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

Alessandro Arcovito, Linda Celeste Montemiglio, Claudia Testi, Pierpaolo Ceci, Elisabetta Falvo, Martina Pitea, Carmelinda Savino, Giovanna Peruzzi, Paola Baiocco, Filippo Mancia, Alberto Boffi, Amédée Des Georges, Beatrice Vallone

Risultato della ricerca: Contributo in rivistaArticolo in rivista

42 Citazioni (Scopus)


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.
Lingua originaleEnglish
pagine (da-a)1121-1128
Numero di pagine8
RivistaNature Communications
Stato di pubblicazionePubblicato - 2019


  • Biochemistry, Genetics and Molecular Biology (all)
  • Chemistry (all)
  • Physics and Astronomy (all)


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