Results 161 to 170 of about 4,144,807 (197)

Agglutination ofBordetellaspecies by lectins [PDF]

FEMS Microbiology Letters, 1992
Phase I cells of Bordetella pertussis but not those of B. parapertussis, B. bronchiseptica or B. avium were agglutinated by Limulus polyphemus lectin. Most strains of B. pertussis but not those of the other species were also agglutinated by Helix pomatia lectin. In precipitation reactions between lectins and purified Bordetella lipopolysaccharide (LPS)
M J, Corbel, A M, Abraham
exaly   +4 more sources

The classical Bordetella species and MALDI-TOF technology: a brief experience

Journal of Medical Microbiology, 2018
Fil: Zintgraff, Jonathan. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Enfermedades Infecciosas. Departamento de Bacteriología. Servicio de Bacteriología Clínica; Argentina.Fil: Irazu, Lucía. ANLIS Dr.C.G.Malbrán.
Jonathan Zintgraff
exaly   +2 more sources

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Bordetella Species Other than Bordetella pertussis

Clinical Microbiology Newsletter, 2015
Most clinicians and microbiologists are familiar with Bordetella pertussis, its associated clinical syndromes and treatment with antimicrobials, and both biochemical and molecular methods for identification. Many of the other Bordetella species are much less well known, though they do cause clinical disease in humans.
Jocelyn A. Srigley, David M. Goldfarb, Jeffrey M. Pernica   +2 more
openaire   +1 more source

All species of the genus bordetella contain genes for pertussis toxin of bordetella pertussis

Zentralblatt für Bakteriologie, Mikrobiologie und Hygiene. Series A: Medical Microbiology, Infectious Diseases, Virology, Parasitology, 1988
A molecular probe for the PT-operon of B. pertussis hybridized with 4.7 Kb EcoRI-fragments of chromosomal DNAs of B. pertussis strain 475 phase I, phase IV, B. parapertussis strains 504 and 17903, B. bronchiseptica strain 214, B. parapertussis strain 17903-convertant of B. pertussis phage 134 but not with phage 134 DNA under stringent conditions of DNA-
M N, Rozinov, A A, Dain, Y L, Shumakov, I A, Lapaeva, T A, Holzmayer   +4 more
openaire   +2 more sources

Environmental regulation of virulence factors in Bordetella species

BioEssays, 1993
AbstractMany bacteria respond in a coordinate manner to environmental changes. External stimuli, sensed by receptors, are transduced to regulatory proteins which participate in well defined pathways of gene expression by varying their structure and mode of action. The network of environmental signal transduction is responsible for a fine and continuous
Scarlato V., Arico B., Domenighini M., Rappuoli R.   +3 more
openaire   +3 more sources

Deoxyribonucleotide Sequence Relationships Among Bordetella Species † [PDF]

International Journal of Systematic and Evolutionary Microbiology, 1981
Deoxyribonucleotide sequence relationships among currently recognized Bordetella species (Bordetella pertussis, Bordetella parapertussis, and Bordetella bronchiseptica) were examined by deoxyribonucleic acid (DNA) hybridization involving the hydroxyapatite batch procedures of Brenner and co-workers.
Walter J Dobrogosz, C R Manclark, Charles R Manclark   +2 more
exaly   +2 more sources

Expression of Pertussis Toxin Correlates with Pathogenesis in Bordetella Species

Journal of Infectious Diseases, 1989
Pertussis toxin is a principal determinant of virulence produced by Bordetella pertussis in the disease whooping cough and is the primary toxinogenic component of the pertussis vaccine. This toxin is not produced by the closely related species Bordetella parapertussis. Toxinogenic strains of B.
D, Monack, J J, Munoz, M G, Peacock, W J, Black, S, Falkow   +4 more
openaire   +2 more sources

Multiple species and isoforms of Bordetella pertussis toxin substrates

Biochemical and Biophysical Research Communications, 1988
In purified G proteins from bovine brain cortex the ADP-ribosylated substrates of Bordetella pertussis toxin (PT) can be resolved in three polypeptides by polyacrylamide gel electrophoresis: a 39 kDa major substrate, corresponding to Go alpha and two others (40 and 41 kDa) assigned to alpha subunits of Gi-like proteins.
P, Brabet, C, Pantaloni, B, Rouot, M, Toutant, A, Garcia-Sainz, J, Bockaert, V, Homburger   +6 more
openaire   +2 more sources

Genetic Regulation of Airway Colonization by Bordetella Species

American Journal of Respiratory and Critical Care Medicine, 1996
Abstract Bordetella species are respiratory pathogens that infect humans and other animals. A majority of the virulence factors expressed by these bacteria are regulated by a master control locus, BvgAS, a member of the two-component family of signal transduction systems.
M H, Yuk, P A, Cotter, J F, Miller
openaire   +2 more sources

Fimbriae and determination of host species specificity of Bordetella bronchiseptica

Journal of Clinical Microbiology, 1993
A monoclonal antibody, designated CF8 and prepared against fimbrial protein enrichments of Bordetella bronchiseptica 110H, was determined by immunogold electron microscopy to bind to some but not all fimbrial filaments on intact bacterial cells. Comparison of the reactivity of this antibody with that of monoclonal antibody BPF2, which is specific for ...
E H, Burns, J M, Norman, M D, Hatcher, D A, Bemis   +3 more
openaire   +2 more sources