f Identification of Fusobacterium species by the electrophoretic migration of glutamate dehydrogenase and 2-oxoglutarate reductase in relation to their DNA base composition and peptidoglycan dibasic amino acids
- Authors: S. E. Gharbia, H. N. Shah
- J. Med. Microbiol., November 1990 33: 183-188, doi: 10.1099/00222615-33-3-183
- Subject: Review Article
- Published Online:
Identification of Fusobacterium species by the electrophoretic migration of glutamate dehydrogenase and 2-oxoglutarate reductase in relation to their DNA base composition and peptidoglycan dibasic amino acids, Page 1 of 1< Previous page | Next page > /docserver/preview/fulltext/jmm/33/3/medmicro-33-3-183-1.gif
Rapid identification of Fusobacterium spp. is hampered by their inability to ferment carbohydrates and the availability of relatively few useful phenotypic characters. In an attempt to identify new diagnostic markers for species, we reported recently the potential utility of glutamate dehydrogenase (GDH) electrophoretic mobilities for distinguishing eight species of Fusobacterium. We have extended these observations to include all recognised members of the genus except F. prausnitzii and F. perfoetens, and our results show that they cluster into three broad electrophoretic groups. Some species, such as F. periodontium, F. simiae and F. necrophorum, possessed GDH with similar electrophoretic mobilities. However, within such clusters, the electrophoretic migration of 2-oxoglutarate reductase (OGR) distinguished between species. Neither GDH or OGR mobility alone clearly differentiated all species, but their combined use provided unambiguous discrimination of all species except F. varium and F. mortiferum. The DNA base compositions of all species except F. naviforme (ATCC 25832) and F. sulci, were within the range 26-34 mol% G + C, suggesting the genus may be homogeneous. However, the peptidoglycan composition divided the genus into two major groups that contained either lanthionine or diaminopimelic acid; F. mortiferum peptidoglycan contained both dibasic amino acids.
© 1990 The Pathological Society of Great Britain and Ireland | Published by the Microbiology Society
Article metrics loading...
Full text loading...
Author and Article Information
/content/journal/jmm/10.1099/00222615-33-3-183dcterms_title,dcterms_subject,pub_serialTitlepub_serialIdent:journal/jmm AND -contentType:BlogPost64
/content/journal/jmm/10.1099/00222615-33-3-183dcterms_title,dcterms_subject-pub_serialIdent:journal/jmm AND -contentType:BlogPost64
Figure data loading....