The fla gene of Borrelia burgdorferi GeHo was analyzed and expressed in Escherichia coli. The structural gene encodes a flagellar protein of 336 amino acids. Comparative sequence analysis of the amino acid sequence revealed a high degree of sequence conservation with flagellins from both phylogenetically related and unrelated bacteria. The antigenic properties of the B. burgdorferi Fla protein were studied by synthesizing overlapping octapeptides, which were screened by using a battery of different monoclonal and polyclonal antibodies from various species directed against native and denatured flagellar proteins. No single species-independent immunodominant epitope could be located. However, immunoreactive oligopeptides clustered within the variable middle region (N-180 to I-260). This region could constitute a candidate antigen for more specific and sensitive serodiagnosis of Lyme borreliosis.
A total of 17 B. burgdorfieri isolates from various sources were characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis of whole-cell proteins, restriction enzyme analysis, Southern hybridization with probes complementary to unique regions of evolutionarily conserved genes (16S rRNA and fla), and direct sequencing of in vitro polymerase chain reaction-amplified fragments of the 16S rRNA gene. Three groups were distinguished on the basis of phenotypic and genotypic traits, the latter traced to the nucleotide sequence level.
Phosphane is one of the last small molecules whose biogenesis has not yet been elucidated. The first analyses of the PH3, content of the rumen and gut as well as the feces and liquid manure of cattle and pigs, of the feces of man and of the intestinal tract of fish indicate the ubiquitous production of PH3, in the bio‐ and hydrosphere and that its formation is closely correlated with methane biogenesis. In view of the toxicity of phosphane these results are particularly significant; on a humorous note, they may also provide a plausible explanation for “fire‐breathing” dragons and will‐o'‐the wisp.
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