Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0149958 (complex partial seizures)
 2,563 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Starting with Neisseria meningitidis strain H44/76, a set of strains was constructed for use in production of a multivalent outer membrane vesicle vaccine. The aim was to remove unwanted outer membrane components and at the same time to improve the range of protection. This was accomplished through transformation with plasmid constructs made in Escherichia coli and their homologous recombination into the meningococcal chromosome. Deletion of the cps locus resulted in loss of expression of the group B capsular polysaccharide as well as the lacto-N-neotetraose structure in lipopolysaccharide. Deletion of the porB gene abolished expression of the class 3 outer membrane protein. Additional copies of the porA gene, encoding the immunodominant class 1 outer membrane protein, were inserted into one of the opa genes and into the rmpM gene encoding the class 4 outer membrane protein. This construction was done with three sets of porA alleles, resulting in three trivalent strains, each of which expressed a different combination of class 1 epitopes.
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PMID:Construction of Neisseria meningitidis strains carrying multiple chromosomal copies of the porA gene for use in the production of a multivalent outer membrane vesicle vaccine. 779 38

DjlA is a bitopic inner membrane protein, which belongs to the DnaJ co-chaperone family in Escherichia coli. Overproduction of DjlA leads to the synthesis of colanic acid, resulting in mucoidy, via the activation of the two-component regulatory system RcsC/B that controls the cps (capsular polysaccharide) operon. This induction requires both the co-chaperone activity of DjlA, in cooperation with DnaK and GrpE, and its unique transmembrane (TM) domain. Here, we show that the TM segment of DjlA acts as a dimerisation domain: when fused to the N-terminal DNA-binding domain of the lambda cI repressor protein, it can substitute for the native C-terminal dimerisation domain of cI, thus generating an active cI repressor. Replacing the TM domain of DjlA by other TM domains, with or without dimerising capacity, revealed that dimerisation is not sufficient for the induction of cps expression, indicating an additional sequence- or structurally specific role for the TM domain. Finally, the conserved glycines present in the TM domain of DjlA are essential for the induction of mucoidy, but not for dimerisation.
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PMID:The transmembrane domain of the DnaJ-like protein DjlA is a dimerisation domain. 1265 2