Abstract
Human intestinal bacteria produce butyrate, which has signalling properties and can be used as energy source by enterocytes thus influencing colonic health. However, the pathways and the identity of bacteria involved in this process remain unclear. Here we describe the isolation from the human intestine of Intestinimonas strain AF211, a bacterium that can convert lysine stoichiometrically into butyrate and acetate when grown in a synthetic medium. Intestinimonas AF211 also converts the Amadori product fructoselysine, which is abundantly formed in heated foods via the Maillard reaction, into butyrate. The butyrogenic pathway includes a specific CoA transferase that is overproduced during growth on lysine. Bacteria related to Intestinimonas AF211 as well as the genetic coding capacity for fructoselysine conversion are abundantly present in colonic samples from some healthy human subjects. Our results indicate that protein can serve as a source of butyrate in the human colon, and its conversion by Intestinimonas AF211 and related butyrogens may protect the host from the undesired side effects of Amadori reaction products.
Highlights
Human intestinal bacteria produce butyrate, which has signalling properties and can be used as energy source by enterocytes influencing colonic health
Intestinimonas AF211 hardly grew on glucose in mineral medium, but its growth rate tripled in the presence of acetate and yeast extract
Here we describe the isolation of a butyrate-producing bacterium, Intestinimonas AF211, abundantly present in the intestine of some humans
Summary
Human intestinal bacteria produce butyrate, which has signalling properties and can be used as energy source by enterocytes influencing colonic health. Our results indicate that protein can serve as a source of butyrate in the human colon, and its conversion by Intestinimonas AF211 and related butyrogens may protect the host from the undesired side effects of Amadori reaction products. Most butyrate produced in the human intestine is assumed to derive from carbohydrates, while some specialized bacteria have been found that convert lactate plus acetate into butyrate[9,10] All of these produce butyrate via the acetyl-CoA pathway[11] (converting acetyl-CoA to butyrate) that involves a complex cascade of reactions, in which butyrate CoA transferase (But) or butyrate kinase (Buk) are key enzymes. We describe the butyrogenic conversion of lysine and the Amadori product fructoselysine by a novel Intestinimonas strain from a healthy volunteer and characterize its butyrate synthesis pathway by using a combined physiological, biochemical and proteogenomic approach
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