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Structural characterization of the lactoferrin receptor from Neisseria meningitidis

T Prinz1, M Meyer, A Pettersson

  • 1Department of Molecular Microbiology and Institute of Biomembranes, Utrecht University, 3584 CH Utrecht, The Netherlands. T.C.Prinz@bio.uu.nl

Journal of Bacteriology
|July 10, 1999
PubMed

Insights

The meningococcal lactoferrin receptor, essential for bacterial iron uptake, involves outer membrane protein LbpA and lipoprotein LbpB. Researchers identified LbpA complexes and surface loops, supporting existing models.

Area of Science:

  • Microbiology
  • Structural Biology
  • Protein Biochemistry

Background:

  • The meningococcal lactoferrin receptor facilitates iron acquisition, crucial for Neisseria meningitidis survival and virulence.
  • This receptor is known to comprise the outer membrane protein LbpA and the lipoprotein LbpB.

Purpose of the Study:

  • To characterize the oligomeric states of the meningococcal lactoferrin receptor components.
  • To identify and map surface-exposed regions of LbpA.
  • To validate a proposed topological model for LbpA.

Main Methods:

  • Analysis of protein complexes using biochemical techniques.
  • Identification of cell surface-exposed loops on LbpA through experimental methods.

Main Results:

  • Homooligomeric complexes of LbpA were detected.
  • Heterooligomeric complexes of LbpA and LbpB were identified.
  • Five distinct cell surface-exposed loops of LbpA were mapped.

Conclusions:

  • The meningococcal lactoferrin receptor exists in various oligomeric forms.
  • The identified surface loops provide partial experimental support for the proposed LbpA topology model.
  • Further structural and functional studies of the receptor complex are warranted.

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