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Key Findings
Mutations in rpoB are responsible for rifampicin resistance in Mycobacterium tuberculosis.
| Gene | Protein Change | Nucleotide Change | Mechanism | Organism | Resistance To | Database | Validation Status |
|---|---|---|---|---|---|---|---|
| H445Y | - | disrupts an intermolecular hydrogen bond between histidine and rifampicin and introduces an aromatic ring that sterically interferes with rifampicin binding | Mycobacterium tuberculosis | Rifampicin | Reslit | - | |
| H445N | - | - | Mycobacterium tuberculosis | Rifampicin | Reslit | - | |
| H445D | - | replaces a neutral histidine with a negatively charged residue, weakening hydrogen bonding and destabilizing drug interactions | Mycobacterium tuberculosis | Rifampicin | Reslit | - | |
| H445L | - | - | Mycobacterium tuberculosis | Rifampicin | Reslit | - | |
| D435V | - | substitutes the negatively charged aspartate with a bulkier nonpolar valine residue causing steric hindrance within the rifampicin-binding pocket | Mycobacterium tuberculosis | Rifampicin | Reslit | - | |
| L452P | - | - | Mycobacterium tuberculosis | Rifampicin | Reslit | - | |
| L430P | - | - | Mycobacterium tuberculosis | Rifampicin | Reslit | - | |
| I491F | - | - | Mycobacterium tuberculosis | Rifampicin | Reslit | - | |
| S450L | - | disrupts a key intermolecular hydrogen bond between serine and RIF and introduces a hydrophobic leucine residue that causes steric hindrance | Mycobacterium tuberculosis | Rifampicin | Reslit | - | |
| D435Y | - | - | Mycobacterium tuberculosis | Rifampicin | Reslit | - |
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