Protective effect of HelD against rifampicin. Credit: Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences (IOCB Prague)
One of the main challenges of contemporary medicine is posed by the resistance of pathogens to antibiotics. An important step in countering it has now been made by researchers from IOCB Prague, in collaboration with colleagues from the Institute of Microbiology and the Institute of Biotechnology of the Czech Academy of Sciences. Leveraging advanced cryogenic electron microscopy and biochemical methods, they have managed to describe how mycobacteria defend themselves against the antibiotic rifampicin. Their latest study on the matter has been published in the journal Nature Communications.
One key component that allows a bacterium to dodge the action of the antibiotic rifampicin is a protein called HelD. It effectively protects bacterial RNA polymerase, which is the enzyme taking care of the transcription of genetic information from DNA to RNA, a process that is crucial for the survival of all bacteria.
The HelD protein acts as a cellular bodyguard. Whenever there’s a snag during the transcription of DNA, HelD comes to the rescue, and this is also what happens after the administration of rifampicin, the role of which is to inhibit RNA polymerase. Without HelD, the whole process would grind to a halt and the bacterium would perish. HelD does not yield even to such a powerful antibiotic as rifampicin, which is used, for example, to treat tuberculosis or severe pneumonia.
By Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences (IOCB Prague)
Article can be accessed on: phys.org
