Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0231530 (twitching)
 2,043 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Nine strains of Rochalimaea spp. that were isolated from patients over a period of 4.5 years were characterized for their enzyme activities, cellular fatty acid compositions, and DNA interrelatedness among Rochalimaea spp., Bartonella bacilliformis, and Afipia felis (cat scratch disease bacillus). All except one isolate, which was Rochalimaea quintana, were determined to belong to a newly proposed species, Rochalimaea henselae sp. nov. After recovery from clinical material, colonies required 5 to 15 days of incubation to become apparent. Cells were small, gram-negative, curved bacilli and displayed twitching motility. Enzyme specificities for amino acid and carbohydrate substrates showed that R. henselae could be distinguished from Rochalimaea vinsonii by L-arginyl-L-arginine and L-lysyl-L-alanine peptidases, but not all strains could be distinguished from R. quintana on the basis of peptidases or carbohydrate utilization. R. henselae also closely resembled R. quintana in cellular fatty acid composition, with both consisting mainly of C18:1, C18:0, and C16:0 fatty acids. However, the strains of R. henselae all contained C18:0 in amounts averaging greater than or equal to 22%, in contrast to R. quintana, which contained this cellular fatty acid in amounts averaging 16 and 18%. DNA hybridization confirmed the identification of one clinical isolate as R. quintana and showed a close interrelatedness (92 to 100%) among the other strains. Under optimal conditions for DNA reassociation, R. henselae showed approximately 70% relatedness to R. quintana and approximately 60% relatedness to R. vinsonii. Relatedness with DNA from B. baciliformis was 43%. R. henselae was unrelated to A. felis. R. henselae is the proposed species of a newly recognized member of the family Rickettsiaceae, which is a pathogen that may be encountered in immunocompromised or immunocompetent patients. Prolonged fever with bacteremia or vascular proliferative lesions are clinical manifestations of the agent.
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PMID:Rochalimaea henselae sp. nov., a cause of septicemia, bacillary angiomatosis, and parenchymal bacillary peliosis. 153 92

Understanding the structural biology of type IV pili, fibres responsible for the virulent attachment and motility of numerous bacterial pathogens, requires a detailed understanding of the three-dimensional structure and chemistry of the constituent pilin subunit. X-ray crystallographic refinement of Neisseria gonorrhoeae pilin against diffraction data to 2.6 A resolution, coupled with mass spectrometry of peptide fragments, reveals phosphoserine at residue 68. Phosphoserine is exposed on the surface of the modelled type IV pilus at the interface of neighbouring pilin molecules. The site-specific mutation of serine 68 to alanine showed that the loss of the phosphorylation alters the morphology of fibres examined by electron microscopy without a notable effect on adhesion, transformation, piliation or twitching motility. The structural and chemical characterization of protein phosphoserine in type IV pilin subunits is an important indication that this modification, key to numerous regulatory aspects of eukaryotic cell biology, exists in the virulence factor proteins of bacterial pathogens. These O-linked phosphate modifications, unusual in prokaryotes, thus merit study for possible roles in pilus biogenesis and modulation of pilin chemistry for optimal in vivo function.
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PMID:Crystallographic structure reveals phosphorylated pilin from Neisseria: phosphoserine sites modify type IV pilus surface chemistry and fibre morphology. 1004 19

Pseudomonas aeruginosa PAO1 produces the biodetergent rhamnolipid and secretes it into the extracellular environment. The role of rhamnolipids in the life cycle and pathogenicity of P. aeruginosa has not been completely understood, but they are known to affect outer membrane composition, cell motility, and biofilm formation. This report is focused on the influence of the outer membrane-bound esterase EstA of P. aeruginosa PAO1 on rhamnolipid production. EstA is an autotransporter protein which exposes its catalytically active esterase domain on the cell surface. Here we report that the overexpression of EstA in the wild-type background of P. aeruginosa PAO1 results in an increased production of rhamnolipids whereas an estA deletion mutant produced only marginal amounts of rhamnolipids. Also the known rhamnolipid-dependent cellular motility and biofilm formation were affected. Although only a dependence of swarming motility on rhamnolipids has been known so far, the other kinds of motility displayed by P. aeruginosa PAO1, swimming and twitching, were also affected by an estA mutation. In order to demonstrate that EstA enzyme activity is responsible for these effects, inactive variant EstA* was constructed by replacement of the active serine by alanine. None of the mutant phenotypes could be complemented by expression of EstA*, demonstrating that the phenotypes affected by the estA mutation depend on the enzymatically active protein.
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PMID:The autotransporter esterase EstA of Pseudomonas aeruginosa is required for rhamnolipid production, cell motility, and biofilm formation. 1763 36

PilA, the major pilin subunit of Pseudomonas aeruginosa type IV pili (T4P), is a principal structural component. PilA has a conserved C-terminal disulfide-bonded loop (DSL) that has been implicated as the pilus adhesinotope. Structural studies have suggested that DSL is involved in intersubunit interactions within the pilus fiber. PilA mutants with single-residue substitutions, insertions, or deletions in the DSL were tested for pilin stability, pilus assembly, and T4P function. Mutation of either Cys residue of the DSL resulted in pilins that were unable to assemble into fibers. Ala replacements of the intervening residues had a range of effects on assembly or function, as measured by changes in surface pilus expression and twitching motility. Modification of the C-terminal P-X-X-C type II beta-turn motif, which is one of the few highly conserved features in pilins across various species, caused profound defects in assembly and twitching motility. Expression of pilins with suspected assembly defects in a pilA pilT double mutant unable to retract T4P allowed us to verify which subunits were physically unable to assemble. Use of two different PilA antibodies showed that the DSL may be an immunodominant epitope in intact pili compared with pilin monomers. Sequence diversity of the type IVa pilins likely reflects an evolutionary compromise between retention of function and antigenic variation. The consequences of DSL sequence changes should be evaluated in the intact protein since it is technically feasible to generate DSL-mimetic peptides with mutations that will not appear in the natural repertoire due to their deleterious effects on assembly.
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PMID:Single-residue changes in the C-terminal disulfide-bonded loop of the Pseudomonas aeruginosa type IV pilin influence pilus assembly and twitching motility. 1971 95

Pseudomonas aeruginosa coordinates the secretion of virulence factors through quorum sensing. Quorum sensing inhibitors can attenuate the pathogenesis of bacteria and help the immune system to eradicate them without targeting the bacterial growth. This study aimed to explore the anti-quorum sensing and anti-virulence activities of sitagliptin against P. aeruginosa PAO1 strain. Sub-inhibitory concentration of sitagliptin significantly inhibited the virulence factors pyocyanin, hemolysin, protease and elastase in addition to blocking swimming, swarming and twitching motilities and biofilm formation. In silico analysis showed that sitagliptin interacted with LasR receptors by hydrogen bonding and hydrophobic interaction, mainly with the amino acids leucine present at positions 40 and 125, tyrosine at position 56, serine at position 129, tryptophan at position 60, alanine at position 50 and phenyl alanine at position 101. qRT-PCR confirmed the anti-quorum sensing activity by reducing the expression level of QS genes lasI, lasR, rhlI, rhlR, pqsA and pqsR. In conclusion, sitagliptin is a novel anti-quorum sensing agent that can be used for treating P. aeruginosa infections.
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PMID:Curtailing Quorum Sensing in Pseudomonas aeruginosa by Sitagliptin. 3202 Apr 64