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Journal of Bacteriology, July 1999, p. 4417-4419, Vol. 181, No. 14
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Structural Characterization of the Lactoferrin Receptor from Neisseria meningitidis

Thorsten Prinz,1,* Markus Meyer,2 Annika Pettersson,1 and Jan Tommassen1

Department of Molecular Microbiology and Institute of Biomembranes, Utrecht University, 3584 CH Utrecht, The Netherlands,1 and Institute of General Zoology and Genetics, University of Münster, 48149 Münster, Germany2

Received 4 January 1999/Accepted 11 May 1999

The meningococcal lactoferrin receptor is composed of the integral outer membrane protein LbpA and the peripheral lipoprotein LbpB. Homooligomeric complexes of LbpA and heterooligomers consisting of LbpA and LbpB were identified. Furthermore, five cell surface-exposed loops of LbpA were identified, which partially confirms a previously proposed topology model.

* Corresponding author. Mailing address: Department of Molecular Microbiology and Institute of Biomembranes, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands. Phone: 31-30-2533111. Fax: 31-30-2513655. E-mail: T.C.Prinz{at}bio.uu.nl.

Journal of Bacteriology, July 1999, p. 4417-4419, Vol. 181, No. 14
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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