- About this Journal ·
- Abstracting and Indexing ·
- Aims and Scope ·
- Article Processing Charges ·
- Articles in Press ·
- Author Guidelines ·
- Bibliographic Information ·
- Citations to this Journal ·
- Contact Information ·
- Editorial Board ·
- Editorial Workflow ·
- Free eTOC Alerts ·
- Publication Ethics ·
- Reviewers Acknowledgment ·
- Submit a Manuscript ·
- Subscription Information ·
- Table of Contents
ISRN Veterinary Science
Volume 2012 (2012), Article ID 802308, 6 pages
Extracellular Proteins of Mycoplasma synoviae
1Centro de Biologia Molecular Estrutural, Departamento de Bioquímica, CCB, Universidade Federal de Santa Catarina, 88040-900 Florianópolis, SC, Brazil
2Embrapa Swine and Poultry Research Center, Animal Health Laboratory, 89700-000 Concordia, SC, Brazil
Received 21 July 2012; Accepted 9 August 2012
Academic Editors: D. Barnard, E. Bártová, and A. Shamay
Copyright © 2012 Manuel Sebastián Rebollo Couto et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
- M. S. Kang, P. Gazdzinski, and S. H. Kleven, “Virulence of recent isolates of Mycoplasma synoviae in turkeys,” Avian Diseases, vol. 46, no. 1, pp. 102–110, 2002.
- S. B. Lockaby, F. J. Hoerr, L. H. Lauerman, and S. H. Kleven, “Pathogenicity of Mycoplasma synoviae in Broiler chickens,” Veterinary Pathology, vol. 35, no. 3, pp. 178–190, 1998.
- F. Dufour-Gesbert, A. Dheilly, C. Marois, and I. Kempf, “Epidemiological study on Mycoplasma synoviae infection in layers,” Veterinary Microbiology, vol. 114, no. 1-2, pp. 148–154, 2006.
- I. Gerchman, I. Lysnyansky, S. Perk, and S. Levisohn, “In vitro susceptibilities to fluoroquinolones in current and archived Mycoplasma gallisepticum and Mycoplasma synoviae isolates from meat-type turkeys,” Veterinary Microbiology, vol. 131, no. 3-4, pp. 266–276, 2008.
- M. Trost, D. Wehmhöner, U. Kärst, G. Dieterich, J. Wehland, and L. Jänsch, “Comparative proteome analysis of secretory proteins from pathogenic and nonpathogenic Listeria species,” Proteomics, vol. 5, no. 6, pp. 1544–1557, 2005.
- S. J. Cordwell, A. S. Nouwens, and B. J. Walsh, “Comparative proteomics of bacterial pathogens,” Proteomics, vol. 1, no. 4, pp. 461–472, 2001.
- P. R. Jungblut, “Proteome analysis of bacterial pathogens,” Microbes and Infection, vol. 3, no. 10, pp. 831–840, 2001.
- A. C. O. Menegatti, C. P. Tavares, J. Vernal, C. S. Klein, L. Huergo, and H. Terenzi, “First partial proteome of the poultry pathogen Mycoplasma synoviae,” Veterinary Microbiology, vol. 145, no. 1-2, pp. 134–141, 2010.
- M. L. Frey, R. P. Hanson, and D. P. Andrson, “A medium for the isolation of avian mycoplasmas,” American Journal of Veterinary Research, vol. 29, no. 11, pp. 2163–2171, 1968.
- J. Jores, J. Meens, F. F. R. Buettner, B. Linz, J. Naessens, and G. F. Gerlach, “Analysis of the immunoproteome of Mycoplasma mycoides subsp. mycoides small colony type reveals immunogenic homologues to other known virulence traits in related Mycoplasma species,” Veterinary Immunology and Immunopathology, vol. 131, no. 3-4, pp. 238–245, 2009.
- S. Naseem, J. Meens, J. Jores et al., “Phage display-based identification and potential diagnostic application of novel antigens from Mycoplasma mycoides subsp. mycoides small colony type,” Veterinary Microbiology, vol. 142, no. 3-4, pp. 285–292, 2010.
- A. S. Kucknoor, V. Mundodi, and J. F. Alderete, “The proteins secreted by Trichomonas vaginalis and vaginal epithelial cell response to secreted and episomally expressed AP65,” Cellular Microbiology, vol. 9, no. 11, pp. 2586–2597, 2007.
- L. A. Bøhle, T. Riaz, W. Egge-Jacobsen et al., “Identification of surface proteins in Enterococcus faecalis V583,” BMC Genomics, vol. 12, article 135, 2011.
- C. L. McGowin, R. A. Spagnuolo, and R. B. Pyles, “Mycoplasma genitalium rapidly disseminates to the upper reproductive tracts and knees of female mice following vaginal inoculation,” Infection and Immunity, vol. 78, no. 2, pp. 726–736, 2010.
- V. G. DelVecchio, J. P. Connolly, T. G. Alefantis et al., “Proteomic profiling and identification of immunodominant spore antigens of Bacillus anthracis, Bacillus cereus, and Bacillus thuringiensis,” Applied and Environmental Microbiology, vol. 72, no. 9, pp. 6355–6363, 2006.
- L. F. Fehri, P. Sirand-Pugnet, G. Gourgues, G. Jan, H. Wróblewski, and A. Blanchard, “Resistance to antimicrobial peptides and stress response in Mycoplasma pulmonis,” Antimicrobial Agents and Chemotherapy, vol. 49, no. 10, pp. 4154–4165, 2005.
- K. Antúnez, M. Anido, J. D. Evans, and P. Zunino, “Secreted and immunogenic proteins produced by the honeybee bacterial pathogen, Paenibacillus larvae,” Veterinary Microbiology, vol. 141, no. 3-4, pp. 385–389, 2010.
- R. L. Berčič, B. Slavec, M. Lavrič et al., “Identification of major immunogenic proteins of Mycoplasma synoviae isolates,” Veterinary Microbiology, vol. 127, no. 1-2, pp. 147–154, 2008.
- E. Izquierdo, P. Horvatovich, E. Marchioni, D. Aoude-Werner, Y. Sanz, and S. Ennahar, “2-DE and MS analysis of key proteins in the adhesion of Lactobacillus plantarum, a first step toward early selection of probiotics based on bacterial biomarkers,” Electrophoresis, vol. 30, no. 6, pp. 949–956, 2009.
- W. Xolalpa, A. J. Vallecillo, M. Lara et al., “Identification of novel bacterial plasminogen-binding proteins in the human pathogen Mycobacterium tuberculosis,” Proteomics, vol. 7, no. 18, pp. 3332–3341, 2007.
- T. Chitlaru, O. Gat, H. Grosfeld, I. Inbar, Y. Gozlan, and A. Shafferman, “Identification of in vivo-expressed immunogenic proteins by serological proteome analysis of the Bacillus anthracis secretome,” Infection and Immunity, vol. 75, no. 6, pp. 2841–2852, 2007.
- S. F. Dallo, T. R. Kannan, M. W. Blaylock, and J. B. Baseman, “Elongation factor Tu and E1 β subunit of pyruvate dehydrogenase complex act as fibronectin binding proteins in Mycoplasma pneumoniae,” Molecular Microbiology, vol. 46, no. 4, pp. 1041–1051, 2002.
- S. Balasubramanian, T. R. Kannan, and J. B. Baseman, “The surface-exposed carboxyl region of Mycoplasma pneumoniae elongation factor Tu interacts with fibronectin,” Infection and Immunity, vol. 76, no. 7, pp. 3116–3123, 2008.
- P. M. Pinto, G. Chemale, L. A. de Castro et al., “Proteomic survey of the pathogenic Mycoplasma hyopneumoniae strain 7448 and identification of novel post-translationally modified and antigenic proteins,” Veterinary Microbiology, vol. 121, no. 1-2, pp. 83–93, 2007.
- J. Mattow, U. E. Schaible, F. Schmidt et al., “Comparative proteome analysis of culture supernatant proteins from virulent Mycobacterium tuberculosis H37Rv and attenuated M. bovis BCG Copenhagen,” Electrophoresis, vol. 24, no. 19-20, pp. 3405–3420, 2003.
- R. A. Bartow and D. N. McMurray, “Cellular and humoral immune responses to mycobacterial stress proteins in experimental pulmonary tuberculosis,” Tubercle and Lung Disease, vol. 78, no. 3-4, pp. 185–193, 1997.
- J. M. Lamonica, M. Wagner, M. Eschenbrenner et al., “Comparative secretome analyses of three Bacillus anthracis strains with variant plasmid contents,” Infection and Immunity, vol. 73, no. 6, pp. 3646–3658, 2005.
- J. Antikainen, V. Kupannen, K. Lähteenmäki, and T. K. Korhonen, “pH-dependent association of enolase and glyceraldehyde-3-phosphate dehydrogenase of Lactobacillus crispatus with the cell wall and lipoteichoic acids,” Journal of Bacteriology, vol. 189, no. 12, pp. 4539–4543, 2007.
- Y. Feng, X. Pan, W. Sun et al., “Streptococcus suis enolase functions as a protective antigen displayed on the bacterial cell surface,” Journal of Infectious Diseases, vol. 200, no. 10, pp. 1583–1592, 2009.
- C. Castaldo, V. Vastano, R. A. Siciliano et al., “Surface displaced alfa-enolase of Lactobacillus plantarum is a fibronectin binding protein,” Microbial Cell Factories, vol. 8, article 14, 2009.
- M. Esgleas, Y. Li, M. A. Hancock, J. Harel, J. D. Dubreuil, and M. Gottschalk, “Isolation and characterization of α-enolase, a novel fibronectin-binding protein from Streptococcus suis,” Microbiology, vol. 154, no. 9, pp. 2668–2679, 2008.
- K. Antúnez, M. Anido, D. Arredondo, J. D. Evans, and P. Zunino, “Paenibacillus larvae enolase as a virulence factor in honeybee larvae infection,” Veterinary Microbiology, vol. 147, no. 1-2, pp. 83–89, 2011.
- H. Chen, S. Yu, X. Shen et al., “The Mycoplasma gallisepticumα-enolase is cell surface-exposed and mediates adherence by binding to chicken plasminogen,” Microbial Pathogenesis, vol. 51, no. 4, pp. 285–290, 2011.
- A. Yavlovich, H. Rechnitzer, and S. Rottem, “α-Enolase resides on the cell surface of Mycoplasma fermentans and binds plasminogen,” Infection and Immunity, vol. 75, no. 12, pp. 5716–5719, 2007.
- S. A. Schreiner, A. Sokoli, K. M. Felder et al., “The surface-localised α-enolase of Mycoplasma suis is an adhesion protein,” Veterinary Microbiology, vol. 156, no. 1-2, pp. 88–95, 2012.