Engineered ferritin for lanthanide binding

Calisti, Lorenzo; Trabuco, Matilde Cardoso; Boffi, Alberto; Testi, Claudia; Montemiglio, Linda Celeste; Georges, Amédée des; Benni, Irene; Ilari, Andrea; Taciak, Bartłomiej; Białasek, Maciej; Rygiel, Tomasz P.; Król, Magdalena; Baiocco, Paola; Bonamore, Alessandra

doi:10.1371/journal.pone.0201859

Cited by 24 publications

(21 citation statements)

References 62 publications

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“…The importance of the CD71/H-Ft interaction is dictated by the emerging physiological and pathological significance of the circulating ferritin and its scavenger receptor 20,21 . Moreover, nano-sized H-Ft homopolymers have moved to the center stage of nanomedicine research as theranostic agents 22 , due to their unique cargo capabilities for small therapeutic molecules or isotopic tracers coupled to selectivity towards CD71 23–25 . CD71 is highly expressed in the most common cancer cell types, further highlighting the interest for this receptor as a privileged target for the selective delivery of cytotoxic drugs coupled to Tf, ferritin, or monoclonal antibody drug conjugates 26–28 .…”

Section: Introductionmentioning

confidence: 99%

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

et al. 2019

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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.

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Section: Introductionmentioning

confidence: 99%

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

et al. 2019

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“…Ferritin proteins have been taking center stage in recent years as smart nanocarriers for drug delivery due to their hollow cage-like structures and their unique 24-meric assembly 4–9 . Human H ferritins are naturally targeted toward TfR1 (or CD71) receptor highly expressed in iron avid, fast replicating, tumor cells 10 .…”

Section: Introductionmentioning

confidence: 99%

Ferritin nanovehicle for targeted delivery of cytochrome C to cancer cells

Macone

Masciarelli²,

Palombarini

et al. 2019

Sci Rep

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In this work, we have exploited the unique properties of a chimeric archaeal-human ferritin to encapsulate, deliver and release cytochrome c and induce apoptosis in a myeloid leukemia cell line. The chimeric protein combines the versatility in 24-meric assembly and cargo incorporation capability of Archaeglobus fulgidus ferritin with specific binding of human H ferritin to CD71, the “heavy duty” carrier responsible for transferrin-iron uptake. Delivery of ferritin-encapsulated cytochrome C to the Acute Promyelocytic Leukemia (APL) NB4 cell line, highly resistant to transfection by conventional methods, was successfully achieved in vitro . The effective liberation of cytochrome C within the cytosolic environment, demonstrated by double fluorescent labelling, induced apoptosis in the cancer cells.

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“…An interesting application has been recently reported by A. Boffi and coworkers who fused a lanthanide binding tag (LBT) to the C-terminal end of mouse H-chain ferritin, HFt (Calisti et al 2018). Ferritin displays 24 symmetrically related recognition epitopes for the CD71 receptor (the receptor of Transferrin) instead of the two of classical antibodies or two of transferrin.…”

Section: Luminescent Lanthanide Binding Tagsmentioning

confidence: 99%

Rare earth elements (REE) in biology and medicine

Ascenzi

Bettinelli

Boffi

et al. 2020

Rend. Fis. Acc. Lincei

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This survey reports on topics that were presented at the workshop on "Challenges with Rare Earth Elements. The Periodic Table at work for new Science & Technology" hold at the Academia dei Lincei in November 2019. The herein reported materials refer to presentations dealing with studies and applications of rare earth elements (REE) in several areas of Biology and Medicine. All together they show the tremendous impact REE have in relevant fields of living systems and highlight, on one hand, the still existing knowledge gap for an in-depth understanding of their function in natural systems as well as the very important role they already have in providing innovative scientific and technological solutions in a number of biomedical areas and in fields related to the assessment of the origin of food and on their manufacturing processes. On the basis of the to-date achievements one expects that new initiatives will bring, in a not too far future, to a dramatic increase of our understanding of the REE involvement in living organisms as well as a ramp-up in the exploitation of the peculiar properties of REE for the design of novel applications in diagnostic procedures and in the setup of powerful medical devices. This scenario calls the governmental authorities for new responsibilities to guarantee a continuous availability of REE to industry and research labs together with providing support to activities devoted to their recovery/recycling.

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Engineered ferritin for lanthanide binding

Cited by 24 publications

References 62 publications

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

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

Ferritin nanovehicle for targeted delivery of cytochrome C to cancer cells

Rare earth elements (REE) in biology and medicine

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