The German organic chemist Johann Peter Griess (1829–88), who first developed the diazotization of aryl amines (the key reaction in the synthesis of the azo dyes), and a major figure in the formation of the modern dye industry, worked for more than a quarter of a century at the brewery of Samuel Allsopp and Sons in Burton upon Trent, which, owing to the presence of several notable figures and an increase in the scientific approach to brewing, became a significant centre of scientific enquiry in the 1870s and 1880s. Unlike the other Burton brewing chemists, Griess paralleled his work at the brewery with significant contributions to the chemistry of synthetic dyes, managing to keep the two activities separate—to the extent that some of his inventions in dye chemistry were filed as patents on behalf of the German dye company BASF, without the involvement of Allsopp's. This seemingly unlikely situation can be explained partly by the very different attitudes to patent protection in Britain and in Germany combined with an apparent indifference to the significant business opportunity that the presence of a leading dye chemist presented to Allsopp's. Although his work for the brewery remained largely proprietary, Griess's discoveries in dye chemistry were exploited by the German dye industry, which quickly outpaced its British counterpart. One less well-known connection between brewing and synthetic dyes, and one that may further explain Allsopp's attitude, is the use of synthetic dyes in identifying microorganisms—the perennial preoccupation of brewers seeking to maintain yield and quality. Developments of Griess's original work continue to be applied to many areas of science and technology.
Humans have co-evolved with a dense community of microbial symbionts that inhabit the lower intestine. In the colon, secreted mucus creates a physical barrier that separates these microbes from the intestinal epithelium. Some gut bacteria are able to utilize mucin glycoproteins, the main mucus component, as a nutrient source. However, it remains unclear which bacterial enzymes initiate the degradation of the highly complex O-glycans found in mucins. In the colon, these glycans are heavily sulfated, but the specific sulfatases that are active on colonic mucins have not been identified. Here, we show that sulfatases are essential to the utilization of colonic mucin O-glycans by the human gut symbiont Bacteroides thetaiotaomicron. We have characterized the activity of 12 different sulfatases encoded by this species, showing that these enzymes collectively are active on all of the known sulfate linkages in colonic O-glycans. Crystal structures of 3 enzymes provide mechanistic insight into the molecular basis of substrate-specificity. Unexpectedly, we found that a single sulfatase is essential for utilization of sulfated O-glycans in vitro and also plays a major role in vivo. Our results provide insight into the mechanisms of mucin degradation by gut bacteria, an important process for both normal microbial gut colonization and diseases such as inflammatory bowel disease (IBD). Sulfatase activity is likely to be a keystone step in bacterial mucin degradation and inhibition of these enzymes may therefore represent a viable therapeutic path for treatment of IBD and other diseases.
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