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posted by janrinok on Wednesday April 08 2020, @11:37PM   Printer-friendly
from the no,-not-the-railway dept.

Blocking the Iron Transport Could Stop Tuberculosis:

"The transport protein, which is located in the bacterial membrane, is essential for the survival of the pathogens. If IrtAB is absent or not functioning, M. tuberculosis can no longer reproduce inside the human cell", says Seeger.

Using a combination of cryo-electron microscopy and X-ray crystallography, the researchers solved for the first time a high-resolution structure of the transport protein IrtAB. This analysis was done in collaboration with Ohad Medalia, professor at the Department of Biochemistry of UZH. According to its spatial structure, IrtAB belongs to the so-called ABC exporters, which are typically involved in the efflux of molecules out of the bacterial cell. "However, we were able to show that IrtAB in fact imports mycobactins into M. tuberculosis. It therefore transports molecules in the opposite direction than expected," says Markus Seeger.

[...] "IrtAB is a potential drug target, because its deletion renders M. tuberculosis inactive and incapable of infection. With our structural and functional elucidation of IrtAB, we opened avenues to develop novel tuberculosis drugs that inhibit the iron transport into the bacteria", Seeger concludes. "In view of Covid-19, a disease that also affects the lungs, tuberculosis will likely play a more important role again in the future. It is quite conceivable that patients weakened by Covid-19 will show increased infection rates with tuberculosis," he adds.

More information: Fabian M. Arnold et al, The ABC exporter IrtAB imports and reduces mycobacterial siderophores, Nature (2020). DOI: 10.1038/s41586-020-2136-9

Journal information: Nature


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  • (Score: 0) by Anonymous Coward on Thursday April 09 2020, @12:07AM

    by Anonymous Coward on Thursday April 09 2020, @12:07AM (#980439)

    Too much salt in your bloodstream, ari.