scholarly journals SopB promotes phosphatidylinositol 3-phosphate formation on Salmonella vacuoles by recruiting Rab5 and Vps34

2008 ◽  
Vol 182 (4) ◽  
pp. 741-752 ◽  
Author(s):  
Gustavo V. Mallo ◽  
Marianela Espina ◽  
Adam C. Smith ◽  
Mauricio R. Terebiznik ◽  
Ainel Alemán ◽  
...  
Keyword(s):  
Phosphatase Activity ◽  
Virulence Factor ◽  
Pi3 Kinase ◽  
Bacterial Virulence ◽  
Host Cells ◽  
Salmonella Infection ◽  
Outer Leaflet ◽  
Phosphoinositide Phosphatase ◽  
Bacterial Virulence Factor ◽  
Phosphatidylinositol 3

Salmonella colonizes a vacuolar niche in host cells during infection. Maturation of the Salmonella-containing vacuole (SCV) involves the formation of phosphatidylinositol 3-phosphate (PI(3)P) on its outer leaflet. SopB, a bacterial virulence factor with phosphoinositide phosphatase activity, was proposed to generate PI(3)P by dephosphorylating PI(3,4)P2, PI(3,5)P2, and PI(3,4,5)P3. Here, we examine the mechanism of PI(3)P formation during Salmonella infection. SopB is required to form PI(3,4)P2/PI(3,4,5)P3 at invasion ruffles and PI(3)P on nascent SCVs. However, we uncouple these events experimentally and reveal that SopB does not dephosphorylate PI(3,4)P2/PI(3,4,5)P3 to produce PI(3)P. Instead, the phosphatase activity of SopB is required for Rab5 recruitment to the SCV. Vps34, a PI3-kinase that associates with active Rab5, is responsible for PI(3)P formation on SCVs. Therefore, SopB mediates PI(3)P production on the SCV indirectly through recruitment of Rab5 and its effector Vps34. These findings reveal a link between phosphoinositide phosphatase activity and the recruitment of Rab5 to phagosomes.

scholarly journals MptpB, a virulence factor from Mycobacterium tuberculosis, exhibits triple-specificity phosphatase activity

2007 ◽  
Vol 406 (1) ◽  
pp. 13-18 ◽  
Author(s):  
Nicola Beresford ◽  
Sumayya Patel ◽  
Jane Armstrong ◽  
Balázs Szöor ◽  
Anthony P. Fordham-Skelton ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Substrate Specificity ◽  
Phosphatase Activity ◽  
Virulence Factor ◽  
Protein Phosphatase ◽  
Host Cells ◽  
Lipid Phosphatases ◽  
Phosphoinositide Phosphatase ◽  
Dual Specificity Protein Phosphatase

Bacterial pathogens have developed sophisticated mechanisms of evading the immune system to survive in infected host cells. Central to the pathogenesis of Mycobacterium tuberculosis is the arrest of phagosome maturation, partly through interference with PtdIns signalling. The protein phosphatase MptpB is an essential secreted virulence factor in M. tuberculosis. A combination of bioinformatics analysis, enzyme kinetics and substrate-specificity characterization revealed that MptpB exhibits both dual-specificity protein phosphatase activity and, importantly, phosphoinositide phosphatase activity. Mutagenesis of conserved residues in the active site signature indicates a cysteine-based mechanism of dephosphorylation and identifies two new catalytic residues, Asp165, essential in catalysis, and Lys164, apparently involved in substrate specificity. Sequence similarities with mammalian lipid phosphatases and a preference for phosphoinositide substrates suggests a potential novel role of MptpB in PtdIns metabolism in the host and reveals new perspectives for the role of this phosphatase in mycobacteria pathogenicity.

Purification of bacterial virulence factor pertactin using high affinity ligands

2020 ◽  
Vol 164 ◽  
pp. 107760
Author(s):  
Umatheny Umatheva ◽  
Braden Sweeting ◽  
Léo Sauvaget ◽  
Nerissa Dela Rosa ◽  
John Riley ◽  
...  
Keyword(s):  
Virulence Factor ◽  
Bacterial Virulence ◽  
Affinity Ligands ◽  
High Affinity ◽  
Bacterial Virulence Factor

scholarly journals Secretion of a bacterial virulence factor is driven by the folding of a C-terminal segment

2010 ◽  
Vol 107 (41) ◽  
pp. 17739-17744 ◽  
Author(s):  
Janine H. Peterson ◽  
Pu Tian ◽  
Raffaele Ieva ◽  
Nathalie Dautin ◽  
Harris D. Bernstein
Keyword(s):  
Virulence Factor ◽  
Terminal Segment ◽  
Bacterial Virulence ◽  
Bacterial Virulence Factor

Dual function of coronatine as a bacterial virulence factor against plants: possible COI1–JAZ-independent role

RSC Advances ◽  
2016 ◽  
Vol 6 (23) ◽  
pp. 19404-19412 ◽  
Author(s):  
Syusuke Egoshi ◽  
Yousuke Takaoka ◽  
Hiroaki Saito ◽  
Yuuki Nukadzuka ◽  
Kengo Hayashi ◽  
...  
Keyword(s):  
Virulence Factor ◽  
Mode Of Action ◽  
Bacterial Virulence ◽  
Dual Function ◽  
Dual Mode ◽  
Bacterial Virulence Factor

A phytotoxin coronatine has a dual mode of action, triggering stomatal reopening through COI1–JAZ-dependent and independent pathways.

scholarly journals Active-Site Flexibility and Substrate Specificity in a Bacterial Virulence Factor: Crystallographic Snapshots of an Epoxide Hydrolase

Structure ◽  
2017 ◽  
Vol 25 (5) ◽  
pp. 697-707.e4 ◽  
Author(s):  
Kelli L. Hvorecny ◽  
Christopher D. Bahl ◽  
Seiya Kitamura ◽  
Kin Sing Stephen Lee ◽  
Bruce D. Hammock ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Virulence Factor ◽  
Active Site ◽  
Epoxide Hydrolase ◽  
Bacterial Virulence ◽  
Bacterial Virulence Factor

scholarly journals Chicoric acid binds to two sites and decreases the activity of the YopH bacterial virulence factor

Oncotarget ◽  
2016 ◽  
Vol 7 (3) ◽  
pp. 2229-2238 ◽  
Author(s):  
Alicja Kuban-Jankowska ◽  
Kamlesh K. Sahu ◽  
Magdalena Gorska ◽  
Jack A. Tuszynski ◽  
Michal Wozniak
Keyword(s):  
Virulence Factor ◽  
Bacterial Virulence ◽  
Chicoric Acid ◽  
Bacterial Virulence Factor

scholarly journals Human C4b-binding Protein, Structural Basis for Interaction with Streptococcal M Protein, a Major Bacterial Virulence Factor

2005 ◽  
Vol 281 (6) ◽  
pp. 3690-3697 ◽  
Author(s):  
Huw T. Jenkins ◽  
Linda Mark ◽  
Graeme Ball ◽  
Jenny Persson ◽  
Gunnar Lindahl ◽  
...  
Keyword(s):  
Virulence Factor ◽  
Binding Protein ◽  
Protein A ◽  
Bacterial Virulence ◽  
M Protein ◽  
Structural Basis ◽  
Streptococcal M Protein ◽  
Bacterial Virulence Factor

Membrane Targeting of a Bacterial Virulence Factor Harbouring an Extended Signal Peptide

2004 ◽  
Vol 8 (1) ◽  
pp. 7-18 ◽  
Author(s):  
Nina Chevalier ◽  
Michael Moser ◽  
Hans-Georg Koch ◽  
Karl-Ludwig Schimz ◽  
Eve Willery ◽  
...  
Keyword(s):  
Virulence Factor ◽  
Signal Peptide ◽  
Bacterial Virulence ◽  
Membrane Targeting ◽  
Bacterial Virulence Factor
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