Heat-inducible surface stress protein (Hsp70) mediates sulfatide recognition of the respiratory pathogen Haemophilus influenzae.
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.
Hartmann
E
E
Zentrum für Infektionsforschung, Universität Würzburg, Röntgenring 11, Würzburg, Germany. evamarie.hartmann@mail.uni-wuerzberg.de
Lingwood
C A
CA
Reidl
J
J
D001426:Bacterial Proteins / Q000378:metabolism*; D003001:Cloning, Molecular; D029968:Escherichia coli Proteins; D019084:Fluorescent Antibody Technique, Indirect; D006017:Glycolipids / Q000378:metabolism; D018840:HSP70 Heat-Shock Proteins / Q000032:analysis / Q000378:metabolism*; D006193:Haemophilus influenzae / Q000378:metabolism*; D006358:Hot Temperature; D013433:Sulfoglycosphingolipids / Q000378:metabolism*
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D006017:Glycolipids; D018840:HSP70 Heat-Shock Proteins; D013433:Sulfoglycosphingolipids; C063842:dnaK protein, E coli