Transferrin-Binding Protein B of Neisseria meningitidis : Sequence-Based Identification of the Transferrin-Binding Site Confirmed by Site-Directed Mutagenesis [PDF]
Journal of Bacteriology, 2004 ABSTRACT A sequence-based prediction method was employed to identify three ligand-binding domains in transferrin-binding protein B (TbpB) of Neisseria meningitidis strain B16B6. Site-directed mutagenesis of residues located in these domains has led to the identification of two domains, amino acids 53 to 57
Renauld-Mongenie, G. +9 more
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Biomedicines, 2022 Background: Obesity is characterized by adipose tissue dysregulation and predisposes individuals to insulin resistance and type 2 diabetes. At the molecular level, adipocyte dysfunction has been linked to obesity-triggered oxidative stress and protein ...
M. Carmen Navarro-Ruiz +12 more
doaj +1 more source
Identification of human transferrin-binding sites within meningococcal transferrin-binding protein B [PDF]
Journal of Bacteriology, 1997 Transferrin-binding protein B (TbpB) from Neisseria meningitidis binds human transferrin (hTf) at the surface of the bacterial cell as part of the iron uptake process. To identify hTf binding sites within the meningococcal TbpB, defined regions of the molecule were produced in Escherichia coli by a translational fusion expression system and the ability
G, Renauld-Mongénie +6 more
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Comparative evaluation of darbepoetin therapy in non-regenerative anaemia associated with Babesia gibsoni infection in dogs [PDF]
Journal of Veterinary and Animal Sciences, 2022 The present study describes a comparative evaluation of haemato-therapeutic response to darbepoetin therapy in non-regenerative anaemia associated with Babesia gibsoni infection in dogs.
J. Parvathy +5 more
doaj +1 more source
Lactoferrin binding protein B - a bi-functional bacterial receptor protein. [PDF]
PLoS Pathogens, 2017 Lactoferrin binding protein B (LbpB) is a bi-lobed outer membrane-bound lipoprotein that comprises part of the lactoferrin (Lf) receptor complex in Neisseria meningitidis and other Gram-negative pathogens. Recent studies have demonstrated that LbpB plays
Nicholas K H Ostan +11 more
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Protein regulation strategies of the mouse spleen in response to Babesia microti infection
Parasites & Vectors, 2021 Background Babesia is a protozoan parasite that infects red blood cells in some vertebrates. Some species of Babesia can induce zoonoses and cause considerable harm.
Xiaomin Xue +10 more
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Frontiers in Microbiology, 2021 Moraxella catarrhalis is a Gram-negative bacterium that is responsible for a substantial proportion of upper respiratory infections in children and lower respiratory infections in the elderly.
Clement Chan +2 more
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Evidence for in vivo expression of transferrin-binding proteins in Haemophilus influenzae type b [PDF]
Infection and Immunity, 1992 Haemophilus influenzae type b acquires transferrin-bound iron via a siderophore-independent mechanism involving direct contact between the human iron-binding glycoprotein and the bacterial cell surface. Evidence has accumulated to show that the transferrin receptor consists of at least two iron-regulated outer membrane transferrin-binding proteins ...
J, Holland +3 more
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Identification of sequences in human transferrin that bind to the bacterial receptor protein, transferrin‐binding protein B [PDF]
Molecular Microbiology, 1999 Alignment of amino‐acid sequences from the N‐terminal and C‐terminal halves of transferrin‐binding protein B revealed an underlying bilobed nature with several regions of identity. Based on this analysis, purified recombinant fusion proteins of maltose‐binding protein (Mbp) with intact TbpB, its N‐terminal half or C‐terminal half from the human ...
M D, Retzer, R H, Yu, A B, Schryvers
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Biochemical, Biophysical, and Cellular Investigations of the Interactions of Transferrin Receptor with Transferrin and the Hereditary Hemochromatosis Protein, HFE [PDF]
, 2004 Hereditary hemochromatosis (HH) is a prevalent genetic disorder that results in the daily excess absorption of dietary iron. If untreated this disease leads to systemic organ failure and death. HH is caused by mutations to the gene coding for a protein
Giannetti, Anthony Michael
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