In addition, commercial manufacturing of vaccines, antibiotics and other medically important proteins could become more efficient by incorporating the unique heat shock proteins into microbial cells in those processes. Future use of the proteins could also impact agriculture, fish production and other commercially important biological processes.
Microorganisms that live in deep ocean vents where water exceeds the normal boiling point possess a phenomenal capacity for resisting heat damage." says Frank Robb of UMBI's Center of Marine Biotechnology. When temperatures rise above 103 ' C, they form heat shock proteins that work as chaperones of key proteins in the cell, protecting and allowing them to remain intact at very high temperatures.
Similar chaperone proteins appear in all branches of life. In humans they help prevent cataracts by keeping the proteins in the eye lens fluids from deteriorating. The polymerase chain reaction, or PCR, which is commonly used in clinical medicine, forensic science, evolutionary biology and archeology, and genetic disease diagnostics, relies on a heat stable DNA polymerase.
Robb explains recent experiments at COMB, "We have been able to show that by adding a small heat shock protein from Pyrococcus furiosus to the DNA polymerase enzymes used in the PCR test, you can increase the sensitivity by about ten times.
In addition, when we put the gene encoding these unique chaperone proteins into E. coli, a common bacterium, the resulting genetically modified E. coli strain could grow and survive at higher temperatures," says Robb.