Results 31 to 40 of about 29,628 (214)

Lectinlike properties of pertussis toxin [PDF]

open access: yesInfection and Immunity, 1989
We have examined the lectinlike properties of pertussis toxin by binding-inhibition assays and affinity chromatography of goose erythrocyte membranes. Although pertussis toxin and wheat germ agglutinin apparently recognize similar sugar sequences on glycoproteins, the binding activities of the two lectins are not identical.
G J, Tyrrell   +5 more
openaire   +2 more sources

Bordetella pertussis Strains with Increased Toxin Production Associated with Pertussis Resurgence

open access: yesEmerging Infectious Diseases, 2009
Before childhood vaccination was introduced in the 1940s, pertussis was a major cause of infant death worldwide. Widespread vaccination of children succeeded in reducing illness and death.
Frits R. Mooi   +10 more
doaj   +1 more source

Lymphocyte receptors for pertussis toxin [PDF]

open access: yesInfection and Immunity, 1990
We have investigated human T-lymphocyte receptors for pertussis toxin by affinity isolation and photoaffinity labeling procedures. T lymphocytes were obtained from peripheral human blood, surface iodinated, and solubilized in Triton X-100. The iodinated mixture was then passed through pertussis toxin-agarose, and the fractions were analyzed by sodium ...
C G, Clark, G D, Armstrong
openaire   +2 more sources

Analysis of Bordetella pertussis pertactin and pertussis toxin types from Queensland, Australia, 1999–2003

open access: yesBMC Infectious Diseases, 2006
Background In Australia two acellular Bordetella pertussis vaccines have replaced the use of a whole cell vaccine. Both of the licensed acellular vaccines contain the following three components; pertussis toxoid, pertussis filamentous haemagglutinin and ...
Slack Andrew T, Byrne Shane
doaj   +1 more source

MODERNIZATION OF GENEOTIPING OF STRAINS B. PERTUSSIS

open access: yesДетские инфекции (Москва), 2015
The new rapid molecular genotyping method was developed for studying the structure of ptxP promoter of pertussis toxin. Method is based on PCR-RFLP analysis, which allows studying the specific restriction profiles of the B.
G. A. Ivashinnikova   +4 more
doaj   +1 more source

Monoclonal antibody against pertussis toxin: effect on toxin activity and pertussis infections [PDF]

open access: yesInfection and Immunity, 1984
Antibody-producing hybridomas of myeloma SP2/O and spleen cells of BALB/c mouse immunized with pertussis toxoid and pertussis toxin were selected by the binding ability of the monoclonal antibody to the subunit protein of the toxin. Two monoclonal antibodies, 1B7 and 3F10, specific for a subunit which has no binding activity to haptoglobin and sheep ...
H, Sato, A, Ito, J, Chiba, Y, Sato
openaire   +2 more sources

Experimental priming of encephalitogenic Th1/Th17 cells requires pertussis toxin-driven IL-1β production by myeloid cells

open access: yesNature Communications, 2016
Pertussis toxin enhances the induction of autoreactive T cells in mouse models of autoimmunity. Here the authors show that stimulation of IL-1β production in myeloid cells by pertussis toxin is necessary to prime pathogenic Th1/Th17 cells in experimental
Francesca Ronchi   +7 more
doaj   +1 more source

Loss of multi-epitope specificity in memory CD4(+) T cell responses to B. pertussis with age. [PDF]

open access: yesPLoS ONE, 2013
Pertussis is still occurring in highly vaccinated populations, affecting individuals of all ages. Long-lived Th1 CD4(+) T cells are essential for protective immunity against pertussis.
Wanda G H Han   +8 more
doaj   +1 more source

Membrane Localization of the S1 Subunit of Pertussis Toxin in Bordetella pertussis and Implications for Pertussis Toxin Secretion [PDF]

open access: greenInfection and Immunity, 2002
ABSTRACT Pertussis toxin is secreted from Bordetella pertussis with the assistance of the Ptl transport system, a member of the type IV family of macromolecular transporters. The S1 subunit and the B oligomer combine to form the holotoxin prior to export from the bacterial cell, although the site of ...
Karen M. Farizo   +3 more
openalex   +3 more sources

Engineered ETS1‐Nanoconjugate Restores Immune Homeostasis through Dual Immune‐Vascular Modulation in Relapsing and Progressive Multiple Sclerosis

open access: yesAdvanced Healthcare Materials, EarlyView.
The biomimetic nanoplatform IMNP (ETS1 pDNA/PBAE@ITP‐MM) undergoes targeted disassembly at inflammatory vascular sites to release the ETS1 plasmid (pETS1). This release initiates a cascade of effects that inhibit pathogenic pathways and support immune homeostasis. (Abbreviations: EndMT, endothelial‐to‐mesenchymal transition; EC, endothelial cell; TC, T
Feng Zhang   +13 more
wiley   +1 more source

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