Neisseria meningitidis transferrin-binding protein 1 expressed in Escherichia coli is surface exposed and binds human transferrin

Palmer, Helen

doi:10.1016/0378-1097(93)90456-c

Cited by 7 publications

(9 citation statements)

References 17 publications

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“…Transferrin receptors from different bacteria have been demonstrated to be surface-exposed (Holland et al, 1992;Ala'Aldeen et al, 1993;Pintor et al, 1993) and since H. influenzae do not elaborate siderophores, the TfR plays an important role in acquiring nutrient iron. Both the Tbp1 and Tbp2 polypeptide chains have been shown to bind transferrin (Schryvers, 1989;Cornelissen et al, 1992;Ferron et al, 1993;Palmer et al, 1993). However, nothing was known about the sequence or antigenic conservation of H. influenzae transferrin receptor proteins.…”

Section: Discussionmentioning

confidence: 99%

Cloning and expression of the Haemophilus influenzae transferrin receptor genes

Loosmore¹,

Yang²,

Coleman³

et al. 1996

Molecular Microbiology

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The genomic transferrin receptor genes (tbpA and tbpB) from two strains of Haemophilus influenzae type b (Hib) and two strains of non-typable H. influenzae (NTHi) have been cloned and sequenced. The deduced protein sequences of the H. influenzae tbpA genes were 95-100% conserved and those of the tbpB genes were 66-100% conserved. The tbpB gene from one strain of NTHi was found to encode a truncated Tbp2 protein. The tbpB genes from four additional NTHi strains were amplified by the polymerase chain reaction (PCR) utilizing primers derived from the conserved N-terminal sequences of Tbp1 and Tbp2 and were found to encode full-length proteins. Although several bacterial species express transferrin receptors, when the Tbp1 and Tbp2 sequences from different organisms were compared, there was only limited homology. Recombinant Tbp1 and Tbp2 proteins were expressed from Escherichia coli and antisera were raised to the purified proteins. There was significant antigenic conservation of both Tbp1 and Tbp2 amongst H. influenzae strains, as determined by Western blot analysis. In a passive model of bacteraemia, infant rats were protected from challenge with Hib after transfer of anti-rTbp2 antiserum, but not after anti-rTbp1 antiserum.

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Section: Discussionmentioning

confidence: 99%

Cloning and expression of the Haemophilus influenzae transferrin receptor genes

Loosmore¹,

Yang²,

Coleman³

et al. 1996

Molecular Microbiology

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“…Expression of Tbp1 in Escherichia coli allows the specific binding of human Tf to the E. coii cell surface (Cornelissen el al., 1993;Palmer et al. 1993).…”

Section: How Do Tbpi and Tbp2 Contribute To Tf Receptor Function?mentioning

confidence: 99%

Iron piracy: acquisition of transferrin‐bound iron by bacterial pathogens

Cornelissen

Sparling

1994

Molecular Microbiology

233

197

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The mechanism of iron utilization from transferrin has been most extensively characterized in the pathogenic Neisseria species and Haemophilus species. Two transferrin-binding proteins, Tbp1 and Tbp2, have been identified in these pathogens and are thought to be components of the transferrin receptor. Tbp1 appears to be an integral, TonB-dependent outer membrane protein while Tbp2, a lipoprotein, may be peripherally associated with the outer membrane. The relative contribution of each of these proteins to transferrin binding and utilization is discussed and a model of iron uptake from transferrin is presented. Sequence comparisons of the genes encoding neisserial transferrin-binding proteins suggest that they are probably under positive selection for variation and may have resulted from inter-species genetic exchange.

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“…Reference source not found.). Other decreased OMPs include virulence factors, such as transferrin-binding protein A [48] and Opa [49, 50]. The cytoplasmic stress protein DnaJ [51] was also decreased in the presence of Mn.…”

Section: Resultsmentioning

confidence: 99%

Manganese regulation of virulence factors and oxidative stress resistance in Neisseria gonorrhoeae

Seib

Srikhanta

et al. 2010

Journal of Proteomics

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Neisseria gonorrhoeae has evolved a complex and novel network of oxidative stress responses, including defense mechanisms that are dependent on manganese (Mn). We performed systematic analyses at the transcriptomic and proteomic (1D SDS-PAGE and Isotope-Coded Affinity Tag [ICAT]) levels to investigate the global expression changes that take place in a high Mn environment, which results in a Mn-dependent oxidative stress resistance phenotype. These studies revealed that 97 proteins are regulated at the post-transcriptional level under conditions of increased Mn concentration, including proteins involved in virulence (eg. Pilin, a key adhesin), oxidative stress defence (eg. superoxide dismutase), cellular metabolism, protein synthesis, RNA processing and cell division. Mn regulation of inorganic pyrophosphatase (Ppa) indicated the potential involvement of phosphate metabolism in the Mn-dependent oxidative stress defense. A detailed analysis of the role of Ppa and polyphosphate kinase (Ppk) in the gonococcal oxidative stress response revealed that ppk and ppa mutant strains showed increased resistance to oxidative stress. Investigation of these mutants grown with high Mn suggests that phosphate and pyrophosphate are involved in Mn-dependent oxidative stress resistance.

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Neisseria meningitidis transferrin-binding protein 1 expressed in Escherichia coli is surface exposed and binds human transferrin

Cited by 7 publications

References 17 publications

Cloning and expression of the Haemophilus influenzae transferrin receptor genes

Cloning and expression of the Haemophilus influenzae transferrin receptor genes

Iron piracy: acquisition of transferrin‐bound iron by bacterial pathogens

Manganese regulation of virulence factors and oxidative stress resistance in Neisseria gonorrhoeae

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