Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0348321 (Haemophilus)
 15,372 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Different tests for the identification of Gardnerella (Haemophilus) vaginalis and for its differentiation from catalase-negative unclassified coryneforms from the vagina were evaluated on over 200 bacterial strains, with special emphasis on optimal test conditions. A presumptive identification of G. vaginalis in the clinical laboratory can be made on the basis of colonial morphology, clear beta-hemolysis with diffuse edges on human blood bilayer-Tween agar, a negative catalase test, and typical cell morphology in the Gram stain. This procedure will correctly identify 90 to 98% of suspect colonies of G. vaginalis with human blood bilayer-Tween agar as primary isolation medium. Useful additional reactions for the confirmation of G. vaginalis include positive hippurate and starch hydrolysis, positive alpha-glucosidase but negative beta-glucosidase tests, the production of acid from glucose and maltose but not from mannitol, and susceptibility to disks containing metronidazole, nitrofurantoin, sulfonamides, and bile.
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PMID:Identification of Gardnerella (Haemophilus) vaginalis. 682 Dec 5

This study describes the characterization of BpH3, a Bordetella pertussis DNA-binding protein. Sequence analysis reveals significant homology with the H-NS sequence of Escherichia coli and Haemophilus influenzae, particularly in the C-terminal part of the proteins. Our results provide evidence that H-NS and BpH3 display functional homology. First, expression of BpH3 in an hns mutant results in restoration of motility, an H-NS-dependent phenotype. This effect is dependent on the level of BpH3 expression and results from transcriptional activation of the flagellar master operon. Second, the high level of beta-glucosidase associated with hns mutations is reversed to the low wild-type level in the presence of BpH3. Third, BpH3 is able, like H-NS, to preferentially bind in vitro to curved DNA fragments, such as flhDC and bla promoter regions. Our results are the first demonstration that proteins homologous to H-NS exist in bacteria phylogenetically distant from H. influenzae and enterobacteria.
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PMID:Characterization of BpH3, an H-NS-like protein in Bordetella pertussis. 919 8