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

Abstract：

:Many pathogens of the Pasteurellaceae and Neisseriaceae possess a surface receptor that binds transferrin (Tf) as an initial step in an iron acquisition process. This receptor is comprised of two proteins, transferrin binding protein A (TbpA) and transferrin binding protein B (TbpB). Since the ability to recognize the iron-loaded form of Tf preferentially would be a useful attribute of these receptors, we examined this property in a number of bacterial species. In solid-phase binding assays with isolated membranes, only the receptor from Moraxella catarrhalis was capable of preferentially binding iron-loaded Tf. In a competitive affinity isolation assay which enabled us to resolve TbpA and TbpB, TbpA from all tested species was shown to bind both apo and iron-loaded Tf. Under these assay conditions TbpB from M. catarrhalis, Haemophilus somnus and Pasteurella haemolytica discriminated between apo and holo Tf, whereas TbpB from Neisseria meningitidis showed no discrimination. The ability of TbpB from N. meningitidis to bind iron-saturated hTf preferentially became evident in a TbpA- background or by using recombinant TbpB. In binding assays with recombinant fusion proteins, both intact TbpB and the N-terminal half of TbpB from all the tested species preferentially bound Fe-loaded Tf, indicating that this may be a conserved mechanism by which these organisms optimize their ability to acquire iron.

journal_name

Microb Pathog

journal_title

Microbial pathogenesis

authors

Retzer MD,Yu Rh,Zhang Y,Gonzalez GC,Schryvers AB

doi

10.1006/mpat.1998.0226

subject

Has Abstract

pub_date

1998-10-01 00:00:00

pages

175-80

issue

4

eissn

0882-4010

issn

1096-1208

pii

S0882401098902261

journal_volume

25

pub_type

杂志文章

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