A proteomic view of an important human pathogen--towards the quantification of the entire Staphylococcus aureus proteome.
The genome sequence is the "blue-print of life," but proteomics provides the link to the actual physiology of living cells. Because of their low complexity bacteria are excellent model systems to identify the entire protein assembly of a living organism. Here we show that the majority of p...
Guardado en:
| Autores principales: | , , , , , , , , , , , , |
|---|---|
| Formato: | article |
| Lenguaje: | EN |
| Publicado: |
Public Library of Science (PLoS)
2009
|
| Materias: | |
| Acceso en línea: | https://doaj.org/article/32e970e70559486db8fef916ac09e1fc |
| Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
| id |
oai:doaj.org-article:32e970e70559486db8fef916ac09e1fc |
|---|---|
| record_format |
dspace |
| spelling |
oai:doaj.org-article:32e970e70559486db8fef916ac09e1fc2021-11-25T06:27:36ZA proteomic view of an important human pathogen--towards the quantification of the entire Staphylococcus aureus proteome.1932-620310.1371/journal.pone.0008176https://doaj.org/article/32e970e70559486db8fef916ac09e1fc2009-12-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/19997597/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203The genome sequence is the "blue-print of life," but proteomics provides the link to the actual physiology of living cells. Because of their low complexity bacteria are excellent model systems to identify the entire protein assembly of a living organism. Here we show that the majority of proteins expressed in growing and non-growing cells of the human pathogen Staphylococcus aureus can be identified and even quantified by a metabolic labeling proteomic approach. S. aureus has been selected as model for this proteomic study, because it poses a major risk to our health care system by combining high pathogenicity with an increasing frequency of multiple antibiotic resistance, thus requiring the development of new anti-staphylococcal therapy strategies. Since such strategies will likely have to target extracellular and surface-exposed virulence factors as well as staphylococcal survival and adaptation capabilities, we decided to combine four subproteomic fractions: cytosolic proteins, membrane-bound proteins, cell surface-associated and extracellular proteins, to comprehensively cover the entire proteome of S. aureus. This quantitative proteomics approach integrating data ranging from gene expression to subcellular localization in growing and non-growing cells is a proof of principle for whole-cell physiological proteomics that can now be extended to address physiological questions in infection-relevant settings. Importantly, with more than 1700 identified proteins (and 1450 quantified proteins) corresponding to a coverage of about three-quarters of the expressed proteins, our model study represents the most comprehensive quantification of a bacterial proteome reported to date. It thus paves the way towards a new level in understanding of cell physiology and pathophysiology of S. aureus and related pathogenic bacteria, opening new avenues for infection-related research on this crucial pathogen.Dörte BecherKristina HempelSusanne SieversDaniela ZühlkeJan Pané-FarréAndreas OttoStephan FuchsDirk AlbrechtJörg BernhardtSusanne EngelmannUwe VölkerJan Maarten van DijlMichael HeckerPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 4, Iss 12, p e8176 (2009) |
| institution |
DOAJ |
| collection |
DOAJ |
| language |
EN |
| topic |
Medicine R Science Q |
| spellingShingle |
Medicine R Science Q Dörte Becher Kristina Hempel Susanne Sievers Daniela Zühlke Jan Pané-Farré Andreas Otto Stephan Fuchs Dirk Albrecht Jörg Bernhardt Susanne Engelmann Uwe Völker Jan Maarten van Dijl Michael Hecker A proteomic view of an important human pathogen--towards the quantification of the entire Staphylococcus aureus proteome. |
| description |
The genome sequence is the "blue-print of life," but proteomics provides the link to the actual physiology of living cells. Because of their low complexity bacteria are excellent model systems to identify the entire protein assembly of a living organism. Here we show that the majority of proteins expressed in growing and non-growing cells of the human pathogen Staphylococcus aureus can be identified and even quantified by a metabolic labeling proteomic approach. S. aureus has been selected as model for this proteomic study, because it poses a major risk to our health care system by combining high pathogenicity with an increasing frequency of multiple antibiotic resistance, thus requiring the development of new anti-staphylococcal therapy strategies. Since such strategies will likely have to target extracellular and surface-exposed virulence factors as well as staphylococcal survival and adaptation capabilities, we decided to combine four subproteomic fractions: cytosolic proteins, membrane-bound proteins, cell surface-associated and extracellular proteins, to comprehensively cover the entire proteome of S. aureus. This quantitative proteomics approach integrating data ranging from gene expression to subcellular localization in growing and non-growing cells is a proof of principle for whole-cell physiological proteomics that can now be extended to address physiological questions in infection-relevant settings. Importantly, with more than 1700 identified proteins (and 1450 quantified proteins) corresponding to a coverage of about three-quarters of the expressed proteins, our model study represents the most comprehensive quantification of a bacterial proteome reported to date. It thus paves the way towards a new level in understanding of cell physiology and pathophysiology of S. aureus and related pathogenic bacteria, opening new avenues for infection-related research on this crucial pathogen. |
| format |
article |
| author |
Dörte Becher Kristina Hempel Susanne Sievers Daniela Zühlke Jan Pané-Farré Andreas Otto Stephan Fuchs Dirk Albrecht Jörg Bernhardt Susanne Engelmann Uwe Völker Jan Maarten van Dijl Michael Hecker |
| author_facet |
Dörte Becher Kristina Hempel Susanne Sievers Daniela Zühlke Jan Pané-Farré Andreas Otto Stephan Fuchs Dirk Albrecht Jörg Bernhardt Susanne Engelmann Uwe Völker Jan Maarten van Dijl Michael Hecker |
| author_sort |
Dörte Becher |
| title |
A proteomic view of an important human pathogen--towards the quantification of the entire Staphylococcus aureus proteome. |
| title_short |
A proteomic view of an important human pathogen--towards the quantification of the entire Staphylococcus aureus proteome. |
| title_full |
A proteomic view of an important human pathogen--towards the quantification of the entire Staphylococcus aureus proteome. |
| title_fullStr |
A proteomic view of an important human pathogen--towards the quantification of the entire Staphylococcus aureus proteome. |
| title_full_unstemmed |
A proteomic view of an important human pathogen--towards the quantification of the entire Staphylococcus aureus proteome. |
| title_sort |
proteomic view of an important human pathogen--towards the quantification of the entire staphylococcus aureus proteome. |
| publisher |
Public Library of Science (PLoS) |
| publishDate |
2009 |
| url |
https://doaj.org/article/32e970e70559486db8fef916ac09e1fc |
| work_keys_str_mv |
AT dortebecher aproteomicviewofanimportanthumanpathogentowardsthequantificationoftheentirestaphylococcusaureusproteome AT kristinahempel aproteomicviewofanimportanthumanpathogentowardsthequantificationoftheentirestaphylococcusaureusproteome AT susannesievers aproteomicviewofanimportanthumanpathogentowardsthequantificationoftheentirestaphylococcusaureusproteome AT danielazuhlke aproteomicviewofanimportanthumanpathogentowardsthequantificationoftheentirestaphylococcusaureusproteome AT janpanefarre aproteomicviewofanimportanthumanpathogentowardsthequantificationoftheentirestaphylococcusaureusproteome AT andreasotto aproteomicviewofanimportanthumanpathogentowardsthequantificationoftheentirestaphylococcusaureusproteome AT stephanfuchs aproteomicviewofanimportanthumanpathogentowardsthequantificationoftheentirestaphylococcusaureusproteome AT dirkalbrecht aproteomicviewofanimportanthumanpathogentowardsthequantificationoftheentirestaphylococcusaureusproteome AT jorgbernhardt aproteomicviewofanimportanthumanpathogentowardsthequantificationoftheentirestaphylococcusaureusproteome AT susanneengelmann aproteomicviewofanimportanthumanpathogentowardsthequantificationoftheentirestaphylococcusaureusproteome AT uwevolker aproteomicviewofanimportanthumanpathogentowardsthequantificationoftheentirestaphylococcusaureusproteome AT janmaartenvandijl aproteomicviewofanimportanthumanpathogentowardsthequantificationoftheentirestaphylococcusaureusproteome AT michaelhecker aproteomicviewofanimportanthumanpathogentowardsthequantificationoftheentirestaphylococcusaureusproteome AT dortebecher proteomicviewofanimportanthumanpathogentowardsthequantificationoftheentirestaphylococcusaureusproteome AT kristinahempel proteomicviewofanimportanthumanpathogentowardsthequantificationoftheentirestaphylococcusaureusproteome AT susannesievers proteomicviewofanimportanthumanpathogentowardsthequantificationoftheentirestaphylococcusaureusproteome AT danielazuhlke proteomicviewofanimportanthumanpathogentowardsthequantificationoftheentirestaphylococcusaureusproteome AT janpanefarre proteomicviewofanimportanthumanpathogentowardsthequantificationoftheentirestaphylococcusaureusproteome AT andreasotto proteomicviewofanimportanthumanpathogentowardsthequantificationoftheentirestaphylococcusaureusproteome AT stephanfuchs proteomicviewofanimportanthumanpathogentowardsthequantificationoftheentirestaphylococcusaureusproteome AT dirkalbrecht proteomicviewofanimportanthumanpathogentowardsthequantificationoftheentirestaphylococcusaureusproteome AT jorgbernhardt proteomicviewofanimportanthumanpathogentowardsthequantificationoftheentirestaphylococcusaureusproteome AT susanneengelmann proteomicviewofanimportanthumanpathogentowardsthequantificationoftheentirestaphylococcusaureusproteome AT uwevolker proteomicviewofanimportanthumanpathogentowardsthequantificationoftheentirestaphylococcusaureusproteome AT janmaartenvandijl proteomicviewofanimportanthumanpathogentowardsthequantificationoftheentirestaphylococcusaureusproteome AT michaelhecker proteomicviewofanimportanthumanpathogentowardsthequantificationoftheentirestaphylococcusaureusproteome |
| _version_ |
1718413672331608064 |