Cloning and expression of the <i>Haemophilus influenzae</i> transferrin receptor genes

Loosmore, Sheena M.; Yang, Yanping; Coleman, Debbie C.; Shortreed, Jean M.; England, Diane M.; Harkness, Robin E.; Chong, Pele; Klein, Michel

doi:10.1046/j.1365-2958.1996.406943.x

Cited by 48 publications

(49 citation statements)

References 28 publications

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“…One vaccine strategy that has been adopted in several other bacterial species in the Pasteurellaceae is to target the surface proteins involved in acquisition of iron in the host as vaccine antigens (20,26,30). The rationale for targeting these antigens is that they are essential for overcoming the iron restriction imposed by the host iron binding protein transferrin (Tf) and are accessible at the cell surface.…”

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confidence: 99%

“…This protein ranges in size from 60 to 90 kDa in different strains and species (15). Experimental studies support the use of TbpBs as a vaccine antigen (20,26,30). TbpA is an integral, TonB-dependent OMP proposed to mediate transport of iron across the outer membrane (32).…”

mentioning

confidence: 99%

“…TbpAs are approximately 100 kDa, significantly larger than the related siderophore receptor proteins that have been more extensively characterized (5,12,19). Although TbpA is absolutely essential for the iron acquisition process (14), there is currently limited evidence to sup-port the use of the intact protein as a vaccine candidate (20,26).…”

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confidence: 99%

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Characterization of a Novel Transferrin Receptor in Bovine Strains of Pasteurella multocida

Ogunnariwo

Schryvers

2001

J Bacteriol

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Analysis of bovine respiratory isolates of Pasteurella multocida demonstrated that six of nine strains tested were capable of growth dependent upon bovine transferrin and of specifically binding ruminant transferrins. A single 82-kDa protein was affinity isolated from the P. multocida strains with immobilized bovine transferrin.In contrast to what has been observed in other species, binding of this protein to immobilized transferrin was specifically blocked by the N-lobe subfragment of bovine transferrin. A single gene encoding the 82-kDa protein was flanked by a leucyl-tRNA synthetase gene and an IS1060 element, in contrast to other species where genes encoding the two receptor proteins (TbpB and TbpA) are found in an operonic arrangement. A similar gene arrangement was observed in all of the receptor-positive strains, in spite of the observation that they belonged to different genomic groups. Analysis of the deduced amino acid sequence of the receptor protein indicated that it is a member of the TonB-dependent outer membrane receptor family, and although it is related to transferrin and lactoferrin receptor proteins (TbpAs and LbpAs) from other species, it differs substantially from other members of this group. Amino acid alignments suggest that the reduced size (20 kDa smaller) of the P. multocida TbpA is primarily due to the absence of larger predicted external loops. Collectively these results suggest that P. multocida has a single, novel receptor protein (TbpA) that is capable of efficiently mediating iron acquisition from bovine transferrin without the involvement of a second receptor protein (TbpB).

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Characterization of a Novel Transferrin Receptor in Bovine Strains of Pasteurella multocida

Ogunnariwo

Schryvers

2001

J Bacteriol

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“…Antiserum raised to purified recombinant Tbp2 has shown protection against bacteremia in a infant-rat model after challenge with an H. influenzae type b strain expressing a homologous Tbp2 protein in its outer membrane. In a similar experiment, antiserum raised to recombinant Tbp1 was not protective (118).…”

Section: Outer Membrane Proteinsmentioning

confidence: 87%

“…At present, two Tbps have been identified, the ironrepressible Tbp1 with a molecular mass of approximately 100 kDa and the more variable Tbp2 with an approximate molecular mass of 85 kDa (176). Cloning and sequencing of several isolates showed Tbp1 to be highly conserved among H. influenzae type b and NTHi strains (118). Initially, it was thought that these proteins were essential for H. influenzae type b to survive as an invasive pathogen because soluble-iron chelators (siderophores) were not found in invasive H. influenzae type b strains (177).…”

Section: Outer Membrane Proteinsmentioning

confidence: 99%

Lower Respiratory Tract Infections

Carroll

Adams

2016

Microbiol Spectr

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This review will focus on the infectious etiologies and more common noninfectious causes of lower respiratory tract syndromes among major immunosuppressed populations. The changing epidemiology of infections in the era of highly active antiretroviral therapy (HAART) in the case of HIV-positive patients and the impacts of both newer immune-suppressant therapies and anti-infective prophylaxis for other immunocompromised hosts will be discussed, with emphasis on diagnostic approaches and practice algorithms.

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Iron Proteins for Storage & Transport & Their Synthetic Analogs

Lewin

Brun

Moore

2005

Encyclopedia of Inorganic Chemistry

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This article reviews proteins involved in iron metabolism. Brief descriptions are given of the biological contexts for the proteins discussed but the main emphasis is on chemical and structural aspects of them. Iron is essential to almost all forms of life, but its low bioavailability and toxicity mean that they require sophisticated mechanisms to transport it. Mammals acquire heme and nonheme iron via proteins in the gut wall, and transport it around the body using serum transferrin, for ferric iron, and hemopexin, for heme. Microbes have an active iron uptake mechanism involving small iron chelators called siderophores, for example, ferrichrome in Escherichia coli . Ferrichrome enters the cell via FhuA, a β‐barrel in the outer membrane. The periplasmic protein FhuD then transfers it to the FhuBC complex in the cytoplasmic membrane. FhuB forms a channel through which the ferric siderophore passes using energy supplied by FhuC. Once inside the cytoplasm the iron is removed from the ligand, possibly via reduction by FhuF. Some pathogenic bacteria have a similar system for heme uptake, secreting hemophores such as HasA, which can remove heme from hemoglobin. Other pathogens have outer membrane receptors that remove ferric iron from transferrin and transport it into the periplasm, where it is bound by ferric binding proteins that closely resemble a single lobe of transferrin. Following its acquisition, iron needs to be stored safely. The most widespread form of iron storage is the ferritin superfamily, which includes ferritin, bacterioferritin, and Dps. Ferritin is found in bacteria, plants, and animals and is a large shell made up of 24 subunits within which up to 4,500 ferric ions can be stored as a ferrihydrite mineral core. Bacterioferritin is found in bacteria and is closely related to ferritin, but contains up to 12 heme groups bound between pairs of subunits, which may play a role in iron release or electron storage. The bacterial protein Dps is smaller than ferritin, with 12 subunits forming the protein shell, and can hold up to 500 ferric ions. All of these proteins contain dinuclear iron sites that catalyze the oxidation of ferrous iron. An alternative form of iron storage is frataxin, found in mitochondria. Although not related to ferritin, this protein has the ability to form large aggregates that can store up to 50 ferric ions per monomer in a mineral core resembling those of ferritins.

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Cloning and expression of the Haemophilus influenzae transferrin receptor genes

Cited by 48 publications

References 28 publications

Characterization of a Novel Transferrin Receptor in Bovine Strains of Pasteurella multocida

Characterization of a Novel Transferrin Receptor in Bovine Strains of Pasteurella multocida

Lower Respiratory Tract Infections

Iron Proteins for Storage & Transport & Their Synthetic Analogs

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