Indole molecule (C8H7N). Source: wikimedia commons |
When a bacterial infection is treated with antibiotics, bacteria
that are in a so-called dormant, inactive state may escape death – this because
antibiotics only kill growing
bacteria. It becomes a serious problem when these sleeping beauties start to
grow again, in particular when they do so after the period of antibiotic
treatment has ended… Thus, an infection that was apparently cured could be
followed by a secondary infection days or weeks later. This problematic phenomenon
is called bacterial persistence, and it should not be confused with bacterial
resistance, in which growing bacteria are immune to one or several antibiotics.
Now what about indole? (The molecule displayed on top of
this post.) Actually indole is present in very common and important biomolecules,
such as the amino acid tryptophan, the animal hormone serotonin and the plant growth
hormone auxin. We have known for more than a century that E. coli produces indole in stationary phase (Lee, 2010), and it
does so thanks to an enzyme called tryptophanase, which cleaves tryptophane
into indole, pyruvate and ammonia.
But E.
coli is not the only bacterium capable of that: more than 85 species (both
Gram-negative and Gram-positive) can synthesize indole (Lee, 2010). For a long time the biological functions of
indole were overlooked, but now we know that indole can act as an extracellular
signal and can for instance increase antibiotic resistance and control biofilm
formation in E. coli.