-
Something wrong with this record ?
Comparative proteomic profiling of culture filtrate proteins of less and highly virulent Francisella tularensis strains
K. Konecna, L. Hernychova, M. Reichelova, J. Lenco, J. Klimentova, J. Stulik, A. Macela, T. Alefantis, VG. Delvecchio
Language English Country Germany
Document type Comparative Study, Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Bacterial Proteins chemistry MeSH
- Virulence Factors chemistry MeSH
- Francisella tularensis chemistry pathogenicity MeSH
- Culture Media, Conditioned MeSH
- Proteome chemistry MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Comparative Study MeSH
The facultative intracellular bacterium Francisella tularensis is the causal agent of the serious infectious disease tularemia. Despite the dynamic progress, which has been made in last few years, important questions regarding Francisella pathogenicity still remain to be answered. Generally, secreted proteins play an important role in pathogenicity of intracellular microbes. In this study, we investigated the protein composition of the culture filtrate proteins of highly virulent F. tularensis subsp. tularensis, strain SCHU S4 and attenuated F. tularensis subsp. holarctica, live vaccine strain using a comparative proteomic analysis. The majority of proteins identified in this study have been implicated in virulence mechanisms of other pathogens, and several have been categorized as having moonlighting properties; those that have more than one unrelated function. This profiling study of secreted proteins resulted in the unique detection of acid phosphatase (precursor) A (AcpA), β-lactamase, and hypothetical protein FTT0484 in the highly virulent strain SCHU S4 secretome. The release of AcpA may be of importance for F. tularensis subsp. tularensis virulence due to the recently described AcpA role in the F. tularensis escape from phagosomes.
Institute for Immunology Purkyne Military Medical Academy Czech Republic
References provided by Crossref.org
- 000
- 00000naa a2200000 a 4500
- 001
- bmc12026600
- 003
- CZ-PrNML
- 005
- 20160301055921.0
- 007
- ta
- 008
- 120816s2010 gw f 000 0#eng||
- 009
- AR
- 024 7_
- $a 10.1002/pmic.201000248 $2 doi
- 035 __
- $a (PubMed)21136602
- 040 __
- $a ABA008 $b cze $d ABA008 $e AACR2
- 041 0_
- $a eng
- 044 __
- $a gw
- 100 1_
- $a Konecna, Klara $u Institute of Molecular Pathology, Faculty of Military Health Sciences, University of Defense, Hradec Kralove, Czech Republic
- 245 10
- $a Comparative proteomic profiling of culture filtrate proteins of less and highly virulent Francisella tularensis strains / $c K. Konecna, L. Hernychova, M. Reichelova, J. Lenco, J. Klimentova, J. Stulik, A. Macela, T. Alefantis, VG. Delvecchio
- 520 9_
- $a The facultative intracellular bacterium Francisella tularensis is the causal agent of the serious infectious disease tularemia. Despite the dynamic progress, which has been made in last few years, important questions regarding Francisella pathogenicity still remain to be answered. Generally, secreted proteins play an important role in pathogenicity of intracellular microbes. In this study, we investigated the protein composition of the culture filtrate proteins of highly virulent F. tularensis subsp. tularensis, strain SCHU S4 and attenuated F. tularensis subsp. holarctica, live vaccine strain using a comparative proteomic analysis. The majority of proteins identified in this study have been implicated in virulence mechanisms of other pathogens, and several have been categorized as having moonlighting properties; those that have more than one unrelated function. This profiling study of secreted proteins resulted in the unique detection of acid phosphatase (precursor) A (AcpA), β-lactamase, and hypothetical protein FTT0484 in the highly virulent strain SCHU S4 secretome. The release of AcpA may be of importance for F. tularensis subsp. tularensis virulence due to the recently described AcpA role in the F. tularensis escape from phagosomes.
- 650 _2
- $a bakteriální proteiny $x chemie $7 D001426
- 650 _2
- $a kultivační média speciální $7 D017077
- 650 _2
- $a Francisella tularensis $x chemie $x patogenita $7 D005604
- 650 _2
- $a proteom $x chemie $7 D020543
- 650 _2
- $a faktory virulence $x chemie $7 D037521
- 655 _2
- $a srovnávací studie $7 D003160
- 655 _2
- $a časopisecké články $7 D016428
- 655 _2
- $a práce podpořená grantem $7 D013485
- 700 1_
- $a Hernychová, Lenka, $d 1965- $7 xx0073983 $u Institute for Radiobiology and Immunology, Purkynĕ Military Medical Academy, Trebesská 1575, 500 01 Hradec Králové, Czech Republic
- 700 1_
- $a Reichelová, Markéta $7 _BN002352
- 700 1_
- $a Lenčo, Juraj, $d 1979- $7 mzk2007377664 $u Faculty of Military Health Sciences, Institute of Molecular Pathology, University of Defense, Hradec Kralove, Czech Republic
- 700 1_
- $a Klimentová, Jana $7 xx0135751 $u Department of Molecular Pathology and Biology, Faculty of Military Health Sciences, University of Defence, Trebesska 1575, 500 01 Hradec Kralove, Czech Republic. Electronic address: jana.klimentova@unob.cz
- 700 1_
- $a Stulík, Jiří, $d 1957- $7 mzk2008473161 $u Faculty of Military Health Sciences, Institute of Molecular Pathology, University of Defense, Hradec Kralove, Czech Republic
- 700 1_
- $a Macela, Aleš, $d 1944- $7 mzk2005279505 $u Institute for Immunology, Purkyne Military Medical Academy, Czech Republic
- 700 1_
- $a Alefantis, Tim $u Vital Probes, Inc., 1300 Old Plank Road, Mayfield, PA 18433, USA $7 gn_A_00003701
- 700 1_
- $a Delvecchio, Vito G. $u Vital Probes, Mayfield, Pennsylvania, USA
- 773 0_
- $w MED00007044 $t Proteomics $x 1615-9861 $g Roč. 10, č. 24 (2010), s. 4501-4511
- 856 41
- $u https://pubmed.ncbi.nlm.nih.gov/21136602 $y Pubmed
- 910 __
- $a ABA008 $b sig $c sign $y m $z 0
- 990 __
- $a 20120816 $b ABA008
- 991 __
- $a 20160301055934 $b ABA008
- 999 __
- $a ok $b bmc $g 948642 $s 783946
- BAS __
- $a 3
- BAS __
- $a PreBMC
- BMC __
- $a 2010 $b 10 $c 24 $d 4501-4511 $e 20101109 $i 1615-9861 $m Proteomics $n Proteomics $x MED00007044
- LZP __
- $b NLK122 $a Pubmed-20120816/11/01