Life in mucus: sugar metabolism in Haemophilus influenzae

Macfadyen, Leah P.; Redfield, Rosemary J.

doi:10.1016/0923-2508(96)84010-1

Cited by 30 publications

(36 citation statements)

References 38 publications

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“…No other mutations giving rise to this general suppressor phenotype have been reported, suggesting that EIIA Glc is unique in being able to regulate PTS-mediated inducer exclusion and to activate adenylate cyclase in enteric bacteria. Therefore, it came as a surprise that a residual level of inducer exclusion was observed in S. enterica serovar Typhimurium crr deletion strains (595 (500,717). In H. influenzae, only fructose, but not glucose, is taken up via a PTS, and a ptsI mutant can therefore ferment glucose (499).…”

Section: Regulation By Eiia Glc -Like Proteinsmentioning

confidence: 99%

How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria

Deutscher

Francke

Postma

2006

Microbiol Mol Biol Rev

1,188

769

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SUMMARY The phosphoenolpyruvate(PEP):carbohydrate phosphotransferase system (PTS) is found only in bacteria, where it catalyzes the transport and phosphorylation of numerous monosaccharides, disaccharides, amino sugars, polyols, and other sugar derivatives. To carry out its catalytic function in sugar transport and phosphorylation, the PTS uses PEP as an energy source and phosphoryl donor. The phosphoryl group of PEP is usually transferred via four distinct proteins (domains) to the transported sugar bound to the respective membrane component(s) (EIIC and EIID) of the PTS. The organization of the PTS as a four-step phosphoryl transfer system, in which all P derivatives exhibit similar energy (phosphorylation occurs at histidyl or cysteyl residues), is surprising, as a single protein (or domain) coupling energy transfer and sugar phosphorylation would be sufficient for PTS function. A possible explanation for the complexity of the PTS was provided by the discovery that the PTS also carries out numerous regulatory functions. Depending on their phosphorylation state, the four proteins (domains) forming the PTS phosphorylation cascade (EI, HPr, EIIA, and EIIB) can phosphorylate or interact with numerous non-PTS proteins and thereby regulate their activity. In addition, in certain bacteria, one of the PTS components (HPr) is phosphorylated by ATP at a seryl residue, which increases the complexity of PTS-mediated regulation. In this review, we try to summarize the known protein phosphorylation-related regulatory functions of the PTS. As we shall see, the PTS regulation network not only controls carbohydrate uptake and metabolism but also interferes with the utilization of nitrogen and phosphorus and the virulence of certain pathogens.

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Section: Regulation By Eiia Glc -Like Proteinsmentioning

confidence: 99%

How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria

Deutscher

Francke

Postma

2006

Microbiol Mol Biol Rev

1,188

769

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“…Even though it has been 8 years since the genome of H. influenzae strain Rd KW20 was sequenced, some critical questions about the metabolic capacities of this organism remain unanswered. For example, although H. influenzae is known to ferment glucose (24,25,39), its glucose transporter remains to be unidentified and properly annotated in the genome database (15,57). The only protein annotated as a component of the glucose transport machinery, a homolog of the E. coli crr gene product, is apparently a part of the fructose-specific phosphoenolpyruvate-dependent phosphotransferase system (40).…”

Section: Discussionmentioning

confidence: 99%

Initial Proteome Analysis of Model MicroorganismHaemophilus influenzaeStrain Rd KW20

Kolker¹,

Purvine²,

Galperin

et al. 2003

J Bacteriol

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The proteome of Haemophilus influenzae strain Rd KW20 was analyzed by liquid chromatography (LC) coupled with ion trap tandem mass spectrometry (MS/MS). This approach does not require a gel electrophoresis step and provides a rapidly developed snapshot of the proteome. In order to gain insight into the central metabolism of H. influenzae, cells were grown microaerobically and anaerobically in a rich medium and soluble and membrane proteins of strain Rd KW20 were proteolyzed with trypsin and directly examined by LC-MS/MS. Several different experimental and computational approaches were utilized to optimize the proteome coverage and to ensure statistically valid protein identification. Approximately 25% of all predicted proteins (open reading frames) of H. influenzae strain Rd KW20 were identified with high confidence, as their component peptides were unambiguously assigned to tandem mass spectra. Approximately 80% of the predicted ribosomal proteins were identified with high confidence, compared to the 33% of the predicted ribosomal proteins detected by previous two-dimensional gel electrophoresis studies. The results obtained in this study are generally consistent with those obtained from computational genome analysis, two-dimensional gel electrophoresis, and whole-genome transposon mutagenesis studies. At least 15 genes originally annotated as conserved hypothetical were found to encode expressed proteins. Two more proteins, previously annotated as predicted coding regions, were detected with high confidence; these proteins also have close homologs in related bacteria. The direct proteomics approach to studying protein expression in vivo reported here is a powerful method that is applicable to proteome analysis of any (micro)organism.

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“…In the absence or at a reduced level of fructose, transport and metabolism of fucose and other sugars are upregulated (40). The genome sequence of H. influenzae has revealed the presence of a cluster of genes involved in the transport and subsequent metabolism of fucose (41,42). One of the genes in the fucose operon is fucK, encoding fuculokinase, which has been included in the multilocus sequence typing (MLST) scheme for H. influenzae (43).…”

Section: The Haemophilus Influenzae Groupmentioning

confidence: 99%

“…Residues 33,42,59, and 61 of OMP P6 are alanine, alanine, aspartate, and threonine, respectively, in H. influenzae, while the corresponding residues in H. haemolyticus are glycine, serine, asparagine, and glutamate; in particular, the conformation of the MAb 7F3 epitope depends on amino acids 59 and 61 (194). Chang and coworkers sequenced the ompP6 genes of 163 isolates obtained from the pharynxes of healthy children and from cases of pediatric otitis media (200).…”

Section: Detection Of Biomarker Genes By Pcrmentioning

confidence: 99%

Classification, Identification, and Clinical Significance of Haemophilus and Aggregatibacter Species with Host Specificity for Humans

2014

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SUMMARY The aim of this review is to provide a comprehensive update on the current classification and identification of Haemophilus and Aggregatibacter species with exclusive or predominant host specificity for humans. Haemophilus influenzae and some of the other Haemophilus species are commonly encountered in the clinical microbiology laboratory and demonstrate a wide range of pathogenicity, from life-threatening invasive disease to respiratory infections to a nonpathogenic, commensal lifestyle. New species of Haemophilus have been described ( Haemophilus pittmaniae and Haemophilus sputorum ), and the new genus Aggregatibacter was created to accommodate some former Haemophilus and Actinobacillus species ( Aggregatibacter aphrophilus , Aggregatibacter segnis , and Aggregatibacter actinomycetemcomitans ). Aggregatibacter species are now a dominant etiology of infective endocarditis caused by fastidious organisms (HACEK endocarditis), and A. aphrophilus has emerged as an important cause of brain abscesses. Correct identification of Haemophilus and Aggregatibacter species based on phenotypic characterization can be challenging. It has become clear that 15 to 20% of presumptive H. influenzae isolates from the respiratory tracts of healthy individuals do not belong to this species but represent nonhemolytic variants of Haemophilus haemolyticus . Due to the limited pathogenicity of H. haemolyticus , the proportion of misidentified strains may be lower in clinical samples, but even among invasive strains, a misidentification rate of 0.5 to 2% can be found. Several methods have been investigated for differentiation of H. influenzae from its less pathogenic relatives, but a simple method for reliable discrimination is not available. With the implementation of identification by matrix-assisted laser desorption ionization–time of flight mass spectrometry, the more rarely encountered species of Haemophilus and Aggregatibacter will increasingly be identified in clinical microbiology practice. However, identification of some strains will still be problematic, necessitating DNA sequencing of multiple housekeeping gene fragments or full-length 16S rRNA genes.

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Life in mucus: sugar metabolism in Haemophilus influenzae

Cited by 30 publications

References 38 publications

How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria

How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria

Initial Proteome Analysis of Model MicroorganismHaemophilus influenzaeStrain Rd KW20

Classification, Identification, and Clinical Significance of Haemophilus and Aggregatibacter Species with Host Specificity for Humans

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