Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0043167 (pertussis)
 19,595 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Two distinct monoclonal antibodies, one to pertussis toxin subunit S2, called 9G8, and another to subunits S2 and S3, called 11E6, were generated from the hybridomas of myeloma SP2/0 and spleen cells of BALB/c mice immunized mainly with the subunit S234 complex. Binding ability of 9G8 and 11E6 to the subunits was confirmed by the enzyme-linked immunosorbent assay and immunoblotting analysis. Generation of 11E6 bound to both S2 and S3 might mean that there is common antigenicity between S2 and S3. Neutralizing activities of 9G8 and 11E6 on various biological activities of pertussis toxin, including ADP-ribosyltransferase and leukocytosis-promoting, islet-activating, permeability-increasing. Chinese hamster ovary (CHO) cell-clustering, and hemagglutinating activities, were compared with those of anti-S1 monoclonal antibodies 1B7 and 3F10, which were isolated and characterized in a previous study (H. Sato, A. Ito, J. Chiba, and Y. Sato, Infect. Immun. 46:422-428, 1984). 1B7 and 3F10 neutralized ADP-ribosyltransferase activity of pertussis toxin or S1, but 9G8 and 11E6 did not. 1B7 showed very potent neutralization against leukocytosis-promoting, islet-activating, permeability-increasing, and CHO cell-clustering activities of pertussis toxin, but 3F10 did not, although anti-ADP-ribosyltransferase activities of both antibodies were identical. 11E6 neutralized leukocytosis-promoting, islet-activating, CHO cell-clustering, and hemagglutinating activities but not permeability-increasing activity. 9G8 showed slight neutralization of leukocytosis-promoting and CHO cell-clustering activities. Specific activities of 1B7 and 11E6 in each neutralization test were higher than or almost comparable to those of polyclonal antibodies to pertussis toxin. The neutralizing mechanism of 1B7 and 11E6 in leukocytosis-promoting activity was compared. 11E6 seemed to interfere with the binding of pertussis toxin to receptors on mouse spleen cells.
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PMID:Effect of monoclonal antibody to pertussis toxin on toxin activity. 243 60

The epitope specificities of 13 hybridomas secreting monoclonal antibodies (MAbs) specific for pertussis toxin (PT) is described. Hybridoma lines were derived by the fusion of spleen cells from mice immunized with native PT, Formalin-detoxified PT, or isolated PT subunits (S1 to S5) with the myeloma line X63-Ag8.653. Five MAbs showed a toxin-neutralizing ability, which was demonstrated by use of a Chinese hamster ovary cell assay system and by a NAD glycohydrolase assay. All five toxin-neutralizing MAbs demonstrated high specificities for and reactivities with native PT but were unable to bind to denatured PT. One MAb was able to neutralize the enzymatic activity of PT. The other four neutralizing MAbs inhibited the binding of PT or PT subunits to the surface of Chinese hamster ovary cells, as shown by an immunofluorescence assay. All neutralizing MAbs reacted with purified S2-S4 or S3-S4 dimers but not with S4 alone. Three MAbs which recognized a common epitope shared by S2 and S3 (which are about 70% homologous at the DNA level) and one MAb which recognized S4 were not neutralizing. Isolated S2-S4 and S3-S4 dimers bound to Chinese hamster ovary cells. These results indicate that the majority of critical epitopes which elicit neutralizing antibody are conformation dependent.
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PMID:Monoclonal antibodies that define neutralizing epitopes of pertussis toxin: conformational dependence and epitope mapping. 247

Monoclonal IgA paraproteins of subclasses 1 and 2, isolated from the sera of myeloma patients, were incubated for 4, 24, 48 and 72 hours with B. pertussis, B. parapertussis, B. bronchiseptica cultures, as well as Haemophilus influenzae strain. The fragmentation of IgA was studied by immunielectrophoresis with antisera to alpha-chain, to Fab alpha + Fc alpha, to Fab alpha and with antisera to light chains corresponding to the type of paraprotein. B. pertussis and B. parapertussis were found to have subclass-unspecific IgA protease which splitted off a cathode fragment, similar to Fab-fragment and, probably, corresponding to the variable domain of alpha-chain (Fv), after 48-hour incubation. Similar IgA protease was detected in H. influenzae, found to have classical IgA1 protease as well. All Bordetella species under study splitted off anode components from IgA paraproteins of both subclasses. These components, containing the determinants of heavy and light IgA chains, were either IgA - alpha I-antitrypsin complexes or some IgA fragments with high electrophoretic motility. None of the strains under study splitted monoclonal IgG.
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PMID:[IgA protease activity of microbes in the genus Bordetella]. 286 69

Antibodies to lipid A were raised in mice immunized with non-hydrolysed Bordetella pertussis microorganisms, coated with lipid A isolated from the same bacteria. Anti-lipid A activity of immune sera was measured by radioimmunoassay. Four hybrid cell lines that secrete antibodies directed against the hydrophobic region of B. pertussis lipopolysaccharide were produced by cell fusion between myeloma cells and spleen cells from immunized C3H/He-PAS mice. Differences were observed in the potency of the isolated monoclonal antibodies to inhibit B cell proliferation induced by lipopolysaccharide (LPS) or by lipid A, suggesting a selective recognition of effector sites present on the hydrophobic region of LPS.
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PMID:Inhibition of lipopolysaccharide mitogenicity with characterized anti-lipid A monoclonal antibodies. 286 28

The ability of injected rat IgE myeloma protein IR162 to inhibit passive and active cutaneous anaphylaxis in Lewis rats was investigated. IgE injected i.p. 24 hr before the sensitization with IgE anti-ovalbumin (OVA) completely inhibited both IgE- and IgG2a-induced passive cutaneous anaphylactic (PCA) reactions at a dose (2.5 mg/100 g body weight) that resulted in peak serum concentrations of 150 micrograms IgE IR162/ml. Peak IgE IR162 serum concentrations of 20 to 60 micrograms/ml inhibited the PCA reaction in approximately 50% of the rats. Intracutaneous injection of a mixture of myeloma IgE and anti-OVA IgE in a ratio of 100:1 or more also inhibited the PCA reaction. In contrast, the PCA reaction was not inhibited by seven daily doses of IgE beginning 24 hr after passive sensitization. Likewise, the cutaneous anaphylactic reaction elicited in rats 14 days after immunization with OVA and Bordetella pertussis was not prevented by daily injections of myeloma IgE despite a 1000- to 3000-fold excess of the myeloma IgE to anti-OVA IgE serum concentration. The data demonstrate that parenteral administration of myeloma IgE inhibits the PCA reaction only when given before passive sensitization and does not prevent cutaneous anaphylaxis in actively immunized rats. Because myeloma IgE failed to inhibit anaphylactic reactions in actively immunized rats, it is questionable whether administering human IgE-derived synthetic peptides or recombinant DNA-produced IgE fragments will be able to prevent allergic diseases by blocking the IgE Fc receptors on mast cells.
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PMID:Effect of myeloma IgE injections on passive and active cutaneous anaphylaxis in rats. 348 88

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 erythrocytes, named S1, and one antibody, 1H2, for a subunit related to the binding activity of the pertussis toxin molecule to haptoglobin or sheep erythrocytes, named S4, were examined for mouse protective activity against pertussis infection. Antibody 1B7 not only neutralized leukocytosis-promoting and islet-activating activities of the toxin but also protected mice against intracerebral and aerosol challenge with Bordetella pertussis. The antibody, furthermore, showed therapeutic effects on mice showing severe clinical signs with pertussis infection. The other two antibodies, 3F10 and 1H2, showed neither neutralizing nor protecting activity, nor significant synergistic effects on antibody 1B7.
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PMID:Monoclonal antibody against pertussis toxin: effect on toxin activity and pertussis infections. 609 51

Monoclonal antibodies to Bordetella pertussis were produced by fusion of mouse myeloma cells and spleen cells of immunized mice. Cell lines were examined for specific antibody production against several crude antigen preparations and lipopolysaccharide. Cross reactivity of monoclonal antibodies was assessed by enzyme immunoassay using cell lysates prepared from Bordetella spp. and several other bacteria. Reactivity of monoclonal antibodies to cell surface components was determined by immunofluorescence microscopy. Monoclonal antibodies represent useful probes to study the antigenic profile and distribution of antigens among various species of Bordetella, as well as specific tools to study the structure and function of B. pertussis virulence factors.
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PMID:Isolation and characterization of monoclonal antibodies to Bordetella pertussis. 609 81

Sufficiently purified IgA, subclass I, has been isolated from the defibrinated plasma of a myeloma patient by chromatography on columns packed with DEAE-Sephadex A-50 or Sephadex G-200, and rabbit antiserum to this immunoglobulin has been obtained. These preparations have been used for detecting specific protease in Bordetella pertussis. The tested B. pertussis strains have been shown to induce, as revealed by immunoelectrophoretic methods, the proteolysis of human IgA, subclass I.
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PMID:[Isolation and characteristics of IgA1 and its use for detecting bacterial IgA1 proteases]. 609 21

Histamine release from isolated rat mast cells from non-immunized and immunized Hooded Lister rats was induced by compound 48/80. The histamine release was decreased with a lower maximum at the optimal concentration of 48/80 when using cells from immunized rats compared to non-immunized control rats. The stimulation of IgE antibody production, after immunization using B. pertussis as an adjuvant was also accompanied by an elevation of total serum IgW. The 48/80 induced histamine release from Sprague Dawley mast cells was not inhibited by immunization. Non-antibody IgE showed a non-competitive inhibition of 48/80 induced histamine release when myeloma IgE was incubated with mast cells from both Hooded Lister and Sprague Dawley rats. The results indicate the existence of different receptors for IgE and 48/80.
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PMID:Effect of sensitization and non-antibody IgE on 48/80 induced histamine release from isolated rat mast cells. 615 31

A murine monoclonal antibody, MAHI 3 (immunoglobulin G2b), that is broadly reactive with Haemophilus influenzae lipopolysaccharides (LPSs) but nonreactive with all enterobacterial LPSs tested was generated by fusing mouse myeloma cells with spleen cells of BALB/c mice immunized with azide-killed H. influenzae RM.7004. MAHI 3 bound to all H. influenzae, all other human Haemophilus spp., all Bordetella pertussis and Bordetella parapertussis, and all Aeromonas spp. tested but not to any Neisseria or Moraxella catarrhalis strains, as determined by enzyme immunoassay, colony dot immunoblotting, and immunoblotting. In an inhibition enzyme immunoassay, MAHI 3 reacted with all 45 H. influenzae LPSs tested but not with the LPS from the rough mutant I69 Rd-/b+, which has only 3-deoxy-D-manno-octulosonic acid (P) [Kdo(P)] and lipid A. The antibody was not inhibited by H. influenzae lipid A or lipid-free polysaccharide isolated after mild acid hydrolysis. Only native LPSs show positive inhibitory activity, indicating that part of lipid A is involved in the binding of MAHI 3. From the results, it is indicated that the structural element recognized by MAHI 3 is Hep alpha 1-->2Hep alpha 1-->3Hep alpha 1-->Kdo together with part of lipid A, including the phosphate.
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PMID:The tetrasaccharide L-alpha-D-heptose1-->2-L-alpha-D-heptose1--> 3-L-alpha-D-heptose1-->(3-deoxy-D-manno-octulosonic acid) and phosphate in lipid A define the conserved epitope in Haemophilus lipopolysaccharides recognized by a monoclonal antibody. 754 87


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