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Journal articles on the topic 'Catarrhalis'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Yang, Min, Antoinette Johnson, and Timothy F. Murphy. "Characterization and Evaluation of theMoraxella catarrhalisOligopeptide Permease A as a Mucosal Vaccine Antigen." Infection and Immunity 79, no. 2 (December 6, 2010): 846–57. http://dx.doi.org/10.1128/iai.00314-10.

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ABSTRACTMoraxella catarrhalisis a common cause of otitis media in children and of lower respiratory tract infections in adults with chronic obstructive pulmonary disease; therefore, these two groups would benefit from a vaccine to preventM. catarrhalisinfections. A genome mining approach for vaccine antigens identified oligopeptide permease protein A (OppA), an oligopeptide binding protein of an apparent oligopeptide transport system. Analysis of theoppAgene by PCR and sequence analysis revealed that OppA is highly conserved among clinical isolates ofM. catarrhalis. Recombinant OppA was expres

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2

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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3

Riou, J. Y., and M. Guibourdenche. "Branhamella catarrhalis." Drugs 31, Supplement 3 (1986): 1–6. http://dx.doi.org/10.2165/00003495-198600313-00003.

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4

SHEFF, BARBARA. "Moraxella Catarrhalis." Nursing 33, no. 1 (January 2003): 81. http://dx.doi.org/10.1097/00152193-200301000-00055.

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5

Otsuka, Taketo, Charmaine Kirkham, Aimee Brauer, Mary Koszelak-Rosenblum, Michael G. Malkowski, and Timothy F. Murphy. "The Vaccine Candidate Substrate Binding Protein SBP2 Plays a Key Role in Arginine Uptake, Which Is Required for Growth of Moraxella catarrhalis." Infection and Immunity 84, no. 2 (November 23, 2015): 432–38. http://dx.doi.org/10.1128/iai.00799-15.

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Moraxella catarrhalisis an exclusively human pathogen that is an important cause of otitis media in children and lower respiratory tract infections in adults with chronic obstructive pulmonary disease. A vaccine to preventM. catarrhalisinfections would have an enormous global impact in reducing morbidity resulting from these infections. Substrate binding protein 2 (SBP2) of an ABC transporter system has recently been identified as a promising vaccine candidate antigen on the bacterial surface ofM. catarrhalis. In this study, we showed that SBP1, -2, and -3 individually bind different basic ami

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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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7

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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Igic, Marija, Ljiljana Kesic, Radmila Obradovic, Gordana Filipovic, Branislava Stojkovic, and Kosta Todorovic. "Comparative clinical evaluation of the therapeutic effects of low-level laser and hyaluronic acid on gingivitis catarrhalis in children." Vojnosanitetski pregled 77, no. 7 (2020): 736–39. http://dx.doi.org/10.2298/vsp171207118i.

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Background/Aim. Gingivitis catarrhalis is the most common disease of the oral mucosa in children, representing an inflammation of the gingiva of an exudative nature. The aim of this study was to evaluate the effectiveness of low-level laser therapy and hyaluronic acid therapy on gingivitis catarrhalis in children using the appropriate clinical parameters. Methods. The study involved 100 children with permanent dentition in whom gingivitis catarrhalis had been diagnosed. The examinees were divided into two groups: the group I consisting of patients with gingival inflammation (50 examinees) in w

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9

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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11

Lierde, Stefaan Van, Jennifer M. Puck, Joseph M. Campos, and Stanley A. Plotkin. "BRANHAMELLA CATARRHALIS SEPSIS." Pediatric Infectious Disease Journal 4, no. 5 (September 1985): 562. http://dx.doi.org/10.1097/00006454-198509000-00031.

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12

Chan, Daisy. "MORAXELLA CATARRHALIS KERATOCONJUNCTIVITIS." Optometry and Vision Science 78, SUPPLEMENT (December 2001): 186. http://dx.doi.org/10.1097/00006324-200112001-00305.

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13

Garcia-Garrote, Fernando, Ana Menasalvas, Luciá Martínez-Sánchez, Emilia Cercenado, Luis Alcalá, and Emilio Bouza. "Moraxella catarrhalis bacteremia." Clinical Microbiology Newsletter 19, no. 23 (December 1997): 183–84. http://dx.doi.org/10.1016/s0196-4399(00)89191-6.

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14

Sadjadi, Seyed-Ali, Paz Obedoza, and Pawan Annamarju. "Moraxella Catarrhalis peritonitis." American Journal of Case Reports 13 (2012): 19–21. http://dx.doi.org/10.12659/ajcr.882358.

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15

Heidemann, David G., Eduardo Alfonso, Richard K. Forster, Saul Ullman, Simon P. Holland, Alan Mendelsohn, and Darlene Miller. "Branhamella catarrhalis Keratitis." American Journal of Ophthalmology 103, no. 4 (April 1987): 576–81. http://dx.doi.org/10.1016/s0002-9394(14)74282-5.

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16

ROMBERGER, JAMES A., ELLEN R. WALD, and PETER F. WRIGHT. "Branhamella catarrhalis Conjunctivitis." Southern Medical Journal 80, no. 7 (July 1987): 926–28. http://dx.doi.org/10.1097/00007611-198707000-00032.

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17

Verghese, Abraham, and Steven L. Berk. "Moraxella (Branhamella) catarrhalis." Infectious Disease Clinics of North America 5, no. 3 (September 1991): 523–38. http://dx.doi.org/10.1016/s0891-5520(20)30404-9.

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18

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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19

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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20

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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21

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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22

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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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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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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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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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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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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Paykel, Jacquelyn M. "Moraxella (branhamella) catarrhalis infections." Primary Care Update for OB/GYNS 9, no. 1 (January 2002): 33–35. http://dx.doi.org/10.1016/s1068-607x(01)00099-3.

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Davies, B. I., and F. P. V. Maesen. "BRANHAMELLA CATARRHALIS CHEST INFECTIONS." Lancet 328, no. 8501 (August 1986): 278. http://dx.doi.org/10.1016/s0140-6736(86)92088-x.

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McMichael, John C. "Vaccines for Moraxella catarrhalis." Vaccine 19 (December 2000): S101—S107. http://dx.doi.org/10.1016/s0264-410x(00)00287-5.

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Pugliese, Gina, and Martin S. Favero. "Nosocomial Pathogen: Moraxella catarrhalis." Infection Control & Hospital Epidemiology 23, no. 2 (February 2002): 112. http://dx.doi.org/10.1017/s0195941700084368.

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Ren, Dabin, and Michael E. Pichichero. "Vaccine targets againstMoraxella catarrhalis." Expert Opinion on Therapeutic Targets 20, no. 1 (August 26, 2015): 19–33. http://dx.doi.org/10.1517/14728222.2015.1081686.

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Hager, H., A. Verghese, S. Alvarez, and S. L. Berk. "Branhamella catarrhalis Respiratory Infections." Clinical Infectious Diseases 9, no. 6 (November 1, 1987): 1140–49. http://dx.doi.org/10.1093/clinids/9.6.1140.

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Wallace, Mark R. "Moraxella (Branhamella) catarrhalis Bacteremia." Archives of Internal Medicine 150, no. 6 (June 1, 1990): 1332. http://dx.doi.org/10.1001/archinte.1990.00390180136025.

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Bergren, Robert L. "Branhamella (Moraxella) catarrhalis Endophthalmitis." Archives of Ophthalmology 111, no. 9 (September 1, 1993): 1169. http://dx.doi.org/10.1001/archopht.1993.01090090021009.

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Anezaki, Hiroki, Norihiko Terada, Takahisa Kawamura, and Hanako Kurai. "Moraxella catarrhalis bacteremic pneumonia." IDCases 19 (2020): e00712. http://dx.doi.org/10.1016/j.idcr.2020.e00712.

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Doern, Gary V. "Branhamella catarrhalis: Phenotypic characteristics." American Journal of Medicine 88, no. 5 (May 1990): S33—S35. http://dx.doi.org/10.1016/0002-9343(90)90259-g.

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Kobayashi, Yoshio. "Bacteremic Moraxella catarrhalis pneumonia." Journal of Infection and Chemotherapy 6, no. 1 (2000): 68. http://dx.doi.org/10.1007/s101560050054.

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Dragas, Ana Zlata, and Maria Gubina. "Methicillin-resistant Branhamella catarrhalis." Journal of Hospital Infection 7, no. 3 (May 1986): 308–9. http://dx.doi.org/10.1016/0195-6701(86)90091-5.

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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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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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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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Prates, Mirela C. M., Edwin Tamashiro, José L. Proenca-Modena, Miriã F. Criado, Tamara H. Saturno, Anibal S. Oliveira, Guilherme P. Buzatto, et al. "The Relationship between Colonization by Moraxella catarrhalis and Tonsillar Hypertrophy." Canadian Journal of Infectious Diseases and Medical Microbiology 2018 (November 1, 2018): 1–9. http://dx.doi.org/10.1155/2018/5406467.

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We sought to investigate the prevalence of potentially pathogenic bacteria in secretions and tonsillar tissues of children with chronic adenotonsillitis hypertrophy compared to controls. Prospective case-control study comparing patients between 2 and 12 years old who underwent adenotonsillectomy due to chronic adenotonsillar hypertrophy to children without disease. We compared detection of Streptococcus pneumoniae, Haemophilus influenzae, Staphylococcus aureus, Pseudomonas aeruginosa, and Moraxella catarrhalis by real-time PCR in palatine tonsils, adenoids, and nasopharyngeal washes obtained f

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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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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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