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)

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 archetypal two-component signal transduction systems include a sensor histidine kinase and a response regulator, which consists of a receiver CheY-like domain and a DNA-binding domain. Sequence analysis of the sensor kinases and response regulators encoded in complete bacterial and archaeal genomes revealed complex domain architectures for many of them and allowed the identification of several novel conserved domains, such as PAS, GAF, HAMP, GGDEF, EAL, and HD-GYP. All of these domains are widely represented in bacteria, including 19 copies of the GGDEF domain and 17 copies of the EAL domain encoded in the Escherichia coli genome. In contrast, these novel signaling domains are much less abundant in bacterial parasites and in archaea, with none at all found in some archaeal species. This skewed phyletic distribution suggests that the newly discovered complexity of signal transduction systems emerged early in the evolution of bacteria, with subsequent massive loss in parasites and some horizontal dissemination among archaea. Only a few proteins containing these domains have been studied experimentally, and their exact biochemical functions remain obscure; they may include transformations of novel signal molecules, such as the recently identified cyclic diguanylate. Recent experimental data provide the first direct evidence of the participation of these domains in signal transduction pathways, including regulation of virulence genes and extracellular enzyme production in the human pathogens Bordetella pertussis and Borrelia burgdorferi and the plant pathogen Xanthomonas campestris. Gene-neighborhood analysis of these new domains suggests their participation in a variety of processes, from mercury and phage resistance to maintenance of virulence plasmids. It appears that the real picture of the complexity of phosphorelay signal transduction in prokaryotes is only beginning to unfold.
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PMID:Novel domains of the prokaryotic two-component signal transduction systems. 1155 34

The purified soluble forms of the histidine kinases BvgS and EvgS of Bordetella pertussis and Escherichia coli, respectively, are shown to be responsive to oxidized ubiquinone-0 (Q-0) in vitro. The oxidized ubiquinone is a strong inhibitor of kinase activity of both enzymes with half maximal inhibition occurring at 11 microm (BvgS) and 4 microm (EvgS). Reduced Q-0 has no effect on the histidine kinases. Kinase activity can reversibly be switched off and on by changing the oxidation status of the quinone. This inhibitory effect is due to a decrease of the kinase activity of BvgS rather than an increase of intrinsic phosphatase activities. Other electron carriers such as menadione (MK-3), NAD or FAD did not have a significant effect on the kinase activities of BvgS and EvgS. Nicotinic acid and sulfate ions, known to inhibit the histidine kinases in vivo, did not affect the purified truncated sensor proteins lacking their periplasmic domains in vitro. Mutations introduced by site-directed mutagenesis into the putative PAS domain of BvgS caused a weak decrease of quinone-dependent inhibition of autophosphorylation. These data suggest that BvgS and EvgS are connected with the oxidation status of the cell via the link to the ubiquinone pool.
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PMID:The unorthodox histidine kinases BvgS and EvgS are responsive to the oxidation status of a quinone electron carrier. 1213 87