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Infect. Immun., May 1997, 1729-1733, Vol 65, No. 5
Copyright © 1997, American Society for Microbiology

Brief heat shock treatment induces a long-lasting alteration in the glycolipid receptor binding specificity and growth rate of Haemophilus influenzae

E Hartmann and C Lingwood
Department of Microbiology, Research Institute, Hospital for Sick Children, Toronto, Ontario, Canada.

After brief heat shock treatment, clinical strains of nontypeable Haemophilus influenzae show a long-lasting change in the binding specificity for glycolipids and a markedly increased growth rate in vitro. Non-heat-shocked H. influenzae specifically binds to phosphatidylethanolamine (PE), gangliotetraosylceramide (Gg4), and gangliotriosylceramide (Gg3) and binds minimally to sulfatoxygalactosylceramide (SGC; also called sulfatide). After a 5-min heat shock at 42 degrees C, strains of H. influenzae showed a marked increase in binding to SGC and acquired the ability to bind to sulfatoxygalactosylglycerol (SGG) in thin-layer chromatography overlays. Additionally, heat-shocked H. influenzae cells showed an increased growth rate (twofold). Increased sulfatide binding and growth rate were retained for approximately 60 generations, after which the heat-shocked organisms reverted to their original glycolipid binding pattern (i.e., PE, Gg3, and Gg4) and growth rate. Such organisms could then be reexposed to heat, and the heat shock phenotype would be reestablished. After exposure of the organisms to brief heat shock, Western blotting of a surface extract of H. influenzae with anti-bovine- brain hsp-70 monoclonal antibody showed an increase in two protein bands at 82 and 60 kDa. This antibody was a potent inhibitor of the binding of heat-shocked H. influenzae to SGC and SGG but had no effect on PE, Gg3, or Gg4 binding in vitro. In contrast, an antibody against an H. influenzae PE-Gg3-Gg4-binding adhesin that was recently identified (J. Busse, E. Hartmann, and C. A. Lingwood, J. Infect. Dis. 175:77-83, 1996) selectively inhibited the organism's binding to PE and Gg3. This indicates that cell surface hsp-70-related heat shock proteins can mediate H. influenzae attachment to sulfoglycolipids following heat shock. We suggest that such increased binding to sulfated glycolipids may be a response to fever following H. influenzae infection in humans.

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