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)

Maternal antibody to an outer membrane 68-kilodalton (kDa) protein of Bordetella bronchiseptica was shown to be protective in experiments on specific-pathogen-free piglets. After challenge with B. bronchiseptica, 100% (n = 19) control piglets from nonimmunized sows developed pneumonia, coughing, and sneezing, and 74% of the animals developed severe atrophic rhinitis. In 12 piglets from a sow immunized with 68-kDa protein, pneumonia occurred only in 34% of offspring, coughing was reduced, the duration of coughing bouts was shortened, and severe atrophic rhinitis occurred in one animal only (8%). The difference in the occurrence of atrophic rhinitis and of pneumonia in immunized and nonimmunized offspring was statistically significant (P less than 0.05). Sera of protected piglets had high titers (enzyme-linked immunosorbent assay) of antibodies that showed a high specificity for the 68-kDa protein isolated from B. bronchiseptica, whereas their reactivity with an analogous 69-kDa protein isolated from Bordetella pertussis was low or absent. The 68-kDa protein of B. bronchiseptica appeared to be the major protective antigen in B. bronchiseptica infection; however, isolated protein alone did not induce such a solid protection, as observed in a previous study after the application of an effective whole cell vaccine.
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PMID:Identification of a 68-kilodalton outer membrane protein as the major protective antigen of Bordetella bronchiseptica by using specific-pathogen-free piglets. 213 11

Adhesion to mucosal cells is an important virulence attribute of bacterial pathogens colonizing these sites. Bacteria of the upper respiratory system, such as members of the genus Bordetella, have well-defined adhesins. The main adhesin of B. pertussis is the filamentous hemagglutinin which can be used by other bacteria for attachment. The main adhesin of B. bronchiseptica is the bovine erythrocyte hemagglutinin. In both Bordetella species the presence of fimbriae does not appear critical to adhesion. In contrast, atrophic rhinitis (AR)-producing strains of Pasteurella multocida colonize poorly the pig's nasal mucosa. We performed an in vitro trial using newborn pigs' turbinate explants and showed that two toxigenic strains (serotype D fimbria + and serotype A fimbria -) were adherent when observed by scanning electron microscopy (SEM). Intranasal inoculation of both six week old and newborn SPF pigs with various strains of P. multocida also resulted in colonization. Adhesion was best achieved by toxigenic strains, regardless of possession of fimbria, hemagglutinin or capsular serotype. Colonization was more abundant and constant in tonsils. Nasal colonization was sporadic and sparse. Colonization of trachea and lung was only observed with serotype A strains. The results showed that toxigenic P. multocida can colonize the upper respiratory tract, especially the tonsils, of pigs.
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PMID:Bacterial adhesion to mucosal surfaces with special reference to Pasteurella multocida isolates from atrophic rhinitis. 214 99

A method was developed which is suitable for the isolation of substantial quantities of outer membrane proteins of Bordetella species in a water-soluble form. The extracted material may then be further fractionated in the absence of detergents by ion-exchange chromatography and preparative flat-bed isoelectrofocusing. These procedures facilitated the isolation of one of the proteins, of molecular weight 68,000, for which the antibody titer correlated with the degree of protection against nasal changes induced in specific-pathogen-free piglets by Bordetella bronchiseptica infection (P. Novotny, M. Kobisch, K. Cownley, A. P. Chubb, and J. A. Montaraz, Infect. Immun. 50:190-198). This protein, which banded between 7.0 and 7.6 pH in preparative isoelectrofocusing, may be further purified with a monoclonal immunosorbent. Immunopurified protein showed adenylate cyclase activity. The enzymatic activity was found to be unstable during processing; i.e., although the crude extract showed up to 150 nmol of cyclic AMP per mg/min, the immunopurified protein showed a maximum of only 200 nmol of cyclic AMP per mg/min. Two strains of B. bronchiseptica, isolated from herds of healthy pigs showing no signs of atrophic rhinitis, did not produce the 68,000-molecular-weight protein and were negative for adenylate cyclase. However, it is not known whether the 68,000-molecular-weight protein is a component of adenylate cyclase or whether it is an unrelated protein associated with this enzyme in some unknown way. Adenylate cyclase activity from culture supernatants of B. bronchiseptica, B. pertussis, and B. parapertussis can be absorbed equally to the same monoclonal immunosorbent.
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PMID:Adenylate cyclase activity of a 68,000-molecular-weight protein isolated from the outer membrane of Bordetella bronchiseptica. 404 33

Bacterial protein toxins are powerful tools for elucidating signaling mechanisms in eukaryotic cells. A number of bacterial protein toxins, e.g. cholera toxin, pertussis toxin (PTx), or Pasteurella multocida toxin (PMT), target heterotrimeric G proteins and have been used to stimulate or block specific signaling pathways or to demonstrate the contribution of their target proteins in cellular effects. PMT is a major virulence factor of P. multocida causing pasteurellosis in man and animals and is responsible for atrophic rhinitis in pigs. PMT modulates various signaling pathways, including phospholipase Cbeta and RhoA, by acting on the heterotrimeric G proteins Galpha(q) and Galpha(12/13), respectively. Here we report that PMT is a powerful activator of G(i) protein. We show that PMT decreases basal isoproterenol and forskolin-stimulated cAMP accumulation in intact Swiss 3T3 cells, inhibits adenylyl cyclase activity in cell membrane preparations, and enhances the inhibition of cAMP accumulation caused by lysophosphatidic acid via endothelial differentiation gene receptors. PMT-mediated inhibition of cAMP production is independent of toxin activation of Galpha(q) and/or Galpha(12/13). Although the effects of PMT are not inhibited by PTx, PMT blocks PTx-catalyzed ADP-ribosylation of G(i). PMT also inhibits steady-state GTPase activity and GTP binding of G(i) in Swiss 3T3 cell membranes stimulated by lysophosphatidic acid. The data indicate that PMT is a novel activator of G(i), modulating its GTPase activity and converting it into a PTx-insensitive state.
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PMID:Activation of Galpha (i) and subsequent uncoupling of receptor-Galpha(i) signaling by Pasteurella multocida toxin. 1858 41

Pathogenic Bordetella bacteria release a neurotropic dermonecrotic toxin (DNT) that is endocytosed into animal cells and permanently activates the Rho family GTPases by polyamination or deamidation of the glutamine residues in their switch II regions (e.g., Gln63 of RhoA). DNT was found to enable high level colonization of the nasal cavity of pigs by B. bronchiseptica and the capacity of DNT to inhibit differentiation of nasal turbinate bone osteoblasts causes atrophic rhinitis in infected pigs. However, it remains unknown whether DNT plays any role also in virulence of the human pathogen B. pertussis and in pathogenesis of the whooping cough disease. We report a procedure for purification of large amounts of LPS-free recombinant DNT that exhibits a high biological activity on cells expressing the DNT receptors Cav3.1 and Cav3.2. Electron microscopy and single particle image analysis of negatively stained preparations revealed that the DNT molecule adopts a V-shaped structure with well-resolved protein domains. These results open the way to structure-function studies on DNT and its interactions with airway epithelial layers.
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PMID:Production of Highly Active Recombinant Dermonecrotic Toxin of Bordetella Pertussis. 3294 77