Abstract
Background Tuberculosis (TB) drug research and development has witnessed resurgence in recent times primarily due to the high mortality rates despite the availability of front line drugs and a prominent BCG vaccine. Synergy of TB with HIV is another factor which has warranted a search for newer therapeutic interventions. Treatment of latent TB infection is also the need of the hour. Iron acquisition is an important virulence mechanism of Mycobacterium tuberculosis (MTB). To scavenge iron, bacterial species have developed high affinity, low molecular weight iron chelators termed as siderophores. To counteract the detrimental effect of microbial iron acquisition systems, the host secretes a 21kDa lipocalin protein (Siderocalin) that binds with these iron laden siderophores in an attempt to restrict the growth of MTB within host macrophages.
Highlights
Tuberculosis (TB) drug research and development has witnessed resurgence in recent times primarily due to the high mortality rates despite the availability of front line drugs and a prominent BCG vaccine
Bacterial species have developed high affinity, low molecular weight iron chelators termed as siderophores
To counteract the detrimental effect of microbial iron acquisition systems, the host secretes a 21kDa lipocalin protein (Siderocalin) that binds with these iron laden siderophores in an attempt to restrict the growth of Mycobacterium tuberculosis (MTB) within host macrophages
Summary
Tuberculosis (TB) drug research and development has witnessed resurgence in recent times primarily due to the high mortality rates despite the availability of front line drugs and a prominent BCG vaccine. Synergy of TB with HIV is another factor which has warranted a search for newer therapeutic interventions. Iron acquisition is an important virulence mechanism of Mycobacterium tuberculosis (MTB). Bacterial species have developed high affinity, low molecular weight iron chelators termed as siderophores. To counteract the detrimental effect of microbial iron acquisition systems, the host secretes a 21kDa lipocalin protein (Siderocalin) that binds with these iron laden siderophores in an attempt to restrict the growth of MTB within host macrophages. Unfavourable positive binding energies for mycobactin- a salicylate derived MTB siderophore indicated that siderocalin does not dock well with mycobactin
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