Informacja

Drogi użytkowniku, aplikacja do prawidłowego działania wymaga obsługi JavaScript. Proszę włącz obsługę JavaScript w Twojej przeglądarce.

Przeglądasz jako GOŚĆ
Tytuł pozycji:

Disarming Burkholderia pseudomallei: structural and functional characterization of a disulfide oxidoreductase (DsbA) required for virulence in vivo.

Tytuł :
Disarming Burkholderia pseudomallei: structural and functional characterization of a disulfide oxidoreductase (DsbA) required for virulence in vivo.
Autorzy :
Ireland PM; 1 Defence Science and Technology Laboratory , Porton Down, Salisbury, Wiltshire, United Kingdom .
McMahon RM
Marshall LE
Halili M
Furlong E
Tay S
Martin JL
Sarkar-Tyson M
Pokaż więcej
Źródło :
Antioxidants & redox signaling [Antioxid Redox Signal] 2014 Feb 01; Vol. 20 (4), pp. 606-17. Date of Electronic Publication: 2013 Sep 20.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
Język :
English
Imprint Name(s) :
Original Publication: Larchmont, NY : Mary Ann Liebert, Inc., 1999-
MeSH Terms :
Bacterial Proteins/*chemistry
Burkholderia pseudomallei/*enzymology
Protein Disulfide Reductase (Glutathione)/*chemistry
Animals ; Bacterial Proteins/metabolism ; Burkholderia pseudomallei/pathogenicity ; Catalytic Domain ; Cell Line ; Crystallography, X-Ray ; Female ; Mice ; Mice, Inbred BALB C ; Models, Molecular ; Oxidation-Reduction ; Peptide Hydrolases/metabolism ; Protein Disulfide Reductase (Glutathione)/metabolism ; Protein Structure, Secondary ; Type C Phospholipases/metabolism ; Virulence
References :
Infect Immun. 2003 Mar;71(3):1590-5. (PMID: 12595484)
J Biol Chem. 1947 Dec;171(2):501-5. (PMID: 20272088)
Antioxid Redox Signal. 2009 Jul;11(7):1485-500. (PMID: 19265485)
J Mol Biol. 1997 Apr 25;268(1):137-46. (PMID: 9149147)
J Biol Chem. 1993 Nov 25;268(33):24547-50. (PMID: 7693702)
Can J Microbiol. 1994 Nov;40(11):903-10. (PMID: 7528633)
Proc Natl Acad Sci U S A. 2008 Aug 19;105(33):11933-8. (PMID: 18695247)
Am J Trop Med Hyg. 2010 Jun;82(6):1113-7. (PMID: 20519609)
J Bacteriol. 2004 Apr;186(8):2288-94. (PMID: 15060030)
J Bacteriol. 1995 Jul;177(14):4121-30. (PMID: 7608087)
J Biol Chem. 2009 Apr 10;284(15):10150-9. (PMID: 19181668)
Infect Immun. 2003 Apr;71(4):2280-2. (PMID: 12654857)
Acta Crystallogr D Biol Crystallogr. 2011 Apr;67(Pt 4):235-42. (PMID: 21460441)
Antioxid Redox Signal. 2010 Apr 15;12(8):921-31. (PMID: 19788398)
Microb Pathog. 2009 Sep;47(3):111-7. (PMID: 19524661)
PLoS Negl Trop Dis. 2010 Nov 30;4(11):e900. (PMID: 21152057)
Proc Natl Acad Sci U S A. 2004 Sep 28;101(39):14240-5. (PMID: 15377794)
Acta Crystallogr D Biol Crystallogr. 2009 Jun;65(Pt 6):582-601. (PMID: 19465773)
Cell. 1991 Nov 1;67(3):581-9. (PMID: 1934062)
Acta Crystallogr D Biol Crystallogr. 2001 Sep;57(Pt 9):1293-5. (PMID: 11526323)
Acta Crystallogr D Biol Crystallogr. 2006 Jan;62(Pt 1):72-82. (PMID: 16369096)
Nat Rev Microbiol. 2009 Mar;7(3):215-25. (PMID: 19198617)
Proc Natl Acad Sci U S A. 1994 Nov 22;91(24):11552-6. (PMID: 7972100)
Br Med Bull. 2011;99:125-39. (PMID: 21558159)
Acta Crystallogr D Biol Crystallogr. 2010 Jan;66(Pt 1):12-21. (PMID: 20057044)
J Biol Chem. 2010 Jun 11;285(24):18423-32. (PMID: 20233716)
Fold Des. 1998;3(3):161-71. (PMID: 9562546)
Acta Crystallogr D Biol Crystallogr. 2008 Jan;64(Pt 1):61-9. (PMID: 18094468)
J Bacteriol. 2001 Jan;183(2):587-96. (PMID: 11133952)
Microbiol Immunol. 2000;44(1):41-50. (PMID: 10711598)
Infect Immun. 2003 Apr;71(4):1622-9. (PMID: 12654773)
Nature. 1993 Sep 30;365(6445):464-8. (PMID: 8413591)
Biochemistry. 1994 May 17;33(19):5974-83. (PMID: 8180227)
Infect Immun. 2002 May;70(5):2297-303. (PMID: 11953363)
Antioxid Redox Signal. 2011 May 1;14(9):1729-60. (PMID: 21241169)
Infect Immun. 1994 May;62(5):1914-9. (PMID: 7513308)
J Clin Microbiol. 2005 Feb;43(2):970-2. (PMID: 15695721)
J Microbiol Methods. 2009 Mar;76(3):320-3. (PMID: 19150470)
Microbiology (Reading). 2007 Jun;153(Pt 6):1907-1915. (PMID: 17526847)
Trans R Soc Trop Med Hyg. 2008 Dec;102 Suppl 1:S140-4. (PMID: 19121676)
Mol Cell. 2008 Sep 26;31(6):896-908. (PMID: 18922471)
Antimicrob Agents Chemother. 2011 Nov;55(11):5388-91. (PMID: 21876049)
N Engl J Med. 2012 Sep 13;367(11):1035-44. (PMID: 22970946)
Biochem Pharmacol. 1961 Jul;7:88-95. (PMID: 13726518)
Biochem Soc Trans. 2011 Oct;39(5):1327-33. (PMID: 21936810)
Proc Natl Acad Sci U S A. 1995 May 23;92(11):4927-31. (PMID: 7761426)
J Biol Chem. 1979 Oct 10;254(19):9627-32. (PMID: 385588)
Cell. 2006 Nov 17;127(4):789-801. (PMID: 17110337)
Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2126-32. (PMID: 15572765)
Clin Microbiol Rev. 2005 Apr;18(2):383-416. (PMID: 15831829)
EMBO J. 2009 Mar 18;28(6):779-91. (PMID: 19214188)
Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):213-21. (PMID: 20124702)
Front Cell Infect Microbiol. 2012 Jun 15;2:85. (PMID: 22919676)
Acta Crystallogr D Biol Crystallogr. 2012 Oct;68(Pt 10):1290-302. (PMID: 22993083)
J Bacteriol. 2006 Jun;188(12):4190-7. (PMID: 16740925)
Clin Infect Dis. 2009 Jan 1;48(1):1-12. (PMID: 19035777)
Acta Crystallogr D Biol Crystallogr. 2011 Apr;67(Pt 4):271-81. (PMID: 21460445)
Acta Trop. 2000 Feb 5;74(2-3):133-7. (PMID: 10674641)
Nat Rev Drug Discov. 2002 Sep;1(9):727-30. (PMID: 12209152)
Nat Rev Microbiol. 2008 Jan;6(1):17-27. (PMID: 18079741)
Clin Infect Dis. 1999 Aug;29(2):408-13. (PMID: 10476750)
Acta Trop. 2000 Feb 5;74(2-3):215-20. (PMID: 10674652)
Lancet. 2003 May 17;361(9370):1715-22. (PMID: 12767750)
Top Curr Chem. 2012;317:1-32. (PMID: 21695633)
J Appl Crystallogr. 2007 Aug 1;40(Pt 4):658-674. (PMID: 19461840)
Science. 2008 Aug 22;321(5892):1078-80. (PMID: 18719281)
Infect Immun. 2011 Nov;79(11):4299-307. (PMID: 21859853)
J Biol Chem. 2004 Mar 26;279(13):12967-73. (PMID: 14726535)
Proc Natl Acad Sci U S A. 1993 Feb 1;90(3):1043-7. (PMID: 8503954)
Anal Biochem. 1976 Sep;75(1):281-9. (PMID: 183567)
Molecular Sequence :
PDB 4K2D
Substance Nomenclature :
0 (Bacterial Proteins)
EC 1.8.4.2 (Protein Disulfide Reductase (Glutathione))
EC 3.1.4.- (Type C Phospholipases)
EC 3.4.- (Peptide Hydrolases)
Entry Date(s) :
Date Created: 20130802 Date Completed: 20140908 Latest Revision: 20211021
Update Code :
20211220
PubMed Central ID :
PMC3901323
DOI :
10.1089/ars.2013.5375
PMID :
23901809
Czasopismo naukowe
Aims: The intracellular pathogen Burkholderia pseudomallei causes the disease melioidosis, a major source of morbidity and mortality in southeast Asia and northern Australia. The need to develop novel antimicrobials is compounded by the absence of a licensed vaccine and the bacterium's resistance to multiple antibiotics. In a number of clinically relevant Gram-negative pathogens, DsbA is the primary disulfide oxidoreductase responsible for catalyzing the formation of disulfide bonds in secreted and membrane-associated proteins. In this study, a putative B. pseudomallei dsbA gene was evaluated functionally and structurally and its contribution to infection assessed.
Results: Biochemical studies confirmed the dsbA gene encodes a protein disulfide oxidoreductase. A dsbA deletion strain of B. pseudomallei was attenuated in both macrophages and a BALB/c mouse model of infection and displayed pleiotropic phenotypes that included defects in both secretion and motility. The 1.9 Å resolution crystal structure of BpsDsbA revealed differences from the classic member of this family Escherichia coli DsbA, in particular within the region surrounding the active site disulfide where EcDsbA engages with its partner protein E. coli DsbB, indicating that the interaction of BpsDsbA with its proposed partner BpsDsbB may be distinct from that of EcDsbA-EcDsbB.
Innovation: This study has characterized BpsDsbA biochemically and structurally and determined that it is required for virulence of B. pseudomallei.
Conclusion: These data establish a critical role for BpsDsbA in B. pseudomallei infection, which in combination with our structural characterization of BpsDsbA will facilitate the future development of rationally designed inhibitors against this drug-resistant organism.

Ta witryna wykorzystuje pliki cookies do przechowywania informacji na Twoim komputerze. Pliki cookies stosujemy w celu świadczenia usług na najwyższym poziomie, w tym w sposób dostosowany do indywidualnych potrzeb. Korzystanie z witryny bez zmiany ustawień dotyczących cookies oznacza, że będą one zamieszczane w Twoim komputerze. W każdym momencie możesz dokonać zmiany ustawień dotyczących cookies