Bacterial lactoferrin-binding protein A binds to both domains of the human lactoferrin C-lobe

Microbiology ◽  
2003 ◽  
Vol 149 (7) ◽  
pp. 1729-1737 ◽  
Author(s):  
Henry Wong ◽  
Anthony B. Schryvers
Keyword(s):  
Binding Proteins ◽  
Binding Protein ◽  
Protein A ◽  
Human Lactoferrin ◽  
Chimeric Proteins ◽  
Iron Binding ◽  
Binding Studies ◽  
Binding Interaction ◽  
Binding Regions ◽  
Iron Binding Proteins

Pathogenic bacteria in the family Neisseriaceae express surface receptors to acquire iron from the mammalian iron-binding proteins. Transferrins and lactoferrins constitute a family of iron-binding proteins highly related in both sequence and structure, yet the bacterial receptors are able to distinguish between these proteins and uphold a strict binding specificity. In order to understand the molecular basis for this specificity, the interaction between human lactoferrin (hLf) and the lactoferrin-binding protein A (LbpA) from Moraxella catarrhalis was studied. A periplasmic expression system was designed for the heterologous expression of LbpA, which enabled the investigation of its binding activity in the absence of lactoferrin-binding protein B (LbpB). To facilitate delineation of the LbpA-binding regions of hLf, chimeric proteins composed of hLf and bovine transferrin were made. Binding studies performed with the chimeric proteins and recombinant LbpA identified two binding regions within the C-terminus of hLf. Furthermore, native LbpA from Moraxella and Neisseria spp. bound the identical spectrum of hybrid proteins as the recombinant receptor, demonstrating a conserved binding interaction with the C-lobe of hLf.

scholarly journals Crystal Structure ofPasteurella haemolyticaFerric Ion-binding Protein A Reveals a Novel Class of Bacterial Iron-binding Proteins

2003 ◽  
Vol 278 (42) ◽  
pp. 41093-41098 ◽  
Author(s):  
Stephen R. Shouldice ◽  
Douglas R. Dougan ◽  
Pamela A. Williams ◽  
Robert J. Skene ◽  
Gyorgy Snell ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Binding Proteins ◽  
Binding Protein ◽  
Protein A ◽  
Ion Binding ◽  
Iron Binding ◽  
Iron Binding Proteins

scholarly journals Purification and properties of a 23 kDa Ca2+-binding protein from Drosophila melanogaster

1990 ◽  
Vol 271 (3) ◽  
pp. 661-666 ◽  
Author(s):  
L E Kelly
Keyword(s):  
Binding Proteins ◽  
Binding Protein ◽  
Protein A ◽  
Mammalian Brain ◽  
Binding Studies ◽  
Mobility Shift ◽  
Western Blots ◽  
Heat Stable ◽  
Drosophila Protein ◽  
Sheep Brain

Recent reports have shown that there exists in mammalian brain a number of heat-stable Ca2(+)-binding proteins that are distinct from calmodulin [McDonald & Walsh (1985) Biochem. J. 232, 559-567]. We have attempted to characterize equivalent Ca2(+)-binding proteins from Drosophila. Affigel-phenothiazine chromatography, which can be used to purify calmodulin and other Ca2(+)-binding proteins, allowed the identification of a possible heat-stable 23 kDa Ca2(+)-binding protein. A purification procedure for this protein has been devised. Purified 23 kDa protein shows characteristics typical of a Ca2(+)-binding protein; there is a mobility shift on SDS/polyacrylamide gels in the presence of EGTA, and Western blotting, followed by the use of the 45Ca2+ overlay technique, confirms that the 23 kDa protein does bind Ca2+. 45Ca2+ binding studies indicate that this protein binds 1 mol of Ca2+/mol of protein, with Kd 1.9 microM. A single band with pI 5.2 is obtained on isoelectric focusing. Analysis of Western blots of Drosophila tissues probed with antibodies to the Ca2(+)-binding protein indicates that it has a widespread distribution, but is absent from muscle tissue. The antibodies also cross-react with a protein of identical molecular mass in extracts of sheep brain. The possible similarity between this Drosophila Ca2(+)-binding protein and mammalian proteins is discussed, and comparison is made between this Drosophila protein and other Ca2(+)-binding proteins purified from vertebrates.

scholarly journals Structural Basis for Iron Binding and Release by a Novel Class of Periplasmic Iron-Binding Proteins Found in Gram-Negative Pathogens

2004 ◽  
Vol 186 (12) ◽  
pp. 3903-3910 ◽  
Author(s):  
Stephen R. Shouldice ◽  
Robert J. Skene ◽  
Douglas R. Dougan ◽  
Gyorgy Snell ◽  
Duncan E. McRee ◽  
...  
Keyword(s):  
Molecular Mechanisms ◽  
Binding Protein ◽  
Iron Acquisition ◽  
Protein A ◽  
Structural Basis ◽  
Mammalian Host ◽  
Iron Binding ◽  
Gram Negative ◽  
Shipping Fever ◽  
Iron Binding Proteins

ABSTRACT We have determined the 1.35- and 1.45-Å structures, respectively, of closed and open iron-loaded forms of Mannheimia haemolytica ferric ion-binding protein A. M. haemolytica is the causative agent in the economically important and fatal disease of cattle termed shipping fever. The periplasmic iron-binding protein of this gram-negative bacterium, which has homologous counterparts in many other pathogenic species, performs a key role in iron acquisition from mammalian host serum iron transport proteins and is essential for the survival of the pathogen within the host. The ferric (Fe3+) ion in the closed structure is bound by a novel asymmetric constellation of four ligands, including a synergistic carbonate anion. The open structure is ligated by three tyrosyl residues and a dynamically disordered solvent-exposed anion. Our results clearly implicate the synergistic anion as the primary mediator of global protein conformation and provide detailed insights into the molecular mechanisms of iron binding and release in the periplasm.

Influence of tobacco smoke on zinc, cadmium, iron, iron-binding proteins, and low-weight anti-oxidant status in pregnancy

2018 ◽  
Vol 30 (13-14) ◽  
pp. 534-541
Author(s):  
Halina Milnerowicz ◽  
Marta Wrześniak ◽  
Małgorzata Królik ◽  
Katarzyna Kowalska
Keyword(s):  
Tobacco Smoke ◽  
Binding Proteins ◽  
Iron Binding ◽  
Low Weight ◽  
Zinc Cadmium ◽  
Anti Oxidant ◽  
Iron Iron ◽  
Iron Binding Proteins ◽  
Oxidant Status ◽  
In Pregnancy
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