Discrimination between apo and iron-loaded forms of transferrin by transferrin binding protein B and its N-terminal subfragment

Retzer, Mark D.; Yu, Rong-hua; Zhang, Yinping; Gonzalez, Guido C.; Schryvers, Anthony B.

doi:10.1006/mpat.1998.0226

Cited by 57 publications

(44 citation statements)

References 14 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The strong preference of TbpB for binding the iron-loaded form of Tf (12,13) and the potential for an unstructured anchor peptide to extend far from the surface of the outer membrane (18) suggest that the primary role of TbpB many be in the initial capture of iron-loaded Tf (19) (Fig. 7).…”

Section: Discussionmentioning

confidence: 99%

“…Studies with a TbpB-deficient strain of the porcine pathogen Actinobacillus pleuropneumoniae demonstrated that although growth with porcine Tf as the iron source was possible in vitro, the strain was avirulent and unable to colonize the host, suggesting that TbpB is essential for iron acquisition in vivo (10). It has been proposed that TbpB may play a role in the efficient capture of the iron-loaded form of Tf (11) because TbpB, but not TbpA, has a strong preference for binding to the iron-loaded form of Tf (12,13).…”

mentioning

confidence: 99%

“…The interaction of TbpB with holoTf involves regions on both the C1 and the C2 domains of the C-lobe (20,21) maintaining Tf in the closed conformation, thus limiting the release of iron (20,23). It is unclear how TbpA is capable of binding both the holo and the apo forms of Tf (12), but it might suggest that TbpA binds both forms of Tf in an intermediate conformation. The proposal that iron removal involves separation of the two Tf domains (C1 and C2) that flank the iron-binding site (24) implies that TbpA binds to both domains.…”

mentioning

confidence: 99%

See 2 more Smart Citations

Anchor Peptide of Transferrin-binding Protein B Is Required for Interaction with Transferrin-binding Protein A

Yang

Calmettes

et al. 2011

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

Background: Transferrin receptors are critical for survival of important Gram-negative bacterial pathogens. Results: The anchoring peptide of TbpB mediates interaction with TbpA. Conclusion:The anchor peptide mediates the process by which TbpB captures transferrin and delivers it to TbpA. Significance: TbpB is critical for survival of important bacterial pathogens and this study provides insights to its role in acquiring iron.

show abstract

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

Anchor Peptide of Transferrin-binding Protein B Is Required for Interaction with Transferrin-binding Protein A

Yang

Calmettes

et al. 2011

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

show abstract

“…TbpBdeficient gonococci can grow only poorly under the same conditions (9). TbpB also has the ability to distinguish between apo-and holotransferrin and binds the holotransferrin with a 100-fold-higher affinity, whereas TbpA does not (26,48,121,125,128,176). The specificity and high affinity of TbpB for the correct iron-loaded substrate is undoubtedly key to its function in the transferrin receptor complex.…”

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

View full text Add to dashboard Cite

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.

show abstract

“…115 Retzer et al 102 proposed that outer membrane iron-binding proteins transferrin-binding protein A and B (Tbp A and Tbp B) could serve as adhesin molecules because their homologue in Neisseria meningitidis is expressed on the bacterial surface. 102 Furthermore, based on evaluation of the M haemolytica genome sequence and in comparison with the sequences from N meningitidis and Bordetella sp filamentous hemagglutinin, Figure 1. Lung; bovine.…”

mentioning

confidence: 99%

Mannheimia haemolytica

2010

View full text Add to dashboard Cite

Mannheimia haemolytica serotype S1 is considered the predominant cause of bovine pneumonic pasteurellosis, or shipping fever. Various virulence factors allow M haemolytica to colonize the lungs and establish infection. These virulence factors include leukotoxin (LKT), lipopolysaccharide, adhesins, capsule, outer membrane proteins, and various proteases. The effects of LKT are species specific for ruminants, which stem from its unique interaction with the bovine b2 integrin receptor present on leukocytes. At low concentration, LKT can activate bovine leukocytes to undergo respiratory burst and degranulation and stimulate cytokine release from macrophages and histamine release from mast cells. At higher concentration, LKT induces formation of transmembrane pores and subsequent oncotic cell necrosis. The interaction of LKT with leukocytes is followed by activation of these leukocytes to undergo oxidative burst and release proinflammatory cytokines such as interleukins 1, 6, and 8 and tumor necrosis factor a. Tumor necrosis factor a and other proinflammatory cytokines contribute to the accumulation of leukocytes in the lung. Formation of transmembrane pores and subsequent cytolysis of activated leukocytes possibly cause leakage of products of respiratory burst and other inflammatory mediators into the surrounding pulmonary parenchyma and so give rise to fibrinous and necrotizing lobar pneumonia. The effects of LKT are enhanced by lipopolysaccharide, which is associated with the release of proinflammatory cytokines from the leukocytes, activation of complement and coagulation cascade, and cell cytolysis. Similarly, adhesins, capsule, outer membrane proteins, and proteases assist in pulmonary colonization, evasion of immune response, and establishment of the infection. This review focuses on the roles of these virulence factors in the pathogenesis of shipping fever.

show abstract

Discrimination between apo and iron-loaded forms of transferrin by transferrin binding protein B and its N-terminal subfragment

Cited by 57 publications

References 14 publications

Anchor Peptide of Transferrin-binding Protein B Is Required for Interaction with Transferrin-binding Protein A

Anchor Peptide of Transferrin-binding Protein B Is Required for Interaction with Transferrin-binding Protein A

Iron Transport Systems in Neisseria meningitidis

Mannheimia haemolytica

Contact Info

Product

Resources

About