Analysis of the molecular mass heterogeneity of the transferrin receptor in Neisseria meningitidis and commensal Neisseria

Ferreirós, C.M.

doi:10.1016/0378-1097(91)90484-r

Cited by 34 publications

(32 citation statements)

References 11 publications

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“…The proteins which bound transferrin were TbpA (formerly Tbp1), which was 98 kDa, and TbpB (formerly Tbp2), which was 68 kDa (66,104,143). Among different meningococcal isolates, the molecular masses of TbpA and -B vary, with TbpA ranging from 93 to 98 kDa and the more heterogeneic TbpB varying from 68 to 85 kDa (58,66,143). TbpA can be found on all strains, both invasive and carrier, and depending on the strain, there are roughly 700 to 4,700 copies per cell (117).…”

Section: Transferrin and Lactoferrin Receptorsmentioning

confidence: 99%

Iron Transport Systems in Neisseria meningitidis

Perkins-Balding

Ratliff-Griffin

Stojiljković

2004

Microbiol Mol Biol Rev

147

146

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SUMMARY Acquisition of iron and iron complexes has long been recognized as a major determinant in the pathogenesis of Neisseria meningitidis. In this review, high-affinity iron uptake systems, which allow meningococci to utilize the human host proteins transferrin, lactoferrin, hemoglobin, and haptoglobin-hemoglobin as sources of essential iron, are described. Classic features of bacterial iron transport systems, such as regulation by the iron-responsive repressor Fur and TonB-dependent transport activity, are discussed, as well as more specific features of meningococcal iron transport. Our current understanding of how N. meningitidis acquires iron from the human host and the vaccine potentials of various components of these iron transport systems are also reviewed.

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Section: Transferrin and Lactoferrin Receptorsmentioning

confidence: 99%

Iron Transport Systems in Neisseria meningitidis

Perkins-Balding

Ratliff-Griffin

Stojiljković

2004

Microbiol Mol Biol Rev

147

146

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“…TbpA is a 93-to 98-kDa outer membrane porin-like protein that interacts with TbpB to optimally remove iron from transferrin. TbpB varies in size from 68 to 85 kDa (6,23).…”

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confidence: 99%

Transgenic Mice Expressing Human Transferrin as a Model for Meningococcal Infection

Zarantonelli¹,

Szatanik²,

Giorgini³

et al. 2007

Infect Immun

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The pathogenesis of meningococcal disease is poorly understood due to the lack of a relevant animal model. Moreover, the use of animal models is not optimal as most meningococcal virulence determinants recognize receptors that are specifically expressed in human tissues. One major element of the host specificity is the system of meningococcal iron uptake by transferrin-binding proteins that bind specifically human transferrin but not murine transferrin. We developed a new mouse model for experimental meningococcal infection using transgenic mice expressing human transferrin. Intraperitoneal challenge of transgenic mice induced bacteremia for at least 48 h with an early stage of multiplication, whereas the initial inoculum was rapidly cleared from blood in wild-type mice. Inflammation in the subarachnoidal space with a high influx of polymorphonuclear cells was observed only in transgenic mice. Meningococcal mutants that were unable to use transferrin as a source of iron were rapidly cleared from both wild-type and transgenic mice. Thus, transgenic mice expressing human transferrin may represent an important advance as a new mouse model for in vivo studies of meningococcal virulence and immunogenicity factors.

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“…The size of Tbpl is about 95,000 in all strains, while the apparent molecular weight (MW) of Tbp2 varies from about 66,000 to 85,000 in different strains (5,18). Antigenic heterogeneity of Tbp2 has been reported in several studies (6,8), while the existence of common antigenic epitopes has been demonstrated among molecularly heterogeneous Thp2s of N. meningitidis (22).…”

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confidence: 99%

Characterization of a highly structured domain in Tbp2 from Neisseria meningitidis involved in binding to human transferrin

et al. 1994

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The binding of iron-loaded human transferrin at the surface of Neisseria meningitidis is mediated by two polypeptides, Tbp1 and Tbp2. Predicted Tbp amino acid sequences from N. meningitidis strains are highly divergent. This variability is particularly pronounced throughout the Tbp2 polypeptide. In this study, a highly structured and extremely stable Tbp2 domain of about 270 to 290 amino acids which is involved in the binding to transferrin and whose position is well conserved has been characterized. The conservation of such a remarkable structure in a very divergent protein domain (there is only 43% amino acid identity within this region) suggests that is plays an essential biological role and raises a number of questions regarding tbp2 evolution.

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Analysis of the molecular mass heterogeneity of the transferrin receptor in Neisseria meningitidis and commensal Neisseria

Cited by 34 publications

References 11 publications

Iron Transport Systems in Neisseria meningitidis

Iron Transport Systems in Neisseria meningitidis

Transgenic Mice Expressing Human Transferrin as a Model for Meningococcal Infection

Characterization of a highly structured domain in Tbp2 from Neisseria meningitidis involved in binding to human transferrin

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