The metalloprotease of Listeria monocytogenes controls cell wall translocation of the broad-range phospholipase C.
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The Metalloprotease Mpl Supports Listeria monocytogenes Dissemination through Resolution of Membrane Protrusions into VacuolesListeria monocytogenes PrsA2 is required for virulence factor secretion and bacterial viability within the host cell cytosol.Differential function of Listeria monocytogenes listeriolysin O and phospholipases C in vacuolar dissolution following cell-to-cell spread.Functional analysis of the Listeria monocytogenes secretion chaperone PrsA2 and its multiple contributions to bacterial virulence.Posttranslocation chaperone PrsA2 regulates the maturation and secretion of Listeria monocytogenes proprotein virulence factorsCompartmentalization of the broad-range phospholipase C activity to the spreading vacuole is critical for Listeria monocytogenes virulence.Protein transport across the cell wall of monoderm Gram-positive bacteria.Differentiation of propeptide residues regulating the compartmentalization, maturation and activity of the broad-range phospholipase C of Listeria monocytogenes.Recombinant broad-range phospholipase C from Listeria monocytogenes exhibits optimal activity at acidic pH.From hot dogs to host cells: how the bacterial pathogen Listeria monocytogenes regulates virulence gene expression.Development of a mariner-based transposon and identification of Listeria monocytogenes determinants, including the peptidyl-prolyl isomerase PrsA2, that contribute to its hemolytic phenotype.The posttranslocation chaperone PrsA2 contributes to multiple facets of Listeria monocytogenes pathogenesisMembrane chaperone SecDF plays a role in the secretion of Listeria monocytogenes major virulence factors.Propeptides as modulators of functional activity of proteases.The metalloprotease of Listeria monocytogenes is regulated by pH.Listeria monocytogenes phosphatidylinositol-specific phospholipase C: Kinetic activation and homing in on different interfaces.A non-catalytic histidine residue influences the function of the metalloprotease of Listeria monocytogenes.The metalloprotease of Listeria monocytogenes is activated by intramolecular autocatalysis.The propeptide of the metalloprotease of Listeria monocytogenes controls compartmentalization of the zymogen during intracellular infection.Listeriolysin O mediates cytotoxicity against human brain microvascular endothelial cells.
P2860
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P2860
The metalloprotease of Listeria monocytogenes controls cell wall translocation of the broad-range phospholipase C.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
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2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
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2005年學術文章
@zh-hant
name
The metalloprotease of Listeri ...... e broad-range phospholipase C.
@en
type
label
The metalloprotease of Listeri ...... e broad-range phospholipase C.
@en
prefLabel
The metalloprotease of Listeri ...... e broad-range phospholipase C.
@en
P2093
P2860
P1476
The metalloprotease of Listeri ...... e broad-range phospholipase C.
@en
P2093
Hélène Marquis
Nicholas Zagorski
P S Marie Yeung
P2860
P304
P356
10.1128/JB.187.8.2601-2608.2005
P577
2005-04-01T00:00:00Z