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Journal articles on the topic 'M. catarrhalis'

Author: Grafiati

Published: 4 June 2021

Last updated: 19 February 2022

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1

Aebi, Christoph, Leslie D. Cope, Jo L. Latimer, Sharon E. Thomas, Clive A. Slaughter, George H. McCracken, and Eric J. Hansen. "Mapping of a Protective Epitope of the CopB Outer Membrane Protein of Moraxella catarrhalis." Infection and Immunity 66, no. 2 (February 1, 1998): 540–48. http://dx.doi.org/10.1128/iai.66.2.540-548.1998.

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ABSTRACT A monoclonal antibody (MAb) (MAb 10F3) directed against the CopB outer membrane protein of Moraxella catarrhalis previously was found to enhance pulmonary clearance of M. catarrhalisin an animal model (M. Helminen, I. Maciver, J. L. Latimer, L. D. Cope, G. H. McCracken, Jr., and E. J. Hansen, Infect. Immun. 61:2003–2010, 1993). In the present study, this same MAb was shown to exert complement-dependent bactericidal activity against this pathogen in vitro. Nucleotide sequence analysis of thecopB gene from two MAb 10F3-reactive and two MAb 10F3-unreactive strains of M. catarrhalis revea

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Slevogt, Hortense, Bernd Schmeck, Carola Jonatat, Janine Zahlten, Wiebke Beermann, Vincent van Laak, Bastian Opitz та ін. "Moraxella catarrhalis induces inflammatory response of bronchial epithelial cells via MAPK and NF-κB activation and histone deacetylase activity reduction". American Journal of Physiology-Lung Cellular and Molecular Physiology 290, № 5 (травень 2006): L818—L826. http://dx.doi.org/10.1152/ajplung.00428.2005.

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Moraxella catarrhalis is a major cause of infectious exacerbations of chronic obstructive lung disease (COPD) and may also contribute to the pathogenesis of COPD. Little is known about M. catarrhalis-bronchial epithelium interaction. We investigated activation of M. catarrhalis infected bronchial epithelial cells and characterized the signal transduction pathways. Moreover, we tested the hypothesis that the M. catarrhalis-induced cytokine expression is regulated by acetylation of histone residues and controlled by histone deacetylase activity (HDAC). We demonstrated that M. catarrhalis induced

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3

Gutbier, Birgitt, Katja Fischer, Jan-Moritz Doehn, Carolin von Lachner, Christian Herr, Esther Klaile, Ursula Frischmann, et al. "Moraxella catarrhalisinduces an immune response in the murine lung that is independent of human CEACAM5 expression and long-term smoke exposure." American Journal of Physiology-Lung Cellular and Molecular Physiology 309, no. 3 (August 1, 2015): L250—L261. http://dx.doi.org/10.1152/ajplung.00265.2014.

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In patients with chronic obstructive pulmonary disease (COPD), Moraxella catarrhalis infection of the lower airways is associated with chronic colonization and inflammation during stable disease and acute exacerbations. Chronic smoke exposure induces chronic inflammation and impairs mucociliary clearance, thus contributing to bacterial colonization of the lower airways in COPD patients. The human-specific carcinoembryonic antigen-related cell adhesion molecule (CEACAM) 5, expressed in human airways, has been shown to contribute to epithelial colonization of CEACAM-binding pathogens. To investi

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Luke, Nicole R., Joseph A. Jurcisek, Lauren O. Bakaletz, and Anthony A. Campagnari. "Contribution of Moraxella catarrhalis Type IV Pili to Nasopharyngeal Colonization and Biofilm Formation." Infection and Immunity 75, no. 12 (October 1, 2007): 5559–64. http://dx.doi.org/10.1128/iai.00946-07.

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ABSTRACT Moraxella catarrhalis is a gram-negative mucosal pathogen of the human respiratory tract. Although little information is available regarding the initial steps of M. catarrhalis pathogenesis, this organism must be able to colonize the human mucosal surface in order to initiate an infection. Type IV pili (TFP), filamentous surface appendages primarily comprised of a single protein subunit termed pilin, play a crucial role in the initiation of disease by a wide range of bacteria. We previously identified the genes that encode the major proteins involved in the biosynthesis of M. catarrha

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5

Attia, Ahmed S., Jennifer L. Sedillo, Wei Wang, Wei Liu, Chad A. Brautigam, Wade Winkler, and Eric J. Hansen. "Moraxella catarrhalis Expresses an Unusual Hfq Protein." Infection and Immunity 76, no. 6 (March 24, 2008): 2520–30. http://dx.doi.org/10.1128/iai.01652-07.

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ABSTRACT The Hfq protein is recognized as a global regulatory molecule that facilitates certain RNA-RNA interactions in bacteria. BLAST analysis identified a 630-nucleotide open reading frame in the genome of Moraxella catarrhalis ATCC 43617 that was highly conserved among M. catarrhalis strains and which encoded a predicted protein with significant homology to the Hfq protein of Escherichia coli. This protein, containing 210 amino acids, was more than twice as large as the Hfq proteins previously described for other bacteria. The C-terminal half of the M. catarrhalis Hfq protein was very hydr

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Hoopman, Todd C., Wei Wang, Chad A. Brautigam, Jennifer L. Sedillo, Thomas J. Reilly, and Eric J. Hansen. "Moraxella catarrhalis Synthesizes an Autotransporter That Is an Acid Phosphatase." Journal of Bacteriology 190, no. 4 (December 7, 2007): 1459–72. http://dx.doi.org/10.1128/jb.01688-07.

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ABSTRACT Moraxella catarrhalis O35E was shown to synthesize a 105-kDa protein that has similarity to both acid phosphatases and autotransporters. The N-terminal portion of the M. catarrhalis acid phosphatase A (MapA) was most similar (the BLAST probability score was 10−10) to bacterial class A nonspecific acid phosphatases. The central region of the MapA protein had similarity to passenger domains of other autotransporter proteins, whereas the C-terminal portion of MapA resembled the translocation domain of conventional autotransporters. Cloning and expression of the M. catarrhalis mapA gene i

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7

Sano, Naoto, Satoshi Matsunaga, Tomonori Akiyama, Yukari Nakashima, Koji Kusaba, Zenzo Nagasawa, Shunzo Koizumi, Masaaki Goto, and Hiroshi Miyamoto. "Moraxella catarrhalis bacteraemia associated with prosthetic vascular graft infection." Journal of Medical Microbiology 59, no. 2 (February 1, 2010): 245–50. http://dx.doi.org/10.1099/jmm.0.013789-0.

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Moraxella catarrhalis, formerly called Branhamella catarrhalis, ‘Neisseria catarrhalis’ or ‘Micrococcus catarrhalis’, is a Gram-negative, aerobic diplococcus frequently found as a colonizer of the upper respiratory tract. Over the last 20–30 years, this bacterium has emerged as a genuine pathogen, and is now considered an important cause of otitis media in children and an aetiological agent in pneumonia in adults with chronic obstructive pulmonary disease. However, bacteraemia due to M. catarrhalis has rarely been reported. Presented here is a case of M. catarrhalis bacteraemia associated with

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8

Verduin, Cees M., Cees Hol, André Fleer, Hans van Dijk, and Alex van Belkum. "Moraxella catarrhalis: from Emerging to Established Pathogen." Clinical Microbiology Reviews 15, no. 1 (January 2002): 125–44. http://dx.doi.org/10.1128/cmr.15.1.125-144.2002.

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SUMMARY Moraxella catarrhalis (formerly known as Branhamella catarrhalis) has emerged as a significant bacterial pathogen of humans over the past two decades. During this period, microbiological and molecular diagnostic techniques have been developed and improved for M. catarrhalis, allowing the adequate determination and taxonomic positioning of this pathogen. Over the same period, studies have revealed its involvement in respiratory (e.g., sinusitis, otitis media, bronchitis, and pneumonia) and ocular infections in children and in laryngitis, bronchitis, and pneumonia in adults. The developm

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Verhaegh, Suzanne J. C., Martine L. Snippe, Foster Levy, Henri A. Verbrugh, Vincent W. V. Jaddoe, Albert Hofman, Henriëtte A. Moll, Alex van Belkum, and John P. Hays. "Colonization of healthy children by Moraxella catarrhalis is characterized by genotype heterogeneity, virulence gene diversity and co-colonization with Haemophilus influenzae." Microbiology 157, no. 1 (January 1, 2011): 169–78. http://dx.doi.org/10.1099/mic.0.042929-0.

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The colonization dynamics of Moraxella catarrhalis were studied in a population comprising 1079 healthy children living in Rotterdam, The Netherlands (the Generation R Focus cohort). A total of 2751 nasal swabs were obtained during four clinic visits timed to take place at 1.5, 6, 14 and 24 months of age, yielding a total of 709 M. catarrhalis and 621 Haemophilus influenzae isolates. Between January 2004 and December 2006, approximate but regular 6-monthly cycles of colonization were observed, with peak colonization incidences occurring in the autumn/winter for M. catarrhalis, and winter/sprin

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Furano, Kristin, and Anthony A. Campagnari. "Identification of a Hemin Utilization Protein of Moraxella catarrhalis (HumA)." Infection and Immunity 72, no. 11 (November 2004): 6426–32. http://dx.doi.org/10.1128/iai.72.11.6426-6432.2004.

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ABSTRACT Moraxella catarrhalis is a major cause of acute otitis media in young children and has also been implicated as an important cause of exacerbations in adults with underlying pulmonary disease. Due to the considerable level of antibiotic resistance and the high degree of carriage rates in young children, it is likely that the incidence of M. catarrhalis infections will continue to rise. M. catarrhalis is a strict human respiratory pathogen, and this bacterium uses both transferrin and lactoferrin receptors to fulfill the essential iron requirement for survival in vivo. However, these ar

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Zaleski, Anthony, N. Karoline Scheffler, Peter Densen, Frank K. N. Lee, Anthony A. Campagnari, Bradford W. Gibson та Michael A. Apicella. "Lipooligosaccharide Pk(Galα1-4Galβ1-4Glc) Epitope of Moraxella catarrhalis Is a Factor in Resistance to Bactericidal Activity Mediated by Normal Human Serum". Infection and Immunity 68, № 9 (1 вересня 2000): 5261–68. http://dx.doi.org/10.1128/iai.68.9.5261-5268.2000.

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ABSTRACT Moraxella catarrhalis is a respiratory pathogen responsible for acute bacterial otitis media in children and exacerbation of chronic bronchitis in adults. M. catarrhalis strains are frequently resistant to the bactericidal activity of normal human serum. In order to determine if the lipooligosaccharide (LOS) of M. catarrhalis has a role in serum resistance, the UDP-glucose-4-epimerase (galE) gene was identified, cloned, and sequenced and a deletion/insertion mutation was introduced into M. catarrhalis strain 2951. GalE enzymatic activity, measured in whole-cell lysates, was ablated in

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12

Bootsma, H. J., H. van Dijk, J. Verhoef, A. Fleer, and F. R. Mooi. "Molecular characterization of the BRO beta-lactamase of Moraxella (Branhamella) catarrhalis." Antimicrobial Agents and Chemotherapy 40, no. 4 (April 1996): 966–72. http://dx.doi.org/10.1128/aac.40.4.966.

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A rapid increase in the prevalence of beta-lactamase-producing Moraxella (Branhamella) catarrhalis strains has been noticed during the last decades. Today, more than 80% of strains isolated worldwide produce beta-lactamase. To investigate beta-lactamase(s) of M. catarrhalis at the molecular level, the BRO-1 beta-lactamase gene (bla) was isolated as part of a 4,223-bp HindIII fragment. Sequence analysis indicated that bla encodes a polypeptide of 314 amino acid residues. Insertional inactivation of bla in M. catarrhalis resulted in complete abrogation of beta-lactamase production and ampicillin

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Luke, Nicole R., Amy J. Howlett, Jianqiang Shao, and Anthony A. Campagnari. "Expression of Type IV Pili by Moraxella catarrhalis Is Essential for Natural Competence and Is Affected by Iron Limitation." Infection and Immunity 72, no. 11 (November 2004): 6262–70. http://dx.doi.org/10.1128/iai.72.11.6262-6270.2004.

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ABSTRACT Type IV pili, filamentous surface appendages primarily composed of a single protein subunit termed pilin, play a crucial role in the initiation of disease by a wide range of pathogenic bacteria. Although previous electron microscopic studies suggested that pili might be present on the surface of Moraxella catarrhalis isolates, detailed molecular and phenotypic analyses of these structures have not been reported to date. We identified and cloned the M. catarrhalis genes encoding PilA, the major pilin subunit, PilQ, the outer membrane secretin through which the pilus filament is extrude

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14

de Vries, Stefan P. W., Hester J. Bootsma, John P. Hays, and Peter W. M. Hermans. "Molecular Aspects of Moraxella catarrhalis Pathogenesis." Microbiology and Molecular Biology Reviews 73, no. 3 (September 2009): 389–406. http://dx.doi.org/10.1128/mmbr.00007-09.

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SUMMARY In recent years, Moraxella catarrhalis has established its position as an important human mucosal pathogen, no longer being regarded as just a commensal bacterium. Further, current research in the field has led to a better understanding of the molecular mechanisms involved in M. catarrhalis pathogenesis, including mechanisms associated with cellular adherence, target cell invasion, modulation of the host's immune response, and metabolism. Additionally, in order to be successful in the host, M. catarrhalis has to be able to interact and compete with the commensal flora and overcome stre

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Aiswariya, Alex, Kundoly Velayudhan Suseela, and Das Subi. "Prevalence of Moraxella catarrhalis in patients of lower respiratory tract infection with underlying risk factors." International Journal of Advances in Medicine 4, no. 2 (March 23, 2017): 442. http://dx.doi.org/10.18203/2349-3933.ijam20171038.

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Background: Moraxella catarrhalis is a Gram-negative diplococcus, commonly found as a normal flora in the human upper respiratory tract. Recently, M. catarrhalis has emerged as an important and common human respiratory tract pathogen. This study was aimed to determine the rate of isolation of M. Catarrhalis in patients attending a tertiary care hospital with lower respiratory tract infection (LRTI), antibiotic susceptibility pattern and predisposing factors responsible for their infection.Methods: A prospective study was carried out in 1001 lower respiratory specimens from patients (above 20 y

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Ruckdeschel, Elizabeth A., Charmaine Kirkham, Alan J. Lesse, Zihua Hu, and Timothy F. Murphy. "Mining the Moraxella catarrhalis Genome: Identification of Potential Vaccine Antigens Expressed during Human Infection." Infection and Immunity 76, no. 4 (January 28, 2008): 1599–607. http://dx.doi.org/10.1128/iai.01253-07.

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ABSTRACT Moraxella catarrhalis is an important cause of respiratory infections in adults and otitis media in children. Developing an effective vaccine would reduce the morbidity, mortality, and costs associated with such infections. An unfinished genome sequence of a strain of M. catarrhalis available in the GenBank database was analyzed, and open reading frames predicted to encode potential vaccine candidates were identified. Three genes encoding proteins having molecular masses of approximately 22, 75, and 78 kDa (designated Msp [Moraxella surface proteins]) (msp22, msp75, and msp78, respect

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Furano, Kristin, and Anthony A. Campagnari. "Inactivation of the Moraxella catarrhalis 7169 Ferric Uptake Regulator Increases Susceptibility to the Bactericidal Activity of Normal Human Sera." Infection and Immunity 71, no. 4 (April 2003): 1843–48. http://dx.doi.org/10.1128/iai.71.4.1843-1848.2003.

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ABSTRACT Moraxella catarrhalis is a strict human pathogen and a significant cause of respiratory disease and otitis media. In direct response to these infections, research efforts have focused primarily on the identification of potential vaccine targets. The general biology of M. catarrhalis, however, including the mechanisms utilized to survive in the human host, remains poorly understood. Previous work has demonstrated that M. catarrhalis expresses iron-repressible proteins, suggesting the presence of iron acquisition systems under the control of a ferric uptake regulator (Fur). In this stud

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Luke, Nicole R., Simon Allen, Bradford W. Gibson, and Anthony A. Campagnari. "Identification of a 3-Deoxy-d-manno-Octulosonic Acid Biosynthetic Operon in Moraxella catarrhalis and Analysis of a KdsA-Deficient Isogenic Mutant." Infection and Immunity 71, no. 11 (November 2003): 6426–34. http://dx.doi.org/10.1128/iai.71.11.6426-6434.2003.

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ABSTRACT Lipooligosaccharide (LOS), a predominant surface-exposed component of the outer membrane, has been implicated as a virulence factor in the pathogenesis of Moraxella catarrhalis infections. However, the critical steps involved in the biosynthesis and assembly of M. catarrhalis LOS currently remain undefined. In this study, we used random transposon mutagenesis to identify a 3-deoxy-d-manno-octulosonic acid (KDO) biosynthetic operon in M. catarrhalis with the gene order pyrG-kdsA-eno. The lipid A-KDO molecule serves as the acceptor onto which a variety of glycosyl transferases sequentia

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Forsgren, Arne, Marta Brant, Mirela Karamehmedovic, and Kristian Riesbeck. "The Immunoglobulin D-Binding Protein MID from Moraxella catarrhalis Is Also an Adhesin." Infection and Immunity 71, no. 6 (June 2003): 3302–9. http://dx.doi.org/10.1128/iai.71.6.3302-3309.2003.

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ABSTRACT The Moraxella catarrhalis immunoglobulin D (IgD)-binding protein (MID) is a 200-kDa outer membrane protein displaying a unique and specific affinity for human IgD. MID is found in the majority of M. catarrhalis strains. In the present paper, we show that MID-expressing M. catarrhalis strains agglutinate human erythrocytes and bind to type II alveolar epithelial cells. In contrast, M. catarrhalis isolates with low MID expression levels and two mutants deficient in MID, but with readily detectable UspA1 expression, do not agglutinate erythrocytes and have a 50% lower adhesive capacity.

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Balder, Rachel, Thomas M. Krunkosky, Chi Q. Nguyen, Lacey Feezel, and Eric R. Lafontaine. "Hag Mediates Adherence of Moraxella catarrhalis to Ciliated Human Airway Cells." Infection and Immunity 77, no. 10 (August 10, 2009): 4597–608. http://dx.doi.org/10.1128/iai.00212-09.

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ABSTRACT Moraxella catarrhalis is a human pathogen causing otitis media in infants and respiratory infections in adults, particularly patients with chronic obstructive pulmonary disease. The surface protein Hag (also designated MID) has previously been shown to be a key adherence factor for several epithelial cell lines relevant to pathogenesis by M. catarrhalis, including NCIH292 lung cells, middle ear cells, and A549 type II pneumocytes. In this study, we demonstrate that Hag mediates adherence to air-liquid interface cultures of normal human bronchial epithelium (NHBE) exhibiting mucociliar

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Gao, Song, Dabin Ren, Daxin Peng, Wenhong Zhang, Artur Muszyński, Russell W. Carlson, and Xin-Xing Gu. "Late acyltransferase genes lpxX and lpxL jointly contribute to the biological activities of Moraxella catarrhalis." Journal of Medical Microbiology 62, no. 6 (June 1, 2013): 807–12. http://dx.doi.org/10.1099/jmm.0.056846-0.

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Lipo-oligosaccharide (LOS) is a major surface component and virulence factor of the human respiratory pathogen Moraxella catarrhalis. Two late acyltransferase genes, lpxX and lpxL, have been identified involved in the incorporation of acyloxyacyl-linked secondary acyl chains into lipid A during M. catarrhalis LOS biosynthesis. In this study, a double mutant with a deletion of both the lpxX and lpxL genes in M. catarrhalis strain O35E was constructed and named O35ElpxXL. Structural analysis of lipid A showed that the O35ElpxXL mutant lacked two decanoic acids (10 : 0) and one dodecanoic (lauric

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Ndiaye, Aissatou Geuye, Cheikh Saadbou Boye, Edwige Hounkponou, Fatou Bintou Gueye, and Aida Badiane. "Antimicrobial susceptibility of select respiratory tract pathogens in Dakar, Senegal." Journal of Infection in Developing Countries 3, no. 09 (October 22, 2009): 660–66. http://dx.doi.org/10.3855/jidc.20.

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Background : Haemophilus influenzae, Moraxella catarrhalis, Streptococcus pyogenes, and Streptococcus pneumoniae are the most common causative agents of respiratory tract infections (RTIs). The increase in resistance to current antibacterial agents highlights the need to monitor the resistance pattern of these bacterial pathogens. Methodology: In this study, we assessed the antibacterial susceptibility of these pathogens causing respiratory tract infections in Dakar, Senegal, during 2007-2008. A total of 290 bacterial isolates (75 H. influenzae, 10 M. catarrhalis, 105 S. pneumoniae, and 100 S.

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Luke, Nicole R., Thomas A. Russo, Neal Luther, and Anthony A. Campagnari. "Use of an Isogenic Mutant Constructed inMoraxella catarrhalis To Identify a Protective Epitope of Outer Membrane Protein B1 Defined by Monoclonal Antibody 11C6." Infection and Immunity 67, no. 2 (February 1, 1999): 681–87. http://dx.doi.org/10.1128/iai.67.2.681-687.1999.

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ABSTRACT Moraxella catarrhalis-induced otitis media continues to be a significant cause of infection in young children, prompting increased efforts at identifying effective vaccine antigens. We have previously demonstrated that M. catarrhalis expresses specific outer membrane proteins (OMPs) in response to iron limitation and that this organism can utilize transferrin and lactoferrin for in vitro growth. One of these proteins, which binds human transferrin, is OMP B1. As the human host presents a naturally iron-limited environment, proteins, like OMP B1, which are expressed in response to this

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Yano, Hisakazu, Mitsuko Suetake, Akio Kuga, Kazuhiko Irinoda, Ryoichi Okamoto, Toshimitsu Kobayashi, and Matsuhisa Inoue. "Pulsed-Field Gel Electrophoresis Analysis of Nasopharyngeal Flora in Children Attending a Day Care Center." Journal of Clinical Microbiology 38, no. 2 (2000): 625–29. http://dx.doi.org/10.1128/jcm.38.2.625-629.2000.

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To investigate how bacterial pathogens spread from child to child in a day care center, we monitored six children, two boys and four girls, born between August 1995 and November 1997, attending a day care center and analyzed nasopharyngeal samples from them using pulsed-field gel electrophoresis (PFGE). We obtained nasopharyngeal cultures from all of the affected children and almost all of the unaffected children between September 1998 and March 1999 after some children presented simultaneously with purulent rhinorrhea. Moreover, when a child was found to have acute otitis media, nasopharyngea

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Шмыленко, Влада, Vlada Shmylenko, Альбина Бондаренко, Albina Bondarenko, Ольга Троценко, Olga Trotsenko, Вячеслав Туркутюков, and Vyacheslav Turkutyukov. "FREQUENCY OF DETECTION OF MORAXELLA CATARRHALIS IN CHILDREN WITH A RECURRENT COURSE OF RESPIRATORY DISEASES IN KHABAROVSK CITY DURING 2016-2017." Bulletin physiology and pathology of respiration 1, no. 68 (June 7, 2018): 52–56. http://dx.doi.org/10.12737/article_5b18b82fc43524.59761242.

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The aim of the study was to evaluate the Moraxella catarrhalis nasopharyngeal carriage prevalence in children of different age groups with a recurrent course of respiratory diseases and perform a comparative analysis of bacterial carriage levels as well as peculiarities of within-year distribution of nasopharyngeal carriage in 2016-2017 years. Bacteriological assessment was performed for 1769 children aged 0 to 14 years old including 1082 children examined in 2016 and 687 children examined in 2017. During the two years of observation the average level of M. catarrhalis carriage for the entire

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Murphy, Timothy F., Aimee L. Brauer, Christoph Aebi, and Sanjay Sethi. "Antigenic Specificity of the Mucosal Antibody Response to Moraxella catarrhalis in Chronic Obstructive Pulmonary Disease." Infection and Immunity 73, no. 12 (December 2005): 8161–66. http://dx.doi.org/10.1128/iai.73.12.8161-8166.2005.

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ABSTRACT Moraxella catarrhalis is an important human mucosal pathogen causing otitis media in children and lower respiratory tract infection in adults with chronic obstructive pulmonary disease (COPD). Little is known about the mucosal antibody response to M. catarrhalis in adults with COPD. In this study, 10 pairs of well-characterized sputum supernatant samples from adults with COPD who had acquired and subsequently cleared M. catarrhalis from their respiratory tracts were studied in detail in an effort to begin to elucidate potentially protective immune responses. Flow cytometry analysis wa

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Hu, Wei-Gang, Jing Chen, James F. Battey, and Xin-Xing Gu. "Enhancement of Clearance of Bacteria from Murine Lungs by Immunization with Detoxified Lipooligosaccharide fromMoraxella catarrhalis Conjugated to Proteins." Infection and Immunity 68, no. 9 (September 1, 2000): 4980–85. http://dx.doi.org/10.1128/iai.68.9.4980-4985.2000.

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ABSTRACT Moraxella catarrhalis strain 25238 detoxified lipooligosaccharide (dLOS)-protein conjugates induced a significant rise of bactericidal anti-LOS antibodies in animals. This study reports the effect of active or passive immunization with the conjugates or their antiserum on pulmonary clearance of M. catarrhalis in an aerosol challenge mouse model. Mice were injected subcutaneously with dLOS-tetanus toxoid (dLOS-TT), dLOS–high-molecular-weight proteins (dLOS-HMP) from nontypeable Haemophilus influenzae(NTHi), or nonconjugated materials in Ribi adjuvant and then challenged with M. catarrh

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Luke, Nicole R., Richard J. Karalus, and Anthony A. Campagnari. "Inactivation of the Moraxella catarrhalis Superoxide Dismutase SodA Induces Constitutive Expression of Iron-Repressible Outer Membrane Proteins." Infection and Immunity 70, no. 4 (April 2002): 1889–95. http://dx.doi.org/10.1128/iai.70.4.1889-1895.2002.

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ABSTRACT Many pathogens produce one or more superoxide dismutases (SODs), enzymes involved in the detoxification of endogenous and exogenous reactive oxygen species that are encountered during the infection process. One detectable cytoplasmic SOD was identified in the human mucosal pathogen Moraxella catarrhalis, and the gene responsible for the SOD activity, sodA, was isolated from a recent pediatric clinical isolate (strain 7169). Sequence analysis of the cloned M. catarrhalis 7169 DNA fragment revealed an open reading frame of 618 bp encoding a polypeptide of 205 amino acids with 48 to 67%

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Faden, Howard, Jung J. Hong, and Nickesh Pahade. "Immune Response to Moraxella Catarrhalis in Children with Otitis Media: Opsonophagocytosis with Antigen-Coated Latex Beads." Annals of Otology, Rhinology & Laryngology 103, no. 7 (July 1994): 522–24. http://dx.doi.org/10.1177/000348949410300704.

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Opsonic antibody activity against Moraxella catarrhalis was determined in sera from children with otitis media. The antibody was determined with a new assay utilizing outer membrane antigen-coated latex beads. Antigen-coated beads opsonized in heat-inactivated pooled human serum phagocytosed 47.5 ± 36.1 beads per 100 neutrophils compared to 15.6 ± 10.2 beads per 100 neutrophils opsonized in hypogammaglobulinemic serum (p < .025). Antigen-coated beads opsonized in homologous sera from 11 children with M catarrhalis otitis media demonstrated increased opsonic activity in convalescent sera (34

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Liu, Dai-Fang, John C. McMichael, and Steven M. Baker. "Moraxella catarrhalis Outer Membrane Protein CD Elicits Antibodies That Inhibit CD Binding to Human Mucin and Enhance Pulmonary Clearance of M. catarrhalis in a Mouse Model." Infection and Immunity 75, no. 6 (April 2, 2007): 2818–25. http://dx.doi.org/10.1128/iai.00074-07.

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ABSTRACT The outer membrane protein CD of Moraxella catarrhalis is considered to be a potential vaccine antigen against Moraxella infection. We purified the native CD from isolate O35E, administered it to mice, and detected considerable titers of anti-CD antibodies. Anti-CD sera were cross-reactive towards six different M. catarrhalis isolates and promoted bacterial clearance of O35E in a pulmonary challenge model. To circumvent the difficulty of generating large quantities of CD from M. catarrhalis for vaccine use, the CD gene from O35E was cloned into Escherichia coli, and the recombinant CD

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Murphy, Timothy F., Aimee L. Brauer, Norine Yuskiw, Erin R. McNamara, and Charmaine Kirkham. "Conservation of Outer Membrane Protein E among Strains of Moraxella catarrhalis." Infection and Immunity 69, no. 6 (June 1, 2001): 3576–80. http://dx.doi.org/10.1128/iai.69.6.3576-3580.2001.

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ABSTRACT Outer membrane protein E (OMP E) is a 50-kDa protein ofMoraxella catarrhalis which has several features that suggest that the protein may be an effective vaccine antigen. To assess the conservation of OMP E among strains of M. catarrhalis,22 isolates were studied with eight monoclonal antibodies which recognize epitopes on different regions of the protein. Eighteen of 22 strains were reactive with all eight antibodies. The sequences ofompE from 16 strains of M. catarrhalis were determined, including the 4 strains which were nonreactive with selected monoclonal antibodies. Analysis of

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Wang, Wei, Larry Reitzer, David A. Rasko, Melanie M. Pearson, Robert J. Blick, Cassie Laurence, and Eric J. Hansen. "Metabolic Analysis of Moraxella catarrhalis and the Effect of Selected In Vitro Growth Conditions on Global Gene Expression." Infection and Immunity 75, no. 10 (July 9, 2007): 4959–71. http://dx.doi.org/10.1128/iai.00073-07.

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ABSTRACT The nucleotide sequence from the genome of Moraxella catarrhalis ATCC 43617 was annotated and used both to assess the metabolic capabilities and limitations of this bacterium and to design probes for a DNA microarray. An absence of gene products for utilization of exogenous carbohydrates was noteworthy and could be correlated with published phenotypic data. Gene products necessary for aerobic energy generation were present, as were a few gene products generally ascribed to anaerobic systems. Enzymes for synthesis of all amino acids except proline and arginine were present. M. catarrha

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Lafontaine, Eric R., David Wall, Serena L. Vanlerberg, Haig Donabedian, and Darren D. Sledjeski. "Moraxella catarrhalis Coaggregates with Streptococcus pyogenes and Modulates Interactions of S. pyogenes with Human Epithelial Cells." Infection and Immunity 72, no. 11 (November 2004): 6689–93. http://dx.doi.org/10.1128/iai.72.11.6689-6693.2004.

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ABSTRACT The pathogens Streptococcus pyogenes and Moraxella catarrhalis colonize overlapping regions of the human nasopharynx. We have found that M. catarrhalis can dramatically increase S. pyogenes adherence to human epithelial cells and that species-specific coaggregation of these bacteria correlates with this enhanced adherence.

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Easton, Donna M., Elke Maier, Roland Benz, A. Ruth Foxwell, Allan W. Cripps, and Jennelle M. Kyd. "Moraxella catarrhalis M35 Is a General Porin That Is Important for Growth under Nutrient-Limiting Conditions and in the Nasopharynges of Mice." Journal of Bacteriology 190, no. 24 (October 17, 2008): 7994–8002. http://dx.doi.org/10.1128/jb.01039-08.

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ABSTRACT Moraxella catarrhalis is a gram-negative respiratory pathogen that is an important causative agent for otitis media and exacerbations of chronic obstructive pulmonary disease. We have previously predicted the outer membrane protein M35 to be a general porin, and in the current study, we have investigated the function of M35 and its importance for survival of M. catarrhalis in vivo. Lipid bilayer experiments reveal that refolded M35 functions as a channel that is typical of gram-negative bacterial porins. M35 forms wide and water-filled channels with a single-channel conductance of abo

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Hu, Wei-Gang, Jing Chen, John C. McMichael, and Xin-Xing Gu. "Functional Characteristics of a Protective Monoclonal Antibody against Serotype A and C Lipooligosaccharides from Moraxella catarrhalis." Infection and Immunity 69, no. 3 (March 1, 2001): 1358–63. http://dx.doi.org/10.1128/iai.69.3.1358-1363.2001.

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ABSTRACT A monoclonal antibody (MAb), designated MAb 8E7 (immunoglobulin G3), specific for Moraxella catarrhalislipooligosaccharide (LOS) was evaluated for its functional activity in vitro and in a mouse model of colonization. Enzyme-linked immunosorbent assay (ELISA) demonstrated that the MAb 8E7 could be prepared to a high titer against LOS of the homologous strain 035E, and that it had bactericidal activity. MAb 8E7 reacted with M. catarrhalisserotype A and C LOSs but not serotype B LOS, as measured by ELISA and Western blotting. On the basis of published structures of LOSs, this suggests t

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Myers, Lisa E., Yan-ping Yang, Run-pan Du, Qijun Wang, Robin E. Harkness, Anthony B. Schryvers, Michel H. Klein, and Sheena M. Loosmore. "The Transferrin Binding Protein B of Moraxella catarrhalis Elicits Bactericidal Antibodies and Is a Potential Vaccine Antigen." Infection and Immunity 66, no. 9 (September 1, 1998): 4183–92. http://dx.doi.org/10.1128/iai.66.9.4183-4192.1998.

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ABSTRACT The transferrin binding protein genes (tbpA andtbpB) from two strains of Moraxella catarrhalis have been cloned and sequenced. The genomic organization of the M. catarrhalistransferrin binding protein genes is unique among known bacteria in that tbpA precedes tbpB and there is a third gene located between them. The deduced sequences of the M. catarrhalis TbpA proteins from two strains were 98% identical, while those of the TbpB proteins from the same strains were 63% identical and 70% similar. The third gene, tentatively called orf3, encodes a protein of approximately 58 kDa that is 9

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Gao, Ya, Jumin Lee, Göran Widmalm, and Wonpil Im. "Preferred conformations of lipooligosaccharides and oligosaccharides of Moraxella catarrhalis." Glycobiology 30, no. 2 (October 16, 2019): 86–94. http://dx.doi.org/10.1093/glycob/cwz086.

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Abstract Moraxella catarrhalis (M. catarrhalis) is a pathogenic gram-negative bacterium that causes otitis media and sinusitis in children. Three major serotypes A, B and C are identified to account for approximately 95% of the clinical isolates. Understanding the conformational properties of different serotypes of M. catarrhalis provides insights into antigenic determinants. In this work, all-atom molecular dynamics simulations were conducted for M. catarrhalis lipooligosaccharide (LOS) bilayer systems and oligosaccharides (OS) in water solution to investigate the conformational similarities

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Schwingel, Johanna M., Katie J. Edwards, Andrew D. Cox, Hussein Masoud, James C. Richards, Frank St. Michael, Carmen D. Tekwe, Sanjay Sethi, Timothy F. Murphy, and Anthony A. Campagnari. "Use of Moraxella catarrhalis Lipooligosaccharide Mutants To Identify Specific Oligosaccharide Epitopes Recognized by Human Serum Antibodies." Infection and Immunity 77, no. 10 (August 3, 2009): 4548–58. http://dx.doi.org/10.1128/iai.00294-09.

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ABSTRACT Moraxella catarrhalis is a causative agent of otitis media in children and lower respiratory tract infections in adults suffering from chronic obstructive pulmonary disease (COPD). This strict human pathogen continues to be a significant cause of disease in this broad spectrum of patients because there is no available vaccine. Although numerous putative vaccine antigens have been described, little is known about the human immune response to M. catarrhalis infection in vivo. Human serum antibodies are directed at a number of surface proteins, and lipooligosaccharides (LOS) and detoxifi

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Pearson, Melanie M., Cassie A. Laurence, Sarah E. Guinn, and Eric J. Hansen. "Biofilm Formation by Moraxella catarrhalis In Vitro: Roles of the UspA1 Adhesin and the Hag Hemagglutinin." Infection and Immunity 74, no. 3 (March 2006): 1588–96. http://dx.doi.org/10.1128/iai.74.3.1588-1596.2006.

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ABSTRACT Mutant analysis was used to identify Moraxella catarrhalis gene products necessary for biofilm development in a crystal violet-based assay involving 24-well tissue culture plates. The wild-type M. catarrhalis strains that formed the most extensive biofilms in this system proved to be refractory to transposon mutagenesis, so an M. catarrhalis strain was constructed that was both able to form biofilms in vitro and amenable to transposon mutagenesis. Chromosomal DNA from the biofilm-positive strain O46E was used to transform the biofilm-negative strain O35E; transformants able to form bi

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Riesbeck, Kristian, Thuan Tong Tan, and Arne Forsgren. "MID and UspA1/A2 of the human respiratory pathogen Moraxella catarrhalis, and interactions with the human host as basis for vaccine development." Acta Biochimica Polonica 53, no. 3 (September 9, 2006): 445–56. http://dx.doi.org/10.18388/abp.2006_3315.

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Moraxella catarrhalis IgD-binding protein MID is a 200 kDa autotransporter protein that exists as a oligomer and is governed at the transcriptional level. The majority of M. catarrhalis clinical isolates expresses MID. Two functional domains have been attributed to MID; MID764-913 functions as an adhesin and promotes the bacteria to attach to epithelial cells, whereas the IgD-binding domain is located within MID962-1200. In parallel, MID is stimulatory for B lymphocytes through the IgD B cell receptor. M. catarrhalis ubiquitous surface proteins A1 and A2 (UspA1/A2) are multifunctional outer me

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Bullard, Brian, Serena L. Lipski, and Eric R. Lafontaine. "Hag Directly Mediates the Adherence of Moraxella catarrhalis to Human Middle Ear Cells." Infection and Immunity 73, no. 8 (August 2005): 5127–36. http://dx.doi.org/10.1128/iai.73.8.5127-5136.2005.

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ABSTRACT Moraxella catarrhalis is a human pathogen that causes otitis media in young children and lung infections in patients with chronic obstructive pulmonary disease. In this study, the role of the surface protein Hag in the adherence of multiple M. catarrhalis strains was examined. The hag genes of four clinical isolates were disrupted with a spectinomycin resistance cassette, and the binding of isogenic mutants to primary cultures of human middle ear epithelial cells (HMEE), as well as A549 pneumocytes, was measured. These experiments revealed that the attachment of most mutants to both c

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Citron, Diane M., Yumi A. Warren, Kerin L. Tyrrell, and Ellie J. C. Goldstein. "Activity of Ceftaroline against Aerobic Gram-Positive and Gram-Negative Pathogens: Effect of Test Method Variability." ISRN Microbiology 2011 (November 17, 2011): 1–5. http://dx.doi.org/10.5402/2011/787290.

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Ceftaroline is a new cephalosporin with bactericidal activity against methicillin-resistant S. aureus (MRSA) as well as gram-negative pathogens. Variations of in vitro test conditions were found to affect ceftaroline activity, with 5% NaCl inhibiting growth and/or reducing the minimum inhibitory concentrations (MICs) for E. coli, K. pneumoniae, M. catarrhalis, H. influenzae, and streptococci, while an inoculum of 106 CFU/mL raised MICs of some E. coli, K. pneumoniae, and M. catarrhalis strains.

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Brueggemann, Angela B., Gary V. Doern, Holly K. Huynh, Elizabeth M. Wingert, and Paul R. Rhomberg. "In Vitro Activity of ABT-773, a New Ketolide, against Recent Clinical Isolates of Streptococcus pneumoniae, Haemophilus influenzae, andMoraxella catarrhalis." Antimicrobial Agents and Chemotherapy 44, no. 2 (February 1, 2000): 447–49. http://dx.doi.org/10.1128/aac.44.2.447-449.2000.

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ABSTRACT The in vitro activity of ABT-773 was evaluated againstStreptococcus pneumoniae, Haemophilus influenzae, and Moraxella catarrhalis isolates. ABT-773 was the most active antimicrobial tested against S. pneumoniae. ABT-773 and azithromycin were equivalent in activity against H. influenzae and M. catarrhalis and more active than either clarithromycin or erythromycin.

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Brook, Itzhak, та Alan E. Gober. "Increased recovery of Moraxella catarrhalis and Haemophilus influenzae in association with group A β-haemolytic streptococci in healthy children and those with pharyngo-tonsillitis". Journal of Medical Microbiology 55, № 8 (1 серпня 2006): 989–92. http://dx.doi.org/10.1099/jmm.0.46325-0.

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The inflamed tonsils harbour numerous types of bacteria, alone or in combination with group A β-haemolytic streptococci (GABHS). The cohabitation of the tonsils by GABHS and certain other bacterial species may contribute to the inflammatory process and the failure of penicillin therapy. This study evaluated the recovery of Moraxella catarrhalis, Haemophilus influenzae, Staphylococcus aureus and Streptococcus pneumoniae in association with GABHS in healthy children and those with acute pharyngo-tonsillitis (APT). Pharyngo-tonsillar cultures were obtained from 548 children with APT and 866 healt

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Attia, Ahmed S., Sanjay Ram, Peter A. Rice, and Eric J. Hansen. "Binding of Vitronectin by the Moraxella catarrhalis UspA2 Protein Interferes with Late Stages of the Complement Cascade." Infection and Immunity 74, no. 3 (March 2006): 1597–611. http://dx.doi.org/10.1128/iai.74.3.1597-1611.2006.

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ABSTRACT Many Moraxella catarrhalis strains are resistant to the bactericidal activity of normal human serum (NHS). The UspA2 protein of the serum-resistant strain O35E has previously been shown to be directly involved in conferring serum resistance on this strain. Testing of 11 additional serum-resistant M. catarrhalis wild-type isolates and their uspA1 and uspA2 mutants showed that the uspA1 mutants of all 11 strains were consistently serum resistant and that the uspA2 mutants of these same 11 strains were always serum sensitive. Analysis of complement deposition on four different serum-resi

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Tan, Thuan Tong, Jens Jørgen Christensen, Morten Hanefeld Dziegiel, Arne Forsgren, and Kristian Riesbeck. "Comparison of the Serological Responses to Moraxella catarrhalis Immunoglobulin D-Binding Outer Membrane Protein and the Ubiquitous Surface Proteins A1 and A2." Infection and Immunity 74, no. 11 (September 11, 2006): 6377–86. http://dx.doi.org/10.1128/iai.00702-06.

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ABSTRACT Moraxella catarrhalis immunoglobulin D-binding protein (MID) is a complex antigen with unique immunoglobulin D (IgD)-binding, adhesion, and hemagglutination properties. Previous studies have shown that antibodies raised against MID764-913 in rabbits inhibited M. catarrhalis adhesion to human alveolar epithelial cells, and immunization with MID764-913 resulted in an increased pulmonary clearance in a murine model. Strong immune responses against MID have also consistently been shown in humans. Here, the MID-specified IgG responses were compared to those of ubiquitous surface proteins A

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Soltan, Mohamed A., Nada Elbassiouny, Helmy Gamal, Eslam B. Elkaeed, Refaat A. Eid, Muhammad Alaa Eldeen, and Ahmed A. Al-Karmalawy. "In Silico Prediction of a Multitope Vaccine against Moraxella catarrhalis: Reverse Vaccinology and Immunoinformatics." Vaccines 9, no. 6 (June 18, 2021): 669. http://dx.doi.org/10.3390/vaccines9060669.

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Moraxella catarrhalis (M. catarrhalis) is a Gram-negative bacterium that can cause serious respiratory tract infections and middle ear infections in children and adults. M. catarrhalis has demonstrated an increasing rate of antibiotic resistance in the last few years, thus development of an effective vaccine is a major health priority. We report here a novel designed multitope vaccine based on the mapped epitopes of the vaccine candidates filtered out of the whole proteome of M. catarrhalis. After analysis of 1615 proteins using a reverse vaccinology approach, only two proteins (outer membrane

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Abdolrasouli, A., A. Amin, M. Baharsefat, A. Roushan, and Y. Hemmati. "Moraxella catarrhalis associated with acute urethritis imitating gonorrhoea acquired by oral–genital contact." International Journal of STD & AIDS 18, no. 8 (August 1, 2007): 579–80. http://dx.doi.org/10.1258/095646207781439775.

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A case of heterosexual transmission of Moraxella catarrhalis by fellatio, which resulted in acute purulent urethritis mimicking gonorrhoea in the male partner, is described. In male patients with urethritis due to M. catarrhalis, orogenital contact with a sexual partner carrying the organism in his/her oropharynx is the probable route of transmission.

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Otsuka, Taketo, Charmaine Kirkham, Antoinette Johnson, Megan M. Jones, and Timothy F. Murphy. "Substrate Binding Protein SBP2 of a Putative ABC Transporter as a Novel Vaccine Antigen of Moraxella catarrhalis." Infection and Immunity 82, no. 8 (June 9, 2014): 3503–12. http://dx.doi.org/10.1128/iai.01832-14.

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ABSTRACTMoraxella catarrhalisis a common respiratory tract pathogen that causes otitis media in children and infections in adults with chronic obstructive pulmonary disease. Since the introduction of the pneumococcal conjugate vaccines with/without protein D of nontypeableHaemophilus influenzae,M. catarrhalishas become a high-priority pathogen in otitis media. For the development of antibacterial vaccines and therapies, substrate binding proteins of ATP-binding cassette transporters are important targets. In this study, we identified and characterized a substrate binding protein, SBP2, ofM. ca

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NAVNE, J. E., M. L. BØRRESEN, H. C. SLOTVED, M. ANDERSSON, M. MELBYE, K. LADEFOGED, and A. KOCH. "Nasopharyngeal bacterial carriage in young children in Greenland: a population at high risk of respiratory infections." Epidemiology and Infection 144, no. 15 (July 13, 2016): 3226–36. http://dx.doi.org/10.1017/s0950268816001461.

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SUMMARYThe incidence of childhood respiratory infections in Greenland is among the highest globally. We performed a population-based study of 352 Greenlandic children aged 0–6 years aiming to describe rates and risk factors for carriage of four key bacteria associated with respiratory infections, their antimicrobial susceptibility and inter-bacterial associations. Nasopharyngeal swabs were tested for Streptococcus pneumoniae grouped by serotypes included (VT) or not included (NVT) in the 13-valent pneumococcal conjugate vaccine, non-typable Haemophilus influenzae (NTHi), Staphylococcus aureus

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