsMEMBRANE PROTEIN / TfR / B19V / VP1u / RBD

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