These new natural antimicrobials to combat antibiotic resistance

Published by Redbran,
Source: CEA IRIG
Other Languages: FR, DE, ES, PT

In the face of antibiotic resistance, researchers at Irig are studying new natural molecules such as Ruminococcins C, which exhibit great stability under physiological conditions, high efficacy at very low doses, and low toxicity.

The WHO warns that antibiotic resistance could cause 10 million deaths annually by 2050. Scientists are therefore focusing their research on new natural molecules with structures and mechanisms of action distinct from conventional antibiotics.

Bacteriocins, or antimicrobial peptides produced by bacteria, represent a highly promising alternative. Thus, bacteria from the human gut microbiota constitute a vast field of investigation that remains largely unexplored.


Ruminococcins C exhibit effective antibacterial activity, except for RumC2, likely due to the nature of the residues (in blue).

Researchers from Irig, in collaboration with the Institut des Sciences Moléculaires de Marseille and the Laboratoire de Microbiologie Génétique et Moléculaire de Toulouse, are focusing on Ruminococcus gnavus E1, a symbiotic bacterium in our digestive system that produces several antimicrobial peptides, including Ruminococcins C.

These peptides, expressed in 5 isoforms (RumC1-5), are highly effective against pathogens that are resistant and multi-resistant to conventional antibiotics. They have varying spectra of activity without synergistic effects between different isoforms. Furthermore, while being low in toxicity, Ruminococcins C also possess other health benefits, notably anti-inflammatory properties.

Ruminococcins C have properties often lacking in other antimicrobial peptides, including high resistance to physiological conditions, efficacy at very low doses, and low toxicity. Ongoing research aims to elucidate the mechanism of action and identify the cellular target(s) of these molecules.

With financial support from ANR RUMBA (2016-2020), ANR RUMisBAC (2021-2025), CFR CEA (2016-2019/2020-2023).

References:
Shamseddine L, Roblin C, Veyrier I, Basset C, De Macedo L, Boyeldieu A, Maresca M, Nicoletti C, Brasseur G, Kieffer-Jaquinod S, Courvoisier-Dezord E, Amouric A, Carpentier P, Campo N, Bergé M, Polard P, Perrier J, Duarte V and Lafond M.
Mechanistic and functional aspects of the Ruminococcin C sactipeptide isoforms.
iScience 2023.
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