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Differentiation of Shigella species from Escherichia coli by glycerol dehydrogenase activity
The biochemical identification of Shigella sometimes presents difficulties in differentiating it from the biochemically atypical E. coli strains. NAD super(+)-linked glycerol dehydrogenase, glyDH-II, induced by glycerol and hydroxyacetone (thus distinct from glyDH-I) responsible for salvaging the gl...
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Published in: | Research in microbiology 1995, Vol.146 (9), p.787-790 |
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Main Authors: | , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | The biochemical identification of Shigella sometimes presents difficulties in differentiating it from the biochemically atypical E. coli strains. NAD super(+)-linked glycerol dehydrogenase, glyDH-II, induced by glycerol and hydroxyacetone (thus distinct from glyDH-I) responsible for salvaging the glycerol moiety of degradation products of phospholipids and triglycerides, has been described in E. coli. This study evaluated glyDHs as complementary tests for differentiating E. coli from Shigella species. A total of 1,000 recent isolates belonging to E. coli (626 strains) and Shigella species (374 strains) from human clinical specimens (stool, urine, blood) or veterinary specimens (E. coli only) received at the French Salmonella and Shigella Reference Center (CNS) were included. 610/626 (97%) of E. coli strains tested produced a glyDH type II induced by glycerol and hydroxyacetone, and no Shigella strain demonstrated such activity except S. flexneri serotype 6 biotype Manchester. |
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ISSN: | 0923-2508 1769-7123 |
DOI: | 10.1016/0923-2508(96)81074-6 |