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Infection and Immunity, May 2001, p. 3438-3441, Vol. 69, No. 5
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.5.3438-3441.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Heat-Inducible Surface Stress Protein (Hsp70) Mediates Sulfatide Recognition of the Respiratory Pathogen Haemophilus influenzae

Evamarie Hartmann,1,* Clifford A. Lingwood,2 and Joachim Reidl1

Zentrum für Infektionsforschung, Universität Würzburg, Röntgenring 11, Würzburg, Germany,1 and Research Institute, Hospital for Sick Children, and Departments of Biochemistry and Laboratory Medicine and Pathobiology, University of Toronto, Toronto, Canada2

Received 27 November 2000/Returned for modification 27 December 2000/Accepted 29 January 2001

The in vitro glycolipid binding specificity of clinical strains of nontypeable Haemophilus influenzae is altered to include sulfated glycolipids following a brief heat shock. We have constructed, expressed, and purified a recombinant protein of H. influenzae Hsp70, which showed significant specific binding to sulfated galactolipids in vitro. Furthermore, indirect immunofluorescence demonstrates that Hsp70 proteins are surface exposed in H. influenzae only after heat shock and are contained in the outer membrane protein fractions.

* Corresponding author. Mailing address: Zentrum für Infektionsforschung, Universität Würzburg, 97070 Würzburg, Germany. Phone: 0049 (0) 931/312125. Fax: 0049 (0) 931/312578. E-mail: evamarie.hartmann{at}mail.uni-wuerzburg.de.

Infection and Immunity, May 2001, p. 3438-3441, Vol. 69, No. 5
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.5.3438-3441.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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Copyright © 2001 by the American Society for Microbiology. All rights reserved.