Enhanced levels of Staphylococcus aureus stress protein GroEL and DnaK homologs early in infection of human epithelial cells.
Antibodies to Staphylococcus aureus heat shock proteins (Hsps) are present in the sera of patients with S. aureus endocarditis (M. W. Qoronfleh, W. Weraarchakul, and B. J. Wilkinson, Infect. Immun. 61:1567-1570, 1993). Although these proteins are immunogenic, their role in infection has not been established. We developed a cell culture system as a model to examine the potential involvement of staphylococcal Hsps in the initial events of infection. This study supports a model in which a clinical endocarditis isolate responds to host cell signals by selectively regulating the synthesis of numerous proteins, including the stress proteins Hsp60 (GroEL homolog) and Hsp70 (DnaK homolog) and a unique 58-kDa protein.
Qoronfleh
M W
MW
Structural Biochemistry Program, SAIC Frederick, National Cancer Institute-Frederick Cancer Research and Development Center, Frederick, Maryland 21702-1201, USA. ooronfle@ncifcrf.gov
Bortner
C A
CA
Schwartzberg
P
P
Wilkinson
B J
BJ
D002450:Cell Communication; D002460:Cell Line; D018834:Chaperonin 60 / Q000096:biosynthesis*; D004696:Endocarditis / Q000382:microbiology; D004847:Epithelial Cells / Q000382:microbiology*; D029968:Escherichia coli Proteins; D018840:HSP70 Heat-Shock Proteins / Q000096:biosynthesis*; D006801:Humans; D013211:Staphylococcus aureus / Q000378:metabolism*
D018834:Chaperonin 60; D029968:Escherichia coli Proteins; D018840:HSP70 Heat-Shock Proteins; C063842:dnaK protein, E coli