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Immunogenic membrane-associated proteins of Mycobacterium tuberculosis revealed by proteomics
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| Zeitschriftentitel: | Microbiology |
|---|---|
| Personen und Körperschaften: | , , , , , , , |
| In: | Microbiology, 151, 2005, 7, S. 2411-2419 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Microbiology Society
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| Schlagwörter: |
| author_facet |
Sinha, Sudhir Kosalai, K. Arora, Shalini Namane, Abdelkader Sharma, Pawan Gaikwad, Anil N. Brodin, Priscille Cole, Stewart T. Sinha, Sudhir Kosalai, K. Arora, Shalini Namane, Abdelkader Sharma, Pawan Gaikwad, Anil N. Brodin, Priscille Cole, Stewart T. |
|---|---|
| author |
Sinha, Sudhir Kosalai, K. Arora, Shalini Namane, Abdelkader Sharma, Pawan Gaikwad, Anil N. Brodin, Priscille Cole, Stewart T. |
| spellingShingle |
Sinha, Sudhir Kosalai, K. Arora, Shalini Namane, Abdelkader Sharma, Pawan Gaikwad, Anil N. Brodin, Priscille Cole, Stewart T. Microbiology Immunogenic membrane-associated proteins of Mycobacterium tuberculosis revealed by proteomics Microbiology |
| author_sort |
sinha, sudhir |
| spelling |
Sinha, Sudhir Kosalai, K. Arora, Shalini Namane, Abdelkader Sharma, Pawan Gaikwad, Anil N. Brodin, Priscille Cole, Stewart T. 1350-0872 1465-2080 Microbiology Society Microbiology http://dx.doi.org/10.1099/mic.0.27799-0 <jats:p>Membrane-associated proteins of<jats:italic>Mycobacterium tuberculosis</jats:italic>offer a challenge, as well as an opportunity, in the quest for better therapeutic and prophylactic interventions against tuberculosis. The authors have previously reported that extraction with the detergent Triton X-114 (TX-114) is a useful step in proteomic analysis of mycobacterial cell membranes, and detergent-soluble membrane proteins of mycobacteria are potent stimulators of human T cells. In this study 1-D and 2-D gel electrophoresis-based protocols were used for the analysis of proteins in the TX-114 extract of<jats:italic>M. tuberculosis</jats:italic>membranes. Peptide mass mapping (using MALDI-TOF-MS, matrix assisted laser desorption/ionization time of flight mass spectrometry) of 116 samples led to the identification of 105 proteins, 9 of which were new to the<jats:italic>M. tuberculosis</jats:italic>proteome. Functional orthologues of 73 of these proteins were also present in<jats:italic>Mycobacterium leprae</jats:italic>, suggesting their relative importance. Bioinformatics predicted that as many as 73 % of the proteins had a hydrophobic disposition. 1-D gel electrophoresis revealed more hydrophobic/transmembrane and basic proteins than 2-D gel electrophoresis. Identified proteins fell into the following major categories: protein synthesis, cell wall biogenesis/architecture and conserved hypotheticals/unknowns. To identify immunodominant proteins of the detergent phase (DP), 14 low-molecular-mass fractions prepared by continuous-elution gel electrophoresis were subjected to T cell activation assays using blood samples from BCG-vaccinated healthy donors from a tuberculosis endemic area. Analysis of the responses (cell proliferation and IFN-<jats:italic>γ</jats:italic>production) showed that the immunodominance of certain DP fractions was most probably due to ribosomal proteins, which is consistent with both their specificity for mycobacteria and their abundance. Other membrane-associated proteins, including transmembrane proteins/lipoproteins and ESAT-6, did not appear to contribute significantly to the observed T cell responses.</jats:p> Immunogenic membrane-associated proteins of Mycobacterium tuberculosis revealed by proteomics Microbiology |
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10.1099/mic.0.27799-0 |
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Microbiology Society, 2005 |
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Microbiology Society, 2005 |
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| title |
Immunogenic membrane-associated proteins of Mycobacterium tuberculosis revealed by proteomics |
| title_unstemmed |
Immunogenic membrane-associated proteins of Mycobacterium tuberculosis revealed by proteomics |
| title_full |
Immunogenic membrane-associated proteins of Mycobacterium tuberculosis revealed by proteomics |
| title_fullStr |
Immunogenic membrane-associated proteins of Mycobacterium tuberculosis revealed by proteomics |
| title_full_unstemmed |
Immunogenic membrane-associated proteins of Mycobacterium tuberculosis revealed by proteomics |
| title_short |
Immunogenic membrane-associated proteins of Mycobacterium tuberculosis revealed by proteomics |
| title_sort |
immunogenic membrane-associated proteins of mycobacterium tuberculosis revealed by proteomics |
| topic |
Microbiology |
| url |
http://dx.doi.org/10.1099/mic.0.27799-0 |
| publishDate |
2005 |
| physical |
2411-2419 |
| description |
<jats:p>Membrane-associated proteins of<jats:italic>Mycobacterium tuberculosis</jats:italic>offer a challenge, as well as an opportunity, in the quest for better therapeutic and prophylactic interventions against tuberculosis. The authors have previously reported that extraction with the detergent Triton X-114 (TX-114) is a useful step in proteomic analysis of mycobacterial cell membranes, and detergent-soluble membrane proteins of mycobacteria are potent stimulators of human T cells. In this study 1-D and 2-D gel electrophoresis-based protocols were used for the analysis of proteins in the TX-114 extract of<jats:italic>M. tuberculosis</jats:italic>membranes. Peptide mass mapping (using MALDI-TOF-MS, matrix assisted laser desorption/ionization time of flight mass spectrometry) of 116 samples led to the identification of 105 proteins, 9 of which were new to the<jats:italic>M. tuberculosis</jats:italic>proteome. Functional orthologues of 73 of these proteins were also present in<jats:italic>Mycobacterium leprae</jats:italic>, suggesting their relative importance. Bioinformatics predicted that as many as 73 % of the proteins had a hydrophobic disposition. 1-D gel electrophoresis revealed more hydrophobic/transmembrane and basic proteins than 2-D gel electrophoresis. Identified proteins fell into the following major categories: protein synthesis, cell wall biogenesis/architecture and conserved hypotheticals/unknowns. To identify immunodominant proteins of the detergent phase (DP), 14 low-molecular-mass fractions prepared by continuous-elution gel electrophoresis were subjected to T cell activation assays using blood samples from BCG-vaccinated healthy donors from a tuberculosis endemic area. Analysis of the responses (cell proliferation and IFN-<jats:italic>γ</jats:italic>production) showed that the immunodominance of certain DP fractions was most probably due to ribosomal proteins, which is consistent with both their specificity for mycobacteria and their abundance. Other membrane-associated proteins, including transmembrane proteins/lipoproteins and ESAT-6, did not appear to contribute significantly to the observed T cell responses.</jats:p> |
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| author | Sinha, Sudhir, Kosalai, K., Arora, Shalini, Namane, Abdelkader, Sharma, Pawan, Gaikwad, Anil N., Brodin, Priscille, Cole, Stewart T. |
| author_facet | Sinha, Sudhir, Kosalai, K., Arora, Shalini, Namane, Abdelkader, Sharma, Pawan, Gaikwad, Anil N., Brodin, Priscille, Cole, Stewart T., Sinha, Sudhir, Kosalai, K., Arora, Shalini, Namane, Abdelkader, Sharma, Pawan, Gaikwad, Anil N., Brodin, Priscille, Cole, Stewart T. |
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| description | <jats:p>Membrane-associated proteins of<jats:italic>Mycobacterium tuberculosis</jats:italic>offer a challenge, as well as an opportunity, in the quest for better therapeutic and prophylactic interventions against tuberculosis. The authors have previously reported that extraction with the detergent Triton X-114 (TX-114) is a useful step in proteomic analysis of mycobacterial cell membranes, and detergent-soluble membrane proteins of mycobacteria are potent stimulators of human T cells. In this study 1-D and 2-D gel electrophoresis-based protocols were used for the analysis of proteins in the TX-114 extract of<jats:italic>M. tuberculosis</jats:italic>membranes. Peptide mass mapping (using MALDI-TOF-MS, matrix assisted laser desorption/ionization time of flight mass spectrometry) of 116 samples led to the identification of 105 proteins, 9 of which were new to the<jats:italic>M. tuberculosis</jats:italic>proteome. Functional orthologues of 73 of these proteins were also present in<jats:italic>Mycobacterium leprae</jats:italic>, suggesting their relative importance. Bioinformatics predicted that as many as 73 % of the proteins had a hydrophobic disposition. 1-D gel electrophoresis revealed more hydrophobic/transmembrane and basic proteins than 2-D gel electrophoresis. Identified proteins fell into the following major categories: protein synthesis, cell wall biogenesis/architecture and conserved hypotheticals/unknowns. To identify immunodominant proteins of the detergent phase (DP), 14 low-molecular-mass fractions prepared by continuous-elution gel electrophoresis were subjected to T cell activation assays using blood samples from BCG-vaccinated healthy donors from a tuberculosis endemic area. Analysis of the responses (cell proliferation and IFN-<jats:italic>γ</jats:italic>production) showed that the immunodominance of certain DP fractions was most probably due to ribosomal proteins, which is consistent with both their specificity for mycobacteria and their abundance. Other membrane-associated proteins, including transmembrane proteins/lipoproteins and ESAT-6, did not appear to contribute significantly to the observed T cell responses.</jats:p> |
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| spelling | Sinha, Sudhir Kosalai, K. Arora, Shalini Namane, Abdelkader Sharma, Pawan Gaikwad, Anil N. Brodin, Priscille Cole, Stewart T. 1350-0872 1465-2080 Microbiology Society Microbiology http://dx.doi.org/10.1099/mic.0.27799-0 <jats:p>Membrane-associated proteins of<jats:italic>Mycobacterium tuberculosis</jats:italic>offer a challenge, as well as an opportunity, in the quest for better therapeutic and prophylactic interventions against tuberculosis. The authors have previously reported that extraction with the detergent Triton X-114 (TX-114) is a useful step in proteomic analysis of mycobacterial cell membranes, and detergent-soluble membrane proteins of mycobacteria are potent stimulators of human T cells. In this study 1-D and 2-D gel electrophoresis-based protocols were used for the analysis of proteins in the TX-114 extract of<jats:italic>M. tuberculosis</jats:italic>membranes. Peptide mass mapping (using MALDI-TOF-MS, matrix assisted laser desorption/ionization time of flight mass spectrometry) of 116 samples led to the identification of 105 proteins, 9 of which were new to the<jats:italic>M. tuberculosis</jats:italic>proteome. Functional orthologues of 73 of these proteins were also present in<jats:italic>Mycobacterium leprae</jats:italic>, suggesting their relative importance. Bioinformatics predicted that as many as 73 % of the proteins had a hydrophobic disposition. 1-D gel electrophoresis revealed more hydrophobic/transmembrane and basic proteins than 2-D gel electrophoresis. Identified proteins fell into the following major categories: protein synthesis, cell wall biogenesis/architecture and conserved hypotheticals/unknowns. To identify immunodominant proteins of the detergent phase (DP), 14 low-molecular-mass fractions prepared by continuous-elution gel electrophoresis were subjected to T cell activation assays using blood samples from BCG-vaccinated healthy donors from a tuberculosis endemic area. Analysis of the responses (cell proliferation and IFN-<jats:italic>γ</jats:italic>production) showed that the immunodominance of certain DP fractions was most probably due to ribosomal proteins, which is consistent with both their specificity for mycobacteria and their abundance. Other membrane-associated proteins, including transmembrane proteins/lipoproteins and ESAT-6, did not appear to contribute significantly to the observed T cell responses.</jats:p> Immunogenic membrane-associated proteins of Mycobacterium tuberculosis revealed by proteomics Microbiology |
| spellingShingle | Sinha, Sudhir, Kosalai, K., Arora, Shalini, Namane, Abdelkader, Sharma, Pawan, Gaikwad, Anil N., Brodin, Priscille, Cole, Stewart T., Microbiology, Immunogenic membrane-associated proteins of Mycobacterium tuberculosis revealed by proteomics, Microbiology |
| title | Immunogenic membrane-associated proteins of Mycobacterium tuberculosis revealed by proteomics |
| title_full | Immunogenic membrane-associated proteins of Mycobacterium tuberculosis revealed by proteomics |
| title_fullStr | Immunogenic membrane-associated proteins of Mycobacterium tuberculosis revealed by proteomics |
| title_full_unstemmed | Immunogenic membrane-associated proteins of Mycobacterium tuberculosis revealed by proteomics |
| title_short | Immunogenic membrane-associated proteins of Mycobacterium tuberculosis revealed by proteomics |
| title_sort | immunogenic membrane-associated proteins of mycobacterium tuberculosis revealed by proteomics |
| title_unstemmed | Immunogenic membrane-associated proteins of Mycobacterium tuberculosis revealed by proteomics |
| topic | Microbiology |
| url | http://dx.doi.org/10.1099/mic.0.27799-0 |