Evolution of the ferric enterobactin receptor in gram-negative bacteria

Rutz, Jeanette M.; Abdullah, Tariq; Singh, Shiva P.; Kalve, V I; Klebba, Phillip E.

doi:10.1128/jb.173.19.5964-5974.1991

Cited by 88 publications

(91 citation statements)

References 77 publications

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“…Because it has been previously reported that N. gonorrhoeae can utilize aerobactin (67) and enterobactin (45) as iron sources, we decided to determine if FrpB functioned as either an aerobactin or enterobactin receptor. FA19, FA6808, FA6747, KDF541, KDF541/pABN6, and BN1071 (Table 1) were iron stressed in CDM as described above and plated onto CDM agarose containing 2.5 M 30% iron-saturated Tf.…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Cloning, sequencing, and characterization of the gene encoding FrpB, a major iron-regulated, outer membrane protein of Neisseria gonorrhoeae

Beucher

Sparling

1995

J Bacteriol

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FrpB (for Fe-regulated protein B) is a 76-kDa outer membrane protein that is part of the iron regulon of Neisseria gonorrhoeae and Neisseria meningitidis. The frpB gene from gonococcal strain FA19 was cloned and sequenced. FrpB was homologous to several TonB-dependent outer membrane receptors of Escherichia coli as well as HemR of Yersinia enterocolitica and CopB of Moraxella catarrhalis. An ⍀ insertion into the frpB coding sequence caused a 60% reduction in 55 Fe uptake from heme, but careful analysis suggested that this effect was nonspecific. While FrpB was related to the family of TonB-dependent proteins, a function in iron uptake could not be documented.

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Section: Resultsmentioning

confidence: 99%

“…Nevertheless, it has been reported to utilize the Escherichia coli siderophores aerobactin (67) and enterobactin (45). All gonococci are capable of utilizing Tf-bound iron directly (38).…”

mentioning

confidence: 99%

Cloning, sequencing, and characterization of the gene encoding FrpB, a major iron-regulated, outer membrane protein of Neisseria gonorrhoeae

Beucher

Sparling

1995

J Bacteriol

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“…Since surface domains of OM proteins act as receptors for phages and colicins, the variability in their constituent residues may arise from selective pressure to evade such toxic agents and antibodies (4). Indeed, the study of an OM protein, FepA, among various species showed that the surface residues undergo a more rapid evolutionary change than polypeptides that are buried in the OM bilayer (49).…”

Section: Methodsmentioning

confidence: 99%

“…This finding suggests that appropriate natural or synthetic porin peptides may be effective vaccines against enteric bacterial pathogens. However, such evolutionarily preserved regions of OM proteins are known to consist primarily of polypeptides that are buried within the OM bilayer (24,49) and are therefore refractory to immune recognition. The shielding of OM protein epitopes by LPS and capsule further obscures this question (2,9,18,26,32,36,37,56,57).…”

Section: Methodsmentioning

confidence: 99%

Structural relatedness of enteric bacterial porins assessed with monoclonal antibodies to Salmonella typhimurium OmpD and OmpC

et al. 1992

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The immunochemistry and structure of enteric bacterial porins are critical to the understanding of the immune response to bacterial infection. We raised 41 monoclonal antibodies (MAbs) to SalmoneUla typhimurium OmpD and OmpC porin trimers and monomers. Enzyme-linked immunosorbent assays, immunoprecipitations, and/or Western immunoblot techniques indicated that 39 in the panel are porin specific and one binds to the lipopolysaccharide; the specificity of the remaining MAb probably lies in the porin-lipopolysaccharide complex. Among the porin-specific MAbs, 10 bound cellsurface-exposed epitopes, one reacted with a periplasmic epitope, and the remaining 28 recognized determinants that are buried within the outer membrane bilayer. Many of the MAbs reacting with surface-exposed epitopes were highly specific, recognizing only the homologous porin trimers; this suggests that the cellsurface-exposed regions of porins tend to be quite different among S. typhimurium OmpF, OmpC, and OmpD porins. Immunological cross-reaction showed that S. typhimurium OmpD was very closely related to Escherichia coli NmpC and to the Lc porin of bacteriophage PA-2. Immunologically, E. coli OmpG and protein K also appear to belong to the family of closely related porins including E. coli OmpF, OmpC, PhoE, and NmpC and S. typhimurium OmpF, OmpC, and OmpD. It appears, however, that S. typhimurium "PhoE" is not closely related to this group. Finally, about one-third of the MAbs that presumably recognize buried epitopes reacted with porin domains that are widely conserved in 13 species of the family Enterobacteriaceae, but apparently not in the seven nonenterobacterial species tested. These data are evaluated in relation to host immune response to infection by gram-negative bacteria.

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“…Together, these receptors enable the meningococcus to use various human iron-loaded proteins, such as lactoferrin, transferrin and haemoglobin [5]. Furthermore, although the meningococcus does not appear to produce its own siderophores, it has the ability to use siderophores secreted by other bacteria [6]. The major iron-limitation-induced OMP of N. meningitidis is a w70-kDa protein designated FrpB (Ferric-repressed protein B) [7].…”

Section: Introductionmentioning

confidence: 99%

Immunogenicity and structural characterisation of an in vitro folded meningococcal siderophore receptor (FrpB, FetA)

Kortekaas

Müller

Ringler

et al. 2006

Microbes and Infection

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The iron-limitation-inducible protein FrpB of Neisseria meningitidis is an outer-membrane-localized siderophore receptor. Because of its abundance and its capacity to elicit bactericidal antibodies, it is considered a vaccine candidate. Bactericidal antibodies against FrpB are, however, type-specific. Hence, an FrpB-based vaccine should comprise several FrpB variants to be capable of providing broad protection. To facilitate the development of a meningococcal subunit vaccine, we have established a procedure to obtain large quantities of the protein in a native-like conformation. The protein was expressed without its signal sequence in Escherichia coli, where it accumulated in inclusion bodies. After in vitro folding, the protein was biochemically, biophysically and biologically characterised. Our results show that in vitro folded FrpB assembles into oligomers, presumably dimers, and that it induces high levels of bactericidal antibodies in laboratory animals.

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Evolution of the ferric enterobactin receptor in gram-negative bacteria

Abstract: Using sodium dodecyl sulfate-polyacrylamide gel electrophoresis of iron-deficient and replete cell

Cited by 88 publications

References 77 publications

Cloning, sequencing, and characterization of the gene encoding FrpB, a major iron-regulated, outer membrane protein of Neisseria gonorrhoeae

Cloning, sequencing, and characterization of the gene encoding FrpB, a major iron-regulated, outer membrane protein of Neisseria gonorrhoeae

Structural relatedness of enteric bacterial porins assessed with monoclonal antibodies to Salmonella typhimurium OmpD and OmpC

Immunogenicity and structural characterisation of an in vitro folded meningococcal siderophore receptor (FrpB, FetA)

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