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Infection and Immunity, June 2004, p. 3461-3470, Vol. 72, No. 6
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.6.3461-3470.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Role of Transferrin Receptor from a Neisseria meningitidis tbpB Isotype II Strain in Human Transferrin Binding and Virulence

Geneviève Renauld-Mongénie,* David Poncet, Michèle Mignon, Sophie Fraysse, Christophe Chabanel, Bernard Danve, Tino Krell, and Marie-José Quentin-Millet

Aventis Pasteur, 69280 Marcy l'Etoile, France

Received 18 November 2003/ Returned for modification 2 January 2004/ Accepted 28 January 2004

Neisseria meningitidis acquires iron through the action of the transferrin (Tf) receptor, which is composed of the Tf-binding proteins A and B (TbpA and TbpB). Meningococci can be classified into isotype I and II strains depending on whether they harbor a type I or II form of TbpB. Both types of TbpB have been shown to differ in their genomic, biochemical, and antigenic properties. Here we present a comparative study of isogenic mutants deficient in either or both Tbps from the isotype I strain B16B6 and isotype II strain M982. We show that TbpA is essential in both strains for iron uptake and growth with iron-loaded human Tf as a sole iron source. No growth has also been observed for the TbpB– mutant of strain B16B6, as shown previously, whereas the growth of the analogous mutant in M982 was similar to that in the wild type. This indicates that TbpB in the latter strain plays a facilitating but not essential role in iron uptake, which has been observed previously in similar studies of other bacteria. These data are discussed in relation to the fact that isotype II strains represent more than 80% of serogroup B meningococcal strains. The contribution of both subunits in the bacterial virulence of strain M982 has been assessed in a murine model of bacteremia. Both the TbpB– TbpA– mutant and the TbpA– mutant are shown to be nonvirulent in mice, whereas the virulence of the TbpB– mutant is similar to that of the wild type.

* Corresponding author. Mailing address: Aventis Pasteur, Campus Mérieux, 1541, Ave. Marcel Mérieux, 69280 Marcy l'Étoile, France. Phone: (33) 4 37 37 35 05. Fax: (33) 4 37 37 36 39. E-mail: genevieve.renauld{at}aventis.com.

Editor: D. L. Burns

Infection and Immunity, June 2004, p. 3461-3470, Vol. 72, No. 6
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.6.3461-3470.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Knight, S. A. B., Vilaire, G., Lesuisse, E., Dancis, A. (2005). Iron Acquisition from Transferrin by Candida albicans Depends on the Reductive Pathway. Infect. Immun. 73: 5482-5492 [Abstract] [Full Text]  


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