ArticleJournal of bacteriology1995
Topological analysis of the Escherichia coli ferrichrome-iron receptor by using monoclonal antibodies.
Article in Journal of bacteriology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 22 citations in OpenAlex.
- TonB induces conformational changes in surface-exposed loops of FhuA, outer membrane receptor of Escherichia coli.Protein science : a publication of the Protein Society · 2008Article
- Genes under positive selection in Escherichia coli.Genome research · 2007Article
- Surface polysaccharides and iron-uptake systems of Actinobacillus pleuropneumoniae.Canadian journal of veterinary research = Revue canadienne de recherche veterinaire · 2004Review
- Determination of surface-exposed, functional domains of gonococcal transferrin-binding protein A.Infection and immunity · 2004Article
- Bacterial phage receptors, versatile tools for display of polypeptides on the cell surface.Journal of bacteriology · 2001Article
- Characterization of in vitro interactions between a truncated TonB protein from Escherichia coli and the outer membrane receptors FhuA and FepA.Journal of bacteriology · 2001Article
- Prediction by a neural network of outer membrane beta-strand protein topology.Protein science : a publication of the Protein Society · 1998Article
- Identification of a new site for ferrichrome transport by comparison of the FhuA proteins of Escherichia coli, Salmonella paratyphi B, Salmonella typhimurium, and Pantoea agglomerans.Journal of bacteriology · 1998Article
- An internal affinity-tag for purification and crystallization of the siderophore receptor FhuA, integral outer membrane protein from Escherichia coli K-12.Protein science : a publication of the Protein Society · 1998Article
- Specific in vivo labeling of cell surface-exposed protein loops: reactive cysteines in the predicted gating loop mark a ferrichrome binding site and a ligand-induced conformational change of the Escherichia coli FhuA protein.Journal of bacteriology · 1998Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ferrichrome-iron transport in Escherichia coli is initiated by the outer membrane receptor FhuA. Thirty-five anti-FhuA monoclonal antibodies (MAbs) were isolated to examine the surface accessibility of FhuA sequences and their contribution to ligand binding. The determinants of 32 of the MAbs were mapped to eight distinct regions in the primary sequence of FhuA by immunoblotting against (i) five internal deletion FhuA proteins and (ii) four FhuA peptides generated by cyanogen bromide cleavage. Two groups of MAbs bound to FhuA in outer membrane vesicles but not to intact cells, indicating that their determinants, located between residues 1 and 20 and 21 and 59, are exposed to the periplasm. One of the 28 strongly immunoblot-reactive MAbs bound to FhuA on intact cells in flow cytometry, indicating that its determinant, located between amino acids 321 and 381, is cell surface exposed. This MAb and four others which in flow cytometry bound to cells expressing FhuA were tested for the ability to block ligand binding. While no MAb inhibited growth promotion by ferrichrome or cell killing by microcin 25, some prevented killing by colicin M and were partially able to inhibit the inactivation of T5 phage. These data provide evidence for spatially distinct ligand binding sites on FhuA. The lack of surface reactivity of most of the immunoblot-reactive MAbs suggests that the majority of FhuA sequences which lie external to the outer membrane may adopt a tightly ordered organization with little accessible linear sequence.
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