Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0348321 (Haemophilus)
 15,372 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

This investigation was designed to characterize the immunoprotective antigen of ribosomal preparations from Haemophilus influenzae. The ribosomes that elicited 80 to 90% protection contained 25% protein and 75% ribonucleic acid but did not contain any detectable hexoses. The immunodiffusion and hemagglutination inhibition tests also failed to demonstrate that the capsular material (polyribose phosphate) was in ribosomal preparations. Treatment of ribosomes with ribonuclease degraded 78% ribonucleic acid but did not affect the immunogenicity of such preparations. The proteolytic enzymes reduced the immunogenicity of ribosomes corresponding to the amount of protein degraded. The protection elicited by ribosomal protein extracted with 2-chloroethanol was comparable to that induced by intact ribosomes. In contrast, the low levels of protection observed by immunization with phenol-extracted ribonucleic acid were dependent on the amounts of contaminating protein. Finally, immunogenicity of ribosomal ribonucleic acid and protein was abrogated by treatment with proteolytic enzymes. These results clearly indicate that the protein associated with Haemophilus ribosomes is the major immunoprotective antigen.
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PMID:Characterization of the immunoprotective antigen of ribosomal preparations from Haemophilus influenzae. 30 44

The in vitro activity of S-6123, a synthetic antimicrobial compound of the new oxazolidinone series, was compared with those of other orally administered agents against 328 clinical isolates. The compound was moderately active (MICs, 16 to 64 micrograms/ml) against 90% of staphylococci, nonenterococcal streptococci, and Haemophilus influenzae, including strains resistant to beta-lactam antibiotics. S-6123 was minimally active against enterococci and facultative gram-negative bacilli. Nevertheless, the compound had significant activity in a lethal rat Escherichia coli peritonitis model at serum concentrations of one-tenth the MIC against the infecting organism. The drug demonstrated only bacteriostatic activity against susceptible organisms. Studies to define the mechanism of antibacterial action revealed that S-6123 inhibited ribosomal protein synthesis without inhibiting DNA or RNA synthesis. This compound represents a new series of antibacterial agents not related to any other antibacterial compound of natural or synthetic origin.
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PMID:Mechanism of action and in vitro and in vivo activities of S-6123, a new oxazolidinone compound. 305 18

We have cloned the L4 ribosomal protein genes from Morganella morganii and Haemophilus influenza. The sequences of these genes were compared with published sequences for Escherichia coli, Yersinia pseudotuberculosis, and Bacillus stearothermophilus. All five of these L4 genes were expressed in E. coli and shown to function as repressors of both transcription and translation of the E. coli S10 operon. Possible implications for regulation of r-protein synthesis in species other E. coli are discussed.
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PMID:Regulation of the Escherichia coli S10 ribosomal protein operon by heterologous L4 ribosomal proteins. 872 27

In the human pathogen Staphylococcus aureus, many proteins involved in the infection process are preferentially produced during the stationary growth phase. Using a DNA probe corresponding to the Bacillus subtilis gene encoding the stationary-phase sigma factor SigB (sigmaB), we identified a gene in S. aureus with similarity to B. subtilis sigB. The sigB region was mapped on the SmaI I fragment of the S. aureus chromosome and contains a total of six open reading frames (orf1-6). The deduced amino acid sequences of orf2, orf3, orf4, and orf5 show 64, 67, 71, and 77% similarity to the B. subtilis proteins RsbU, RsbV, RsbW, and SigB, respectively, with SigB representing the sigma factor and the Rsb proteins representing regulators of sigma B. Furthermore, the relative position of the corresponding genes is conserved in B. subtilis, which strongly suggests that we identified the sigB operon of S. aureus, encoding an alternative sigma factor in this organism. The proposed gene products of the two remaining open reading frames show 48-62% similarity to the PemK, ChpAK, and ChpBK growth inhibitors of Escherichia coli (ORF1) and 61% similarity to the ribosomal protein S1 of Haemophilus influenzae (ORF6). Northern blot analysis of the sigB region in S. aureus revealed that four different transcripts are expressed under different conditions of growth phase and stress. These results indicate a complex transcriptional regulation that differs between S. aureus and B. subtilis.
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PMID:The alternative sigma factor sigmaB in Staphylococcus aureus: regulation of the sigB operon in response to growth phase and heat shock 904 55

LytB of Escherichia coli is an essential gene involved in penicillin tolerance and the stringent response. The lytB gene of Campylobacter jejuni was cloned and characterized. It could complement a temperature-sensitive E. coli lytB mutant. The C. jejuni lytB gene encodes a protein of 277 amino acids that has 34, 36 and 40% amino acid identity with the LytB proteins of E. coli, Haemophilus influenzae, and Synechocystis sp. PCC6803, respectively. The lytB gene is situated between the aroA gene and a gene that encodes ribosomal protein S1.
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PMID:Cloning and characterization of the lytB gene of Campylobacter jejuni. 941 46

We have cloned and sequenced the 5.2 kb EcoRI fragment that contained part of the S10 operon from Actinobacillus actinomycetemcomitans FDC Y4. The order of the ribosomal protein genes was identical to that of the S10 operon of Haemophilus influenzae and Escherichia coli. The deduced amino acid sequences of ribosomal proteins in this operon displayed significant homologies (65.3%-100%) to those of H. influenzae, E. coli, Yersinia enterocolitica and Yersinia pseudotuberculosis. Phylogenetic trees obtained for these ribosomal proteins were similar to that obtained for 16S rRNA.
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PMID:Cloning and sequencing of part of the S10 operon from Actinobacillus actinomycetemcomitans FDC Y4. 946 4

We have assigned codon-anticodon recognition patterns for the whole set of transfer RNAs of Haemophilus influenzae Rd, Methanococcus jannaschii, and Synechocystis sp. PCC6803 using sequence information derived from the complete genome sequence of these organisms and have tabulated them along with those previously reported for Escherichia coli, Mycoplasma genitalium, Mycoplasma pneumoniae, and Saccharomyces cerevisiae. Using the resulting codon-anticodon tables, the bias in codon usage of genes encoding the entire protein and ribosomal protein complement of each of the seven microbial genomes was analyzed. Then, the codon adaptation index (CAIrp) for each protein gene was calculated using the codon usage preference of the ribosomal protein genes of the corresponding organism. Of the seven genomes examined, six showed CAIrp scores that roughly coincided with the expected level of gene expression. The result demonstrates that CAIrp analysis may be useful for prediction of the expression level of unknown genes when all or at least considerable portions of the genome sequence are available.
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PMID:Codon-anticodon assignment and detection of codon usage trends in seven microbial genomes. 968 28

We investigated the regulation of the S10 ribosomal protein (r-protein) operon among members of the gamma subdivision of the proteobacteria, which includes Escherichia coli. In E. coli, this 11-gene operon is autogenously controlled by r-protein L4. This regulation requires specific determinants within the untranslated leader of the mRNA. Secondary structure analysis of the S10 leaders of five enterobacteria (Salmonella typhimurium, Citrobacter freundii, Yersinia enterocolitica, Serratia marcescens, and Morganella morganii) and two nonenteric members of the gamma subdivision (Haemophilus influenzae and Vibrio cholerae) shows that these foreign leaders share significant structural homology with the E. coli leader, particularly in the region which is critical for L4-mediated autogenous control in E. coli. Moreover, these heterologous leaders produce a regulatory response to L4 oversynthesis in E. coli. Our results suggest that an E. coli-like L4-mediated regulatory mechanism may operate in all of these species. However, the mechanism is not universally conserved among the gamma subdivision members, since at least one, Pseudomonas aeruginosa, does not contain the required S10 leader features, and its leader cannot provide the signals for regulation by L4 in E. coli. We speculate that L4-mediated autogenous control developed during the evolution of the gamma branch of proteobacteria.
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PMID:Phylogenetic analysis of L4-mediated autogenous control of the S10 ribosomal protein operon. 1049 27

Our approach in predicting gene expression levels relates to codon usage differences among gene classes. In prokaryotic genomes, genes that deviate strongly in codon usage from the average gene but are sufficiently similar in codon usage to ribosomal protein genes, to translation and transcription processing factors, and to chaperone-degradation proteins are predicted highly expressed (PHX). By these criteria, PHX genes in most prokaryotic genomes include those encoding ribosomal proteins, translation and transcription processing factors, and chaperone proteins and genes of principal energy metabolism. In particular, for the fast-growing species Escherichia coli, Vibrio cholerae, Bacillus subtilis, and Haemophilus influenzae, major glycolysis and tricarboxylic acid cycle genes are PHX. In Synechocystis, prime genes of photosynthesis are PHX, and in methanogens, PHX genes include those essential for methanogenesis. Overall, the three protein families-ribosomal proteins, protein synthesis factors, and chaperone complexes-are needed at many stages of the life cycle, and apparently bacteria have evolved codon usage to maintain appropriate growth, stability, and plasticity. New interpretations of the capacity of Deinococcus radiodurans for resistance to high doses of ionizing radiation is based on an excess of PHX chaperone-degradation genes and detoxification genes. Expression levels of selected classes of genes, including those for flagella, electron transport, detoxification, histidine kinases, and others, are analyzed. Flagellar PHX genes are conspicuous among spirochete genomes. PHX genes are positively correlated with strong Shine-Dalgarno signal sequences. Specific regulatory proteins, e.g., two-component sensor proteins, are rarely PHX. Genes involved in pathways for the synthesis of vitamins record low predicted expression levels. Several distinctive PHX genes of the available complete prokaryotic genomes are highlighted. Relationships of PHX genes with stoichiometry, multifunctionality, and operon structures are discussed. Our methodology may be used complementary to experimental expression analysis.
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PMID:Predicted highly expressed genes of diverse prokaryotic genomes. 1096 Jan 11

The complete genomic nucleotide sequence data of more than 10 unicellular organisms have become available. During the past years, we have been focusing our attention to the analysis of the structure and function of the ribosome and its protein components. By making use of the genomic sequence data, our work can now be extended to comparative analysis of the ribosomal components at the genomic level. Such analysis will contribute to our understanding of the structure-function relationship of the ribosome that is vital to the expression of genetic information. Bearing these in mind, the ribosomal protein genes of organisms whose genomic sequence data are available were analyzed, which included Aquifex aeolicus; Archaeoglobus fulgidus; Borrelia burgdorferi; Bacillus subtilis; Escherichia coli; Haemophilus influenzae; Helicobacter pylori; Methanococcus jannaschii; Mycoplasma genitalium; Mycoplasma pneumoniae; Synechosystis sp., and Saccharomyces cerevisiae. In addition, the amino acid sequence data of Bacillus stearothermophilus ribosomal proteins were used in the evolutionary evaluation. The results indicate that, in eubacteria including two species of Mycoplasma, the operon structure of ribosomal protein genes is well conserved, while their relative orientation and chromosomal location are diverged into several classes. The operon structure in M. jannaschii on the other hand is quite different from the eubacterial one and we noticed that its many genes show similarity to rat ribosomal protein genes. The degrees of sequence conservation differ from one ribosomal protein gene to another, but several genes encoding proteins that are considered to be of structural importance are conserved throughout the bacterial species including archaebacteria and further in S. cerevisiae.
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PMID:Genomic Analysis of the Genes Encoding Ribosomal Proteins in Eight Eubacterial Species and Saccharomyces cerevisiae. 1107 16


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