{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Sun Y"],"funding":["National Natural Science Foundation of China"],"pagination":["698-713"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9037478"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13(1)"],"pubmed_abstract":["Extraintestinal pathogenic <i>Escherichia coli</i> (ExPEC) is a common anthropozoonotic pathogen that causes systemic infections. To establish infection, ExPEC must utilize essential nutrients including iron from the host. Transferrin is an important iron source for multiple bacteria. However, the mechanism by which ExPEC utilizes transferrin remains unclear. In this study, we found that iron-saturated holo-transferrin rather than iron-free apo-transferrin promoted the vitality of ExPEC in heat-inactivated human serum. The multifunctional protein Elongation factor Tu (EFTu) worked as a holo-transferrin binding protein. EFTu not only bound holo-transferrin rather than apo-transferrin but also released transferrin-related iron, with all domains of EFTu involved in holo-transferrin binding an"],"journal":["Virulence"],"pubmed_title":["Extraintestinal pathogenic <i>Escherichia coli</i> utilizes the surface-expressed elongation factor Tu to bind and acquire iron from holo-transferrin."],"pmcid":["PMC9037478"],"funding_grant_id":["31872479"],"pubmed_authors":["Xue F","Li J","Wang X","Sun Y","Tang F","Dai J"],"additional_accession":[]},"is_claimable":false,"name":"Extraintestinal pathogenic <i>Escherichia coli</i> utilizes the surface-expressed elongation factor Tu to bind and acquire iron from holo-transferrin.","description":"Extraintestinal pathogenic <i>Escherichia coli</i> (ExPEC) is a common anthropozoonotic pathogen that causes systemic infections. To establish infection, ExPEC must utilize essential nutrients including iron from the host. Transferrin is an important iron source for multiple bacteria. However, the mechanism by which ExPEC utilizes transferrin remains unclear. In this study, we found that iron-saturated holo-transferrin rather than iron-free apo-transferrin promoted the vitality of ExPEC in heat-inactivated human serum. The multifunctional protein Elongation factor Tu (EFTu) worked as a holo-transferrin binding protein. EFTu not only bound holo-transferrin rather than apo-transferrin but also released transferrin-related iron, with all domains of EFTu involved in holo-transferrin binding an","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Dec","modification":"2026-05-31T18:50:23.084Z","creation":"2025-04-05T22:21:01.168Z"},"accession":"S-EPMC9037478","cross_references":{"pubmed":["35443872"],"doi":["10.1080/21505594.2022.2066274"]}}