Heat-Inducible Surface Stress Protein (Hsp70) Mediates Sulfatide Recognition of the Respiratory Pathogen Haemophilus influenzae
AUTOR(ES)
Hartmann, Evamarie
FONTE
American Society for Microbiology
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=98307Documentos Relacionados
- Construction of a heat-inducible gene for plants. Demonstration of heat-inducible activity of the Drosophila hsp70 promoter in plants
- Heat-inducible human factor that binds to a human hsp70 promoter.
- Heat-inducible mutants of corynebacteriophage.
- Control of Heat-Inducible λ Bacteriophage
- Inhibition of heat shock protein synthesis by heat-inducible antisense RNA.