Cryo-EM structure of the human ferritin–transferrin receptor 1 complex

Linda Celeste Montemiglio, Claudia Testi, Pierpaolo Ceci, Elisabetta Falvo, Martina Pitea, Carmelinda Savino, Alessandro Arcovito, Giovanna Peruzzi, Paola Baiocco, Filippo Mancia, Alberto Boffi, Amédée des Georges () and Beatrice Vallone ()
Additional contact information
Linda Celeste Montemiglio: Sapienza University of Rome
Claudia Testi: Sapienza University of Rome
Pierpaolo Ceci: National Research Council
Elisabetta Falvo: National Research Council
Martina Pitea: Sapienza University of Rome
Carmelinda Savino: National Research Council
Alessandro Arcovito: Università Cattolica del Sacro Cuore
Giovanna Peruzzi: Istituto Italiano di Tecnologia
Paola Baiocco: Istituto Italiano di Tecnologia
Filippo Mancia: Columbia University Medical Center
Alberto Boffi: Sapienza University of Rome
Amédée des Georges: Advanced Science Research Center at The Graduate Center of the City University of New York
Beatrice Vallone: Sapienza University of Rome

Nature Communications, 2019, vol. 10, issue 1, 1-8

Abstract: Abstract Human transferrin receptor 1 (CD71) guarantees iron supply by endocytosis upon binding of iron-loaded transferrin and ferritin. Arenaviruses and the malaria parasite exploit CD71 for cell invasion and epitopes on CD71 for interaction with transferrin and pathogenic hosts were identified. Here, we provide the molecular basis of the CD71 ectodomain-human ferritin interaction by determining the 3.9 Å resolution single-particle cryo-electron microscopy structure of their complex and by validating our structural findings in a cellular context. The contact surfaces between the heavy-chain ferritin and CD71 largely overlap with arenaviruses and Plasmodium vivax binding regions in the apical part of the receptor ectodomain. Our data account for transferrin-independent binding of ferritin to CD71 and suggest that select pathogens may have adapted to enter cells by mimicking the ferritin access gate.

Date: 2019
References: Add references at CitEc
Citations: View citations in EconPapers (2)

Downloads: (external link)
https://www.nature.com/articles/s41467-019-09098-w Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-09098-w

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-019-09098-w

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().