Antibacterial Properties of the Mammalian L-Amino Acid Oxidase IL4I1.

Marie-Line Puiffe 1 Isabelle Lachaise 2 Valérie Molinier-Frenkel 3, * Flavia Castellano 3, *
* Auteur correspondant
1 Equipe 09
IMRB - Institut Mondor de Recherche Biomédicale
2 ICMPE - Institut de Chimie et des Matériaux Paris-Est
3 Equipe 09
Service d'immunologie biologique, IMRB - Institut Mondor de Recherche Biomédicale
Abstract : L-amino acid oxidases (LAAO) are flavoproteins that catalyze the oxidative deamination of L-amino acids to a keto-acid along with the production of H(2)O(2) and ammonia. Interleukin 4 induced gene 1 (IL4I1) is a secreted LAAO expressed by macrophages and dendritic cells stimulated by microbial derived products or interferons, which is endowed with immunoregulatory properties. It is the first LAAO described in mammalian innate immune cells. In this work, we show that this enzyme blocks the in vitro and in vivo growth of Gram negative and Gram positive bacteria. This antibiotic effect is primarily mediated by H(2)O(2) production but is amplified by basification of the medium due to the accumulation of ammonia. The depletion of phenylalanine (the primary amino acid catabolized by IL4I1) may also participate in the in vivo inhibition of staphylococci growth. Thus, IL4I1 plays a distinct role compared to other antibacterial enzymes produced by mononuclear phagocytes.
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PLoS ONE, Public Library of Science, 2013, 8 (1), pp.e54589. 〈10.1371/journal.pone.0054589〉
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Marie-Line Puiffe, Isabelle Lachaise, Valérie Molinier-Frenkel, Flavia Castellano. Antibacterial Properties of the Mammalian L-Amino Acid Oxidase IL4I1.. PLoS ONE, Public Library of Science, 2013, 8 (1), pp.e54589. 〈10.1371/journal.pone.0054589〉. 〈inserm-00796014〉

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