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1860799930455556096
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| building |
INTELEK Repository
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| collection |
Online Access
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| collectionurl |
https://intelek.unisza.edu.my/intelek/pages/search.php?search=!collection407072
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| date |
2013-02-13 13:58:16
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| format |
Restricted Document
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| id |
7963
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| institution |
UniSZA
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| internalnotes |
Archer, G. L. 1998. Staphylococcus aureus: A well-armed pathogen. Clinical Infectious Diseases 26: 1179-1181. Bjellqvist, B., Hughes, G. J., Pasquali, Ch., Paquet, N., Ravier, F., Sanchez, J. -Ch., Frutiger, S. & Hochstrasser, D. F. 1993. The focusing positions of polypeptides in immobilized pH gradients can be predicted from their amino acid sequences. Electrophoresis 14: 1023-1031. Cheng, A. G., Kim, H. K., Burts, M. L., Krausz, T., Schneewind, O. & Missiakas, D. M. 2009. Genetic requirements for Staphylococcus aureus abscess formation and persistence in host tissues. FASEB Journal 23: 1-12. Cole, C., Barber, J. D. & Barton, G. J. 2008. The Jpred 3 secondary structure prediction server. Nucleic Acids Research 36(suppl. 2): W197-W201. Cuff, J. A. & Barton, G. J. 2000. Application of multiple sequence alignment profiles to improve protein secondary structure prediction. PROTEINS: Structure Function and Genetics 40: 502-511. Duthie, E. S. & Lorenz, L. L. 1952. Staphylococcal coagulase: Mode of action and antigenicity. Journal of General Microbiology 6: 95-107. Easmon, C. S. F. & Adlam, C. 1983. Staphylococci and Staphylococcal Infections, Vols. 1 and 2. Academic Press, London. Field, H. & Smith, H. W. 1945. Coagulase test for staphylococci. Journal of Comparative Pathology 55: 63. Foster, T. J., O‟Reilly, M., Phonimdaeng, P., Cooney, J., Patel, A. H. & Bramley, A. J. 1990. Genetic studies of virulence factors of Staphylococcus aureus - Properties of coagulase and gamma-toxin, alpha-toxin, beta-toxin and protein A in the pathogenesis of S. aureus infections. In Molecular Biology of Staphylococci. R. P. Novick (ed.). VCH Publishing, New York. p. 403-420. Friedrich, R., Panizzi, P., Fuentes-Prior, P., Richter, K., Verhamme, I., Anderson, P. J., Kawabata, S., Huber, R., Bode, W. & Bock, P. E. 2003. Staphylocoagulase is a prototype for the mechanism of cofactor-induced zymogen activation. Nature 425: 535-539. Gardy, J. L., Spencer, C., Wang, K., Ester, M., Tusnady, G. E., Simon, I., Hua, S., deFays, K., Lambert, C., Nakai, K. & Brinkman, F. S. L. 2003. PSORT-B: Improving protein subcellular localization prediction for Gram-negative bacteria. Nucleic Acids Research 31: 3613-3617. Gardy, J. L., Laird, M. R., Chen, F., Rey, S., Walsh, C. J., Ester, M., & Brinkman, F. S. L. 2005. PSORTb v.2.0: Expanded prediction of bacterial protein subcellular localization and insights gained from comparative proteome analysis. Bioinformatics 21: 617-623. Gasteiger, E., Hoogland, C., Gattiker, A., Duvaud, S., Wilkins, M. R., Appel, R. D. & Bairoch, A. 2005. Protein identification and analysis tools on the ExPASy server. In The Proteomics Protocols Handbook. John M. Walker (ed.). Humana Press, New York. p. 571-607. Heilmann, C., Herrmann, M., Kehrel, B. E. & Peters, G. 2002. Platelet-binding domains in two fibrinogen-binding proteins of Staphylococcus aureus identified by phage display. Journal of Infectious Disease 186: 32-39. Hofmann, K. & Stoffel, W. 1993. TMBASE - A database of membrane spanning protein segments. Biological Chemistry Hoppe-Seyler 374: 166-173. Kloos, W. E. & Bannerman, T. L. 1995. Staphylococcus and Micrococcus. In Manual of Clinical Microbiology. P. R. Murray, E. J. Baron, M. A. Pfaller, F. C. Tenover and R. H. Yolken (eds.). American Society for Microbiology Press, Washington. p. 282-298. Koneman, E. W. 1997. Color Atlas and Textbook of Diagnostic Microbiology, 5th ed. J. B. Lippincott Company, Philadelphia, P.A. Lindberg, M., Jonsson, K., Muller, H., Jonsson, H., Signas, C., Hook, M., Raja, R., Raucci, G. & Anantharamaiah, G. M. (1990). Fibronectin-binding proteins in Staphylococcus aureus. In Molecular Biology of Staphylococci. R. P. Novick (ed.). VCH Publishing, New York, N.Y. p. 343-353. Lindsay, J. A., Ruzin, A., Ross, H. F., Kurepina, N. & Novick, R. P. 1998. The gene for toxic shock toxin is carried by a family of mobile pathogenicity islands in Staphylococcus aureus. Molecular Microbiology 29: 527-543. Loeb, L. 1903. The influence of certain bacteria on the coagulation of blood. Journal of Medical Research 10: 407-419. Mohamed, N. A., Mohamed, R. & Chong, T. T. 2012. Homology modeling of coagulase in Staphylococcus aureus. Bioinformation 8: 412-414. Novick, R. P. 2000. Pathogenicity factors and their regulation. In Gram-positive Pathogens. V. A. Fischetti, R. P. Novick, J. J. Ferretti, D. A. Portnoy and J. A. Rood (eds.). American Society for Microbiology Press, Washington. p. 392- 407. Panizzi, P., Friedrich, R., Fuentes-Prior, P., Richter, K., Bock, P. E. & Bode, W. 2006. Fibrinogen substrate recognition by staphylocoagulase-(prothrombin) complexes. Journal of Biological Chemistry 281: 1179-1187. Phonimdaeng, P., O‟Reilly, M., Nowlan, P., Bramley, A. J. & Foster, T. J. 1990. The coagulase of Staphylococcus aureus 8325-4 sequence analysis and virulence of site-specific coagulase-deficient mutants. Molecular Microbiology 4: 393-404. Projan, S. J., Nesin, M. & Dunman, P. M. 2006. Staphylococcal vaccines and immunotherapy: To dream the impossible dream? Current Opinion in Pharmacology 6: 473-479. Rogers, D. E. & Melly, M. A. 1965. Speculation on the immunology of Mudd, S. Capsulation, pseudocapsulation, and the somatic antigens of the surface of Staphylococcus aureus. Annals of the New York Academy of Sciences 128: 45-56. Smith, W., Hale, J. H. & Smith, M. M. 1947. The role of coagulase in staphylococcal infection. British Journal of Experimental Pathology 28: 57-67. Spyropoulos, I. C., Liakopoulos, T. D., Bagos, P. G. & Hamodrakas, S. J. 2004. TMRPres2D: High quality visual representation of transmembrane protein models. Bioinformatics 20: 3258-3260. Yu, N. Y., Wagner, J. R., Laird, M. R., Melli, G., Rey, S., Lo, R., Dao, P., Sahinalp, S. C., Ester, M., Foster, L. J. & Brinkman, F. S. L. 2010. PSORTb 3.0: Improved protein subcellular localization prediction with refined localization subcategories and predictive capabilities for all prokaryotes. Bioinformatics 26: 1608-1615
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3771-01-FH02-FBIM-19-25214.pdf
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Matzakaria
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oai_dc
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https://intelek.unisza.edu.my/intelek/pages/view.php?ref=7963
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| spelling |
7963 https://intelek.unisza.edu.my/intelek/pages/view.php?ref=7963 https://intelek.unisza.edu.my/intelek/pages/search.php?search=!collection407072 Restricted Document Article Journal application/pdf 11 1.6 Adobe Acrobat Pro DC 20 Paper Capture Plug-in Matzakaria 2013-02-13 13:58:16 3771-01-FH02-FBIM-19-25214.pdf UniSZA Private Access In Silico Sequence Analysis of Coagulase in Staphylococcus aureus Journal Of Agrobiotechnology Coagulase production is generally accepted as being characteristic of pathogenic and potentially pathogenic strains. Coagulase can cause clot formation in the immediate vicinity of the bacterium. The protein has been shown to contribute to bacterial virulence in wound infections owing to its ability to delay the healing processes. In this study, we conducted in silico sequence analysis using coagulase from the Gram-positive human pathogen Staphylococcus aureus with GenBank Accession no. CAC 84776.1. Various bioinformatics tools were used to predict the properties of the S. aureus coagulase. The N-terminal portion of coagulase was predicted to form transmembrane helices whereas the majority of the protein was hydrophilic in nature and was predicted to form several alpha-helices. Coagulase was also predicted to localize extracellularly and has a pI value of 8.41. The in silico analysis carried out offers an alternative way to obtain structural information and will assist in determining the structural prediction of the S. aureus coagulase. 3 1 35-45 Archer, G. L. 1998. Staphylococcus aureus: A well-armed pathogen. Clinical Infectious Diseases 26: 1179-1181. Bjellqvist, B., Hughes, G. J., Pasquali, Ch., Paquet, N., Ravier, F., Sanchez, J. -Ch., Frutiger, S. & Hochstrasser, D. F. 1993. The focusing positions of polypeptides in immobilized pH gradients can be predicted from their amino acid sequences. Electrophoresis 14: 1023-1031. Cheng, A. G., Kim, H. K., Burts, M. L., Krausz, T., Schneewind, O. & Missiakas, D. M. 2009. Genetic requirements for Staphylococcus aureus abscess formation and persistence in host tissues. FASEB Journal 23: 1-12. Cole, C., Barber, J. D. & Barton, G. J. 2008. The Jpred 3 secondary structure prediction server. Nucleic Acids Research 36(suppl. 2): W197-W201. Cuff, J. A. & Barton, G. J. 2000. Application of multiple sequence alignment profiles to improve protein secondary structure prediction. PROTEINS: Structure Function and Genetics 40: 502-511. Duthie, E. S. & Lorenz, L. L. 1952. Staphylococcal coagulase: Mode of action and antigenicity. Journal of General Microbiology 6: 95-107. Easmon, C. S. F. & Adlam, C. 1983. Staphylococci and Staphylococcal Infections, Vols. 1 and 2. Academic Press, London. Field, H. & Smith, H. W. 1945. Coagulase test for staphylococci. Journal of Comparative Pathology 55: 63. Foster, T. J., O‟Reilly, M., Phonimdaeng, P., Cooney, J., Patel, A. H. & Bramley, A. J. 1990. Genetic studies of virulence factors of Staphylococcus aureus - Properties of coagulase and gamma-toxin, alpha-toxin, beta-toxin and protein A in the pathogenesis of S. aureus infections. In Molecular Biology of Staphylococci. R. P. Novick (ed.). VCH Publishing, New York. p. 403-420. Friedrich, R., Panizzi, P., Fuentes-Prior, P., Richter, K., Verhamme, I., Anderson, P. J., Kawabata, S., Huber, R., Bode, W. & Bock, P. E. 2003. Staphylocoagulase is a prototype for the mechanism of cofactor-induced zymogen activation. Nature 425: 535-539. Gardy, J. L., Spencer, C., Wang, K., Ester, M., Tusnady, G. E., Simon, I., Hua, S., deFays, K., Lambert, C., Nakai, K. & Brinkman, F. S. L. 2003. PSORT-B: Improving protein subcellular localization prediction for Gram-negative bacteria. Nucleic Acids Research 31: 3613-3617. Gardy, J. L., Laird, M. R., Chen, F., Rey, S., Walsh, C. J., Ester, M., & Brinkman, F. S. L. 2005. PSORTb v.2.0: Expanded prediction of bacterial protein subcellular localization and insights gained from comparative proteome analysis. Bioinformatics 21: 617-623. Gasteiger, E., Hoogland, C., Gattiker, A., Duvaud, S., Wilkins, M. R., Appel, R. D. & Bairoch, A. 2005. Protein identification and analysis tools on the ExPASy server. In The Proteomics Protocols Handbook. John M. Walker (ed.). Humana Press, New York. p. 571-607. Heilmann, C., Herrmann, M., Kehrel, B. E. & Peters, G. 2002. Platelet-binding domains in two fibrinogen-binding proteins of Staphylococcus aureus identified by phage display. Journal of Infectious Disease 186: 32-39. Hofmann, K. & Stoffel, W. 1993. TMBASE - A database of membrane spanning protein segments. Biological Chemistry Hoppe-Seyler 374: 166-173. Kloos, W. E. & Bannerman, T. L. 1995. Staphylococcus and Micrococcus. In Manual of Clinical Microbiology. P. R. Murray, E. J. Baron, M. A. Pfaller, F. C. Tenover and R. H. Yolken (eds.). American Society for Microbiology Press, Washington. p. 282-298. Koneman, E. W. 1997. Color Atlas and Textbook of Diagnostic Microbiology, 5th ed. J. B. Lippincott Company, Philadelphia, P.A. Lindberg, M., Jonsson, K., Muller, H., Jonsson, H., Signas, C., Hook, M., Raja, R., Raucci, G. & Anantharamaiah, G. M. (1990). Fibronectin-binding proteins in Staphylococcus aureus. In Molecular Biology of Staphylococci. R. P. Novick (ed.). VCH Publishing, New York, N.Y. p. 343-353. Lindsay, J. A., Ruzin, A., Ross, H. F., Kurepina, N. & Novick, R. P. 1998. The gene for toxic shock toxin is carried by a family of mobile pathogenicity islands in Staphylococcus aureus. Molecular Microbiology 29: 527-543. Loeb, L. 1903. The influence of certain bacteria on the coagulation of blood. Journal of Medical Research 10: 407-419. Mohamed, N. A., Mohamed, R. & Chong, T. T. 2012. Homology modeling of coagulase in Staphylococcus aureus. Bioinformation 8: 412-414. Novick, R. P. 2000. Pathogenicity factors and their regulation. In Gram-positive Pathogens. V. A. Fischetti, R. P. Novick, J. J. Ferretti, D. A. Portnoy and J. A. Rood (eds.). American Society for Microbiology Press, Washington. p. 392- 407. Panizzi, P., Friedrich, R., Fuentes-Prior, P., Richter, K., Bock, P. E. & Bode, W. 2006. Fibrinogen substrate recognition by staphylocoagulase-(prothrombin) complexes. Journal of Biological Chemistry 281: 1179-1187. Phonimdaeng, P., O‟Reilly, M., Nowlan, P., Bramley, A. J. & Foster, T. J. 1990. The coagulase of Staphylococcus aureus 8325-4 sequence analysis and virulence of site-specific coagulase-deficient mutants. Molecular Microbiology 4: 393-404. Projan, S. J., Nesin, M. & Dunman, P. M. 2006. Staphylococcal vaccines and immunotherapy: To dream the impossible dream? Current Opinion in Pharmacology 6: 473-479. Rogers, D. E. & Melly, M. A. 1965. Speculation on the immunology of Mudd, S. Capsulation, pseudocapsulation, and the somatic antigens of the surface of Staphylococcus aureus. Annals of the New York Academy of Sciences 128: 45-56. Smith, W., Hale, J. H. & Smith, M. M. 1947. The role of coagulase in staphylococcal infection. British Journal of Experimental Pathology 28: 57-67. Spyropoulos, I. C., Liakopoulos, T. D., Bagos, P. G. & Hamodrakas, S. J. 2004. TMRPres2D: High quality visual representation of transmembrane protein models. Bioinformatics 20: 3258-3260. Yu, N. Y., Wagner, J. R., Laird, M. R., Melli, G., Rey, S., Lo, R., Dao, P., Sahinalp, S. C., Ester, M., Foster, L. J. & Brinkman, F. S. L. 2010. PSORTb 3.0: Improved protein subcellular localization prediction with refined localization subcategories and predictive capabilities for all prokaryotes. Bioinformatics 26: 1608-1615
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| spellingShingle |
In Silico Sequence Analysis of Coagulase in Staphylococcus aureus
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| summary |
Coagulase production is generally accepted as being characteristic of pathogenic and potentially pathogenic strains. Coagulase can cause clot formation in the immediate vicinity of the bacterium. The protein has been shown to contribute to bacterial virulence in wound infections owing to its ability to delay the healing processes. In this study, we conducted in silico sequence analysis using coagulase from the Gram-positive human pathogen Staphylococcus aureus with GenBank Accession no. CAC 84776.1. Various bioinformatics tools were used to predict the properties of the S. aureus coagulase. The N-terminal portion of coagulase was predicted to form transmembrane helices whereas the majority of the protein was hydrophilic in nature and was predicted to form several alpha-helices. Coagulase was also predicted to localize extracellularly and has a pI value of 8.41. The in silico analysis carried out offers an alternative way to obtain structural information and will assist in determining the structural prediction of the S. aureus coagulase.
|
| title |
In Silico Sequence Analysis of Coagulase in Staphylococcus aureus
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| title_full |
In Silico Sequence Analysis of Coagulase in Staphylococcus aureus
|
| title_fullStr |
In Silico Sequence Analysis of Coagulase in Staphylococcus aureus
|
| title_full_unstemmed |
In Silico Sequence Analysis of Coagulase in Staphylococcus aureus
|
| title_short |
In Silico Sequence Analysis of Coagulase in Staphylococcus aureus
|
| title_sort |
in silico sequence analysis of coagulase in staphylococcus aureus
|