Bordetella Pertussis
Mostrando 25-36 de 711 artigos, teses e dissertações.
-
25. Vag8, a Bordetella pertussis bvg-Regulated Protein
Bordetella pertussis expresses a bvg-regulated 95-kDa protein, Vag8, encoded by vag-8. Southern blot analysis indicates that strains of Bordetella bronchiseptica and Bordetella parapertussis have DNA homologous to vag-8. Antiserum raised to a fusion of maltose binding protein to an N-terminal 60-kDa fragment of Vag8 recognizes the native 95-kDa protein in im
American Society for Microbiology.
-
26. Detection and subcellular localization of three Ptl proteins involved in the secretion of pertussis toxin from Bordetella pertussis.
The ptl locus of Bordetella pertussis contains eight open reading frames which are predicted to encode proteins (PtlA to PtlH) that are essential for secretion of pertussis toxin from the bacterium and which are members of a family of transport proteins found in other types of bacteria. We have detected PtlE, PtlF, and PtlG in immunoblots of extracts of B. p
-
27. Real-Time PCR Assay Targeting IS481 of Bordetella pertussis and Molecular Basis for Detecting Bordetella holmesii
Detection of Bordetella holmesii by a real-time PCR assay targeting IS481 of Bordetella pertussis is reported. Sequencing of IS481-specific PCR products from B. pertussis and B. holmesii isolates revealed sequence homology. Restriction fragment length polymorphism demonstrated a low copy number of IS481-like sequences in B. holmesii. These results, and cultu
American Society for Microbiology.
-
28. Bordetella pertussis and Bordetella parapertussis: two immunologically distinct species.
Bordetella pertussis and Bordetella parapertussis are closely related species. Both are responsible for outbreaks of whooping cough in humans and produce similar virulence factors, with the exception of pertussis toxin, specific to B. pertussis. Current pertussis whole-cell vaccine will soon be replaced by acellular vaccines containing major adhesins (filame
-
29. Bordetella parapertussis and Bordetella bronchiseptica contain transcriptionally silent pertussis toxin genes.
Pertussis toxin, the major virulence factor of Bordetella pertussis, is not produced by the closely related species Bordetella parapertussis and Bordetella bronchiseptica. It is shown here that these two species possess but do not express the complete toxin operon. Nucleotide sequencing of an EcoRI fragment of 5 kilobases comprising the regions homologous to
-
30. Identification of a Bordetella pertussis regulatory factor required for transcription of the pertussis toxin operon in Escherichia coli.
Transcription of the pertussis toxin operon (ptx) is positively regulated in Bordetella pertussis by the bvgAS locus. However, a ptx-lacZ transcriptional fusion in Escherichia coli cannot be activated by bvgAS in trans. This suggests that an additional factor(s) is required for transcription of ptx. A gene encoding a Bvg accessory factor (Baf) was identified
-
31. CHEMICAL STUDIES ON CELLULAR COMPONENTS OF BORDETELLA PERTUSSIS III. : Isolation of Highly Potent Toxin from Bordetella Pertussis
Onoue, Kaoru (Kyushu University, Fukuoka, Japan), Masayasu Kitagawa, and Yuichi Yamamura. Chemical studies on cellular components of Bordetella pertussis. III. Isolation of highly potent toxin from Bordetella pertussis. J. Bacteriol. 86:648–655. 1963.—The thermolabile toxin of Bordetella pertussis was extracted at alkaline pH with 0.15 m saline from the
-
32. Evaluation of Real-Time PCR for Detection of and Discrimination between Bordetella pertussis, Bordetella parapertussis, and Bordetella holmesii for Clinical Diagnosis
PCR is increasingly being used as a diagnostic test for the detection of Bordetella pertussis and Bordetella parapertussis DNA, as it has improved sensitivity and specificity in comparison to conventional techniques. The assay described here uses the two insertion sequences IS481 and IS1001 for B. pertussis and B. parapertussis, respectively, with detection
American Society for Microbiology.
-
33. Serum Immunoglobulin G Antibody Responses to Bordetella pertussis Lipooligosaccharide and B. parapertussis Lipopolysaccharide in Children with Pertussis and Parapertussis
Serum immunoglobulin G (IgG) antibodies against the lipooligosaccharide (LOS) of Bordetella pertussis and the lipopolysaccharide (LPS) of Bordetella parapertussis were measured by enzyme-linked immunosorbent assay in paired sera from 40 children with pertussis and 14 with parapertussis. Wide differences in the individual responses were noted. Both anti-LOS a
American Society for Microbiology.
-
34. Monoclonal antibody-based sandwich enzyme-linked immunosorbent assay for detection of Bordetella pertussis filamentous hemagglutinin.
Hybrid cell lines producing monoclonal antibodies against Bordetella pertussis filamentous hemagglutinin (FHA) were established. The specificity of the antibodies was ascertained by enzyme-linked immunosorbent assay (ELISA), sandwich ELISA, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis followed by electroblotting. The monoclonal antibody-base
-
35. Agglutinating monoclonal antibodies that specifically recognize lipooligosaccharide A of Bordetella pertussis.
Monoclonal antibodies that specifically agglutinate strains of Bordetella pertussis having serotype 1 agglutinogen were uniquely reactive with the electrophoretically slow-migrating A form of lipooligosaccharide. These monoclonal antibodies should be useful for the structural analysis of B. pertussis lipooligosaccharide and for the establishment of a better-
-
36. Production of recombinant Bordetella pertussis serotype 2 fimbriae in Bordetella parapertussis and Bordetella bronchiseptica: utility of Escherichia coli gene expression signals.
Serotype-specific fimbriae of Bordetella pertussis are considered potential components of new-generation vaccines against whooping cough. Attempts to characterize fimbriae, and indeed other virulence determinants, produced by B. pertussis have been frustrated on one hand by low yields from B. pertussis itself and on the other by an inability to produce nativ