Analysis of expression of GroEL (Hsp60) of Clostridium difficile in response to stress.
Our laboratory has previously shown that adherence of Clostridium difficile to tissue culture cells is augmented by various stresses and that GroEL, a heat shock protein, serves an adhesive function in this bacterium. In this communication, RT-PCR, SDS-PAGE and immunoblotting were used to study the stress response in C. difficile following heat, acid or osmotic shock, iron deprivation or presence of a subinhibitory concentration of ampicillin in the culture medium. All these stresses increased transcription of groEL and production of GroEL to various degrees. Furthermore, the protein was found in membrane fractions and in the extracellular space after heat stress.
Hennequin
C
C
Universite de Paris-Sud, Faculte de Pharmacie, Department de Microbiologie, 5 Rue JB Clement, F-92296 Chatenay-Malabry Cedex, France.
Collignon
A
A
Karjalainen
T
T
D000667:Ampicillin / Q000494:pharmacology; D018834:Chaperonin 60 / Q000235:genetics* / Q000378:metabolism*; D016360:Clostridioides difficile / Q000235:genetics / Q000502:physiology*; D003470:Culture Media; D004591:Electrophoresis, Polyacrylamide Gel; D018869:Heat-Shock Response; D006801:Humans; D015151:Immunoblotting; D010406:Penicillins / Q000494:pharmacology; D020133:Reverse Transcriptase Polymerase Chain Reaction; D014158:Transcription, Genetic
D018834:Chaperonin 60; D003470:Culture Media; D010406:Penicillins; D000667:Ampicillin