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PubMed2004

Amperometric microbial biosensor for p-nitrophenol using Moraxella sp.-modified carbon paste electrode.

An amperometric microbial biosensor for highly specific, sensitive and rapid quantitative determination of p-nitrophenol was developed. The biosensor takes advantage of the ability of Moraxella sp. to specifically degrade p-nitrophenol to hydroquinone, a more electroactive compound than p-nitrophenol. The electrochemical oxidation current of hydroquinone formed in biodegradation of p-nitrophenol was measured at Moraxella sp.-modified carbon paste electrode and correlated to p-phenol concentrations. The optimum response was realized by electrode constructed using 15 mg of dry cell weight per 1 g of carbon paste and operating at 0.3 V (versus Ag/AgCl reference) in pH 7.5, 20 mM sodium phosphate buffer. Operating at these optimum conditions the biosensor had excellent selectivity against phenol derivatives and was able to measure as low as 20 nM (2.78 ppb) p-nitrophenol with very good accuracy and reproducibility. The biosensor was stable for approximately 3 weeks when stored at 4 degrees C. The applicability of the biosensor to measure p-nitrophenol in lake water was demonstrated.

Biological Assay↗
PubMed2000

Using a green fluorescent protein gene-labeled p-nitrophenol-degrading Moraxella strain to examine the protective effect of alginate encapsulation against protozoan grazing.

A gfp-labeled p-nitrophenol-degrading Moraxella strain G21 was used to study grazing of a Tetrahymena thermophila strain in liquid medium. This allowed visualization of the feeding process. Under an epifluorescent microscope, individual G21 fluorescent cells could be seen in vacuoles within the protozoans. Most of the G21 cells appeared to be lysed by T. thermophila and green fluorescent protein released from the bacteria yielded brightly fluorescent food vacuoles inside the protozoans, Examination of population dynamics of a mixed culture of T. thermophila and Moraxella sp. G21 showed that the protozoan reduced the bacterial density from 7.6 to 5.8 log CFU/ml in 2 days. Encapsulating the bacteria in alginate prevented grazing by the protozoans and the density of G21 cells in the beads increased steadily from about 8.3 to 8.9 log CFU/ml in 15 days regardless of the presence of the protozoans.

Alginates↗
PubMed2003

Molecular cloning and characterization of a 79-kDa iron-repressible outer-membrane protein of Moraxella bovis.

Moraxella bovis expresses an iron-repressible 79-kDa outer-membrane protein, IrpA. DNA and N-terminal amino acid sequence analysis indicate that IrpA is closely related to FrpB of Neisseria meningitidis, FetA of Neisseria gonorrhoeae and CopB of Moraxella catarrhalis. The results of manganese mutagenesis and a gel-shift assay suggested that the transcription of irpA is negatively regulated by the ferric uptake regulator. The insertion of an antibiotic resistance cassette into the irpA gene affected the strain's ability to utilize bovine transferrin and lactoferrin. IrpA was detected in geographically diverse clinical isolates, and the antigenicity of IrpA was conserved in all the isolates tested. Therefore, IrpA may have potential as a candidate vaccine.

Amino Acid Sequence↗
PubMed1998

In vitro evaluation of a novel orally administered cephalosporin (Cefditoren) tested against 1249 recent clinical isolates of Haemophilus influenzae, Moraxella catarrhalis, and Streptococcus pneumoniae.

Cefditoren (formerly ME-1206), a new orally administered cephalosporin, was evaluated in vitro against 1249 recently isolated strains of Streptococcus pneumoniae (500 strains), Moraxella catarrhalis (250 strains), and Haemophilus influenzae (499 strains). Reference National Committee for Clinical Laboratory Standards methods were used and the strains were representative for the current rates of beta-lactamase production or penicillin resistance. Cefditoren had MIC50/MIC90 results for Moraxella catarrhalis and Haemophilus influenzae of 0.12/0.5 and < or = 0.008/0.015 microgram/mL, respectively. The pneumococci were consistently twofold to eightfold more susceptible to cefditoren than other oral cephalosporins or penicillins. The MIC90 for penicillin-resistant S. pneumoniae was only 2 micrograms cefditoren/mL, and the highest recorded MIC was 4 micrograms/mL. Cefditoren appears to be a very promising beta-lactam possessing the greatest potency and potential spectrum versus contemporary (1997) respiratory tract pathogens.

Anti-Bacterial Agents↗
PubMed1999

Stereospecificity of hydrogen transfer by the NAD(+)-linked alcohol dehydrogenase from the Antarctic psychrophile Moraxella sp. TAE123.

Investigation of the stereochemistry of the hydride transfer in reactions catalyzed by the recently isolated NAD(+)-linked alcohol dehydrogenase from the Antarctic psychrophile Moraxella sp. TAE123 was accomplished by using 1H NMR spectroscopy of the deuterated coenzyme. It was found that this new psychrophilic enzyme is a type A dehydrogenase. Moraxella sp. ADH reduces stereospecifically 2-butanone to produce (S)-2-butanol.

Alcohol Dehydrogenase↗
PubMed2001

Sequence analysis and insertional inactivation of a gene encoding Moraxella sp. CK-1 cell wall hydrolase.

Sequencing of the Moraxella sp. CK-1 autolysin (cell wall hydrolases) gene showed the presence of an open reading frame which encodes a polypeptide of 273 amino acids with a molecular mass of 33,316 Da. A presumed ribosomal binding site, a possible -10 and -35 region, and rho-dependent terminators were found. The C-terminal region of the mature protein showed considerable homology with the Thermus sp. serine proteinase. Enzyme assay suggests that the recombinant autolysin has amidase or endopeptidase activity. Analysis of the peptidoglycan fragments, following the treatment with the autolysin, indicates that this protein is an N-acetylmuramyl-L-alanine amidase. Insertional inactivation of the autolysin of Moraxella sp. CK-1 chromosome led to a decrease in cell wall hydrolytic activity, clumping of the cells, and color change. No lytic band present in inactivated magA mutant by renaturing SDS-PAGE.

Amino Acid Sequence↗
PubMed1998

Purification and characterization of an alcohol dehydrogenase from the Antarctic psychrophile Moraxella sp. TAE123.

An NAD+-dependent alcohol dehydrogenase (ADH) of the Antarctic psychrophile Moraxella sp. TAE123 was purified to homogeneity with an overall yield of 16.7% and further characterized. The native enzyme had an apparent molecular mass of 240 kDa and consisted of four identical 52-kDa subunits. The pI of the enzyme was determined to be 5.5, while its optimum pH is 7.5. The enzyme contained 1 zinc atom/subunit and exhibited a remarkable thermal lability. Moraxella sp. TAE123 ADH exhibited a wide range of substrate specificity similar to its mammalian counterparts and in contrast to other microbial ADHs. It oxidized mainly primary and secondary aliphatic alcohols. The highest reaction rate was observed when ethanol was used as substrate. A gradual decrease in rate was observed by increasing the length and branching of the carbon chain of the alcohol. This enzyme oxidized effectively large bulky alcohols, such as diphenylmethanol. Reduction of aldehydes and ketones was also observed. N-terminal amino acid sequence analysis of the enzyme did not reveal any similarity with the amino termini of all other ADHs, while an unexpected significant similarity was observed with the amino terminal sequence of four prokaryotic aldehyde dehydrogenases.

Alcohol Dehydrogenase↗
PubMed2000

Antimicrobial susceptibility of Streptococcus pneumoniae, Haemophilus influenzae and Moraxella catarrhalis collected from five centers in Brazil, 1997-98.

OBJECTIVE: To assess the susceptibility of the key respiratory pathogens Streptococcus pneumoniae, Haemophilus influenzae and Moraxella catarrhalis to antimicrobial agents used to treat respiratory tract infections. METHODS: Isolates were collected from five centers in Brazil during 1997-98, and susceptibility testing was conducted at a central laboratory according to National Committee for Clinical Laboratory Standards criteria. RESULTS: Of the 359Streptococcus pneumoniae isolates tested, 77% were susceptible, 19% were intermediate and 4% were resistant to penicillin. The susceptibility of S. pneumoniae to other beta-lactams and macrolides was greater than 90%, but cotrimoxazole was active against only 48% of the isolates. The prevalence of susceptible isolates was 100.0% for vancomycin and 99.7% for levofloxacin. beta-Lactam, macrolide, and cotrimoxazole activities were negatively associated with penicillin resistance. Of the 219 isolates of Haemophilus influenzae tested, 11% produced beta-lactamase and 11% were not susceptible to ampicillin. Nearly all H. influenzae isolates were susceptible to all other drugs, except cotrimoxazole (47% susceptibility). Of the 52 Moraxella catarrhalis isolates, 98% produced beta-lactamase, and the MIC of all drugs was </=4 mg/L, with the exception of ampicillin, where the MIC90 was> 8 mg/L. CONCLUSIONS: When these data are compared with previous reports, our findings suggest that the prevalence of pneumococci that are resistant to agents such as penicillin and cotrimoxazole may be increasing in Brazil, which highlights the need to continue surveillance programs.

Anti-Bacterial Agents↗
PubMed1993

Gene organization and primary structure of human hormone-sensitive lipase: possible significance of a sequence homology with a lipase of Moraxella TA144, an antarctic bacterium.

The human hormone-sensitive lipase (HSL) gene encodes a 786-aa polypeptide (85.5 kDa). It is composed of nine exons spanning approximately 11 kb, with exons 2-5 clustered in a 1.1-kb region. The putative catalytic site (Ser423) and a possible lipid-binding region in the C-terminal part are encoded by exons 6 and 9, respectively. Exon 8 encodes the phosphorylation site (Ser551) that controls cAMP-mediated activity and a second site (Ser553) that is phosphorylated by 5'-AMP-activated protein kinase. Human HSL showed 83% identity with the rat enzyme and contained a 12-aa deletion immediately upstream of the phosphorylation sites with an unknown effect on the activity control. Besides the catalytic site motif (Gly-Xaa-Ser-Xaa-Gly) found in most lipases, HSL shows no homology with other known lipases or proteins, except for a recently reported unexpected homology between the region surrounding its catalytic site and that of the lipase 2 of Moraxella TA144, an antarctic psychrotrophic bacterium. The gene of lipase 2, which catalyses lipolysis below 4 degrees C, was absent in the genomic DNA of five other Moraxella strains living at 37 degrees C. The lipase 2-like sequence in HSL may reflect an evolutionarily conserved cold adaptability that might be of critical survival value when low-temperature-mobilized endogenous lipids are the primary energy source (e.g., in poikilotherms or hibernators). The finding that HSL at 10 degrees C retained 3- to 5-fold more of its 37 degrees C catalytic activity than lipoprotein lipase or carboxyl ester lipase is consistent with this hypothesis.

Adipose Tissue↗
PubMed1999

Multiple DNA binding activities of the novel site-specific recombinase, Piv, from Moraxella lacunata.

The recombinase, Piv, is essential for site-specific DNA inversion of the type IV pilin DNA segment in Moraxella lacunata and Moraxella bovis. Piv shows significant homology with the transposases of the IS110/IS492 family of insertion elements, but, surprisingly, Piv contains none of the conserved amino acid motifs of the lambda Int or Hin/Res families of site-specific recombinases. Therefore, Piv may mediate site-specific recombination by a novel mechanism. To begin to determine how Piv may assemble a synaptic nucleoprotein structure for DNA cleavage and strand exchange, we have characterized the interaction of Piv with the DNA inversion region of M. lacunata. Gel shift and nuclease/chemical protection assays, competition and dissociation rate analyses, and cooperativity studies indicate that Piv binds two distinct recognition sequences. One recognition sequence, found at multiple sites within and outside of the invertible segment, is bound by Piv protomers with high affinity. The second recognition sequence is located at the recombination cross-over sites at the ends of the invertible element; Piv interacts with this sequence as an oligomer with apparent low affinity. A model is proposed for the role of the different Piv binding sites of the M. lacunata inversion region in the formation of an active synaptosome.

Base Sequence↗
PubMed2006

The respiratory pathogen moraxella catarrhalis binds to laminin via ubiquitous surface proteins A1 and A2.

Moraxella catarrhalis is one of the leading causes of exacerbations in chronic obstructive pulmonary disease (COPD). In the present article, we show that moraxella (n=15) binds to the major basement-membrane glycoprotein laminin, which is thickened in the airways of smokers. Using clinical strains of M. catarrhalis and their corresponding ubiquitous surface protein (Usp) A1/A2 mutants, we demonstrate that UspA1 and UspA2 are important for the laminin interaction. Binding assays with recombinant proteins demonstrated that the binding regions are localized within the N-terminal fragments, where both proteins form a globular head. Thus, UspA1/A2-dependent interactions with laminin might promote bacterial adhesion, particularly in smokers with COPD.

Bacterial Adhesion↗
PubMed1999

Moraxella catarrhalis bacteremia: a 10-year experience.

BACKGROUND: Moraxella catarrhalis commonly inhabits the upper respiratory tract and is a cause of acute otitis media and sinusitis in children. It is an infrequent cause of invasive disease. METHODS: We reviewed records of all patients with positive blood cultures for M catarrhalis admitted to our hospital during the 10-year period (1988 through 1997). RESULTS: Eleven cases were identified. Age range was 11 to 32 months. Four (44%) had risk factors for infection, including sickle cell disease (2), acquired immunodeficiency syndrome (AIDS) (1), and leukopenia (1). Upper respiratory symptoms and fever were present in all patients. Ten had acute otitis media, five had sinusitis, and three had pneumonia. All isolates were beta-lactamase producers. Treatment included intravenous cefuroxime (8), cefotaxime (2), and ceftazidime (1), followed by oral amoxicillin/clavulanate or cefuroxime axetil. CONCLUSION: Moraxella catarrhalis bacteremia should be considered in febrile young children with upper respiratory infections and/or acute otitis media especially in those with underlying immune dysfunction.

Acute Disease↗
PubMed2001

Nomenclature of the subgenera Moraxella and Branhamella and of the nine species included in these subgenera and proposal to modify rule 34a of the Bacteriological Code (1990 Revision). Request for an opinion.

The subgenera Moraxella and Branhamella and the nine species included in these subgenera were inadvertently omitted from the Approved Lists of Bacterial Names and have never been revived according to Rule 28a of the Bacteriological Code (1990 Revision). The author requests that these names be revived and considered to be validly published in the 'Index of the bacterial and yeast nomenclatural changes published in the International Journal of Systematic Bacteriology since the 1980 Approved Lists of Bacterial Names (1 January 1980 to 1 January 1985)', which appears in the July 1985 issue of the International Journal of Systematic Bacteriology. Another problem is the status of the species included in the subgenera Moraxella and Branhamella because the Bacteriological Code (1990 Revision) does not envisage the status of a species transferred into a subgenus. The same is true for a species transferred into a subspecies. The author requests that such species be considered as new combinations and, according to this, proposes to modify Rule 34a of the Bacteriological Code (1990 Revision).

Bacteriology↗
PubMed1991

The type 4 pilin of Moraxella nonliquefaciens exhibits unique similarities with the pilins of Neisseria gonorrhoeae and Dichelobacter (Bacteroides) nodosus.

Moraxella nonliquefaciens is a bacterium which is part of the normal flora of the human upper respiratory tract and is an occasional cause of disease. Using a previously cloned type 4 pilin gene (tfpQ) from Moraxella bovis as a hybridization probe, we have cloned an 826 bp Sau3 AI fragment which contains an M. nonliquefaciens type 4 pilin gene (tfpA) from strain NCTC 7784. The pilin gene is expressed in Escherichia coli. We have examined NCTC 7784 and nine other M. nonliquefaciens strains by genomic Southern hybridization using tfpA as a probe, and they all appeared to have more than one pilin gene. While the predicted amino acid sequence of the M. nonliquefaciens tfpA pilin has conserved regions as compared to pilins of M. bovis and M. lacunata, it also shows similarities to both the type 4 pilin of Neisseria gonorrhoeae and the type 4 pilin of Dichelobacter nodosus (formerly Bacteroides nodosus).

Amino Acid Sequence↗
PubMed2005

Identification of a conserved Moraxella catarrhalis haemoglobin-utilization protein, MhuA.

Moraxella catarrhalis is a leading cause of acute otitis media in children and is a cause of respiratory disease in adults with underlying lung disease. This organism is a strict human pathogen that has an absolute requirement for iron in order to grow and cause disease. Previous studies identified transferrin and lactoferrin receptors used by M. catarrhalis to obtain iron from the human host, yet other iron-acquisition systems remain undefined. In this study, it is demonstrated that this strict mucosal pathogen can utilize haemoglobin (Hb) as a sole source of iron for growth. A novel 107 kDa outer-membrane protein involved in Hb utilization by this pathogen was also identified. An isogenic mutant defective in this Moraxella Hb-utilization protein (MhuA), 7169 : : mhuA, showed a significant lag during growth in the presence of Hb as the sole iron source. This protein appears to be expressed constitutively, regardless of growth conditions, and a mAb directed to MhuA demonstrated that this protein contains highly conserved, surface-exposed epitopes. Data demonstrating that expression of MhuA may be highly specific to isolates of M. catarrhalis are also presented, suggesting a potential role as a diagnostic marker. To our knowledge, this is the first report demonstrating that M. catarrhalis expresses an Hb-binding protein and that this bacterium can utilize Hb as a sole iron source for growth.

Antibodies, Bacterial↗
PubMed1994

Pre-septal cellulitis and facial erysipelas due to Moraxella species.

We describe a patient with an acute ulcerated pre-septal cellulitis with subsequent spread across the face, in whom conjunctival swabs demonstrated the presence of Moraxella species. Unusually, this organism was resistant to penicillin. Clinical improvement was only achieved when treatment with co-amoxiclav was commenced on the basis of the antibiotic sensitivities demonstrated by culture of this organism. Moraxella species are rare skin pathogens but may be underestimated as they usually respond to a wide range of antibiotics; they should be considered as a cause of facial cellulitis or erysipelas which responds poorly to conventional therapy.

Adult↗
PubMed2006

Moraxella catarrhalis is internalized in respiratory epithelial cells by a trigger-like mechanism and initiates a TLR2- and partly NOD1-dependent inflammatory immune response.

Moraxella catarrhalis is an important pathogen in patients with chronic obstructive lung disease (COPD). While M. catarrhalis has been categorized as an extracellular bacterium so far, the potential to invade human respiratory epithelium has not yet been explored. Our results obtained by electron and confocal microscopy demonstrated a considerable potential of M. catarrhalis to invade bronchial epithelial (BEAS-2B) cells, type II pneumocytes (A549) and primary small airway epithelial cells (SAEC). Moraxella invasion was dependent on cellular microfilament as well as on bacterial viability, and characterized by macropinocytosis leading to the formation of lamellipodia and engulfment of the invading organism into macropinosomes, thus indicating a trigger-like uptake mechanism. In addition, the cells examined expressed TLR2 as well as NOD1, a recently found cytosolic protein implicated in the intracellular recognition of bacterial cell wall components. Importantly, inhibition of TLR2 or NOD1 expression by RNAi significantly reduced the M. catarrhalis-induced IL-8 secretion. The role of TLR2 and NOD1 was further confirmed by overexpression assays in HEK293 cells. Overall, M. catarrhalis may employ lung epithelial cell invasion to colonize and to infect the respiratory tract, nonetheless, the bacteria are recognized by cell surface TLR2 and the intracellular surveillance molecule NOD1.

Cell Line↗
PubMed2006

Polymorphism of the major surface epitope of the CopB outer membrane protein of Moraxella catarrhalis.

The CopB outer membrane protein has been considered a vaccine candidate for the prevention of infections due to Moraxella catarrhalis. Monoclonal antibody 10F3 recognizes whole cells of about 70% of clinical isolates, suggesting that this epitope is reasonably conserved. To determine whether CopB has other surface epitopes, we analyzed M. catarrhalis isolates using polyclonal sera against recombinant CopB proteins from a 10F3 positive isolate and a 10F3 negative isolate, and polyclonal sera against synthetic peptides that contained the sequence corresponding to the 10F3 epitope region of three different isolates. Extensive cross-reactivity was observed with the anti-CopB sera towards purified recombinant CopB proteins in Western blot and antigen ELISA, implying that antigenic regions common to both proteins were present. However, anti-CopB sera resembled anti-CopB peptide sera in exhibiting similar binding specificity to whole cells, segregating M. catarrhalis isolates into four CopB groups. We subsequently cloned and sequenced the copB genes from representative isolates. The deduced CopB amino acid sequences and the degree of sequence identity also demonstrated the existence of the same four CopB groups. Each of the four groups had a unique sequence in the 10F3 epitope region and a fifth group had the epitope deleted. The polymorphism of the major surface epitope prompts further consideration regarding the utility of CopB as a vaccine component as well as the design of an efficacious CopB-based vaccine to achieve broad protection against Moraxella infection.

Animals↗