Reduced virulence of a Listeria monocytogenes phospholipase-deficient mutant obtained by transposon insertion into the zinc metalloprotease gene.
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Invasion of the central nervous system by intracellular bacteriaThe three extra-cellular zinc metalloproteinases of Streptococcus pneumoniae have a different impact on virulence in miceBiochemical and molecular analysis of phospholipase C and phospholipase D activity in mycobacteriaLocalization of the ActA polypeptide of Listeria monocytogenes in infected tissue culture cell lines: ActA is not associated with actin "comets".Activation of the human complement alternative pathway by Listeria monocytogenes: evidence for direct binding and proteolysis of the C3 component on bacteriaThe zinc metalloprotease of Listeria monocytogenes is required for maturation of phosphatidylcholine phospholipase C: direct evidence obtained by gene complementation.Modulation of enzymatic activity and biological function of Listeria monocytogenes broad-range phospholipase C by amino acid substitutions and by replacement with the Bacillus cereus orthologPhosphatidylcholine-specific phospholipase C from Listeria monocytogenes is an important virulence factor in murine cerebral listeriosis.Listeria pathogenesis and molecular virulence determinantsIdentification of Listeria monocytogenes in vivo-induced genes by fluorescence-activated cell sortingBacterial extracellular zinc-containing metalloproteasesListeria monocytogenes PrsA2 is required for virulence factor secretion and bacterial viability within the host cell cytosol.Molecular determinants of Listeria monocytogenes pathogenesisThe broad-range phospholipase C and a metalloprotease mediate listeriolysin O-independent escape of Listeria monocytogenes from a primary vacuole in human epithelial cellsListeria monocytogenes can grow in macrophages without the aid of proteins induced by environmental stresses.Differences in virulence and in expression of PrfA and PrfA-regulated virulence genes of Listeria monocytogenes strains belonging to serogroup 4.pH-regulated activation and release of a bacteria-associated phospholipase C during intracellular infection by Listeria monocytogenes.Compartmentalization of the broad-range phospholipase C activity to the spreading vacuole is critical for Listeria monocytogenes virulence.Proteolytic pathways of activation and degradation of a bacterial phospholipase C during intracellular infection by Listeria monocytogenes.Differentiation of propeptide residues regulating the compartmentalization, maturation and activity of the broad-range phospholipase C of Listeria monocytogenes.Requirement of the Listeria monocytogenes broad-range phospholipase PC-PLC during infection of human epithelial cells.Listeria monocytogenes infection of P388D1 macrophages results in a biphasic NF-kappaB (RelA/p50) activation induced by lipoteichoic acid and bacterial phospholipases and mediated by IkappaBalpha and IkappaBbeta degradation.Recombinant broad-range phospholipase C from Listeria monocytogenes exhibits optimal activity at acidic pH.Dual roles of plcA in Listeria monocytogenes pathogenesisCloning of a metalloprotease gene involved in the virulence mechanism of Vibrio anguillarum.Induction of protective T cells against Listeria monocytogenes in mice by immunization with a listeriolysin O-negative avirulent strain of bacteria and liposome-encapsulated listeriolysin O.Utilization of oligopeptides by Listeria monocytogenes Scott A.A di- and tripeptide transport system can supply Listeria monocytogenes Scott A with amino acids essential for growth.Induction of cytokine gene expression by listeriolysin O and roles of macrophages and NK cellsRestricted translocation across the cell wall regulates secretion of the broad-range phospholipase C of Listeria monocytogenes.Cytokine gene expression in mice at an early stage of infection with various strains of Listeria spp. differing in virulence.The metalloprotease of Listeria monocytogenes controls cell wall translocation of the broad-range phospholipase C.A non-catalytic histidine residue influences the function of the metalloprotease of Listeria monocytogenes.The propeptide of the metalloprotease of Listeria monocytogenes controls compartmentalization of the zymogen during intracellular infection.
P2860
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P2860
Reduced virulence of a Listeria monocytogenes phospholipase-deficient mutant obtained by transposon insertion into the zinc metalloprotease gene.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
1992年论文
@zh
1992年论文
@zh-cn
name
Reduced virulence of a Listeri ...... the zinc metalloprotease gene.
@en
type
label
Reduced virulence of a Listeri ...... the zinc metalloprotease gene.
@en
prefLabel
Reduced virulence of a Listeri ...... the zinc metalloprotease gene.
@en
P2093
P2860
P1476
Reduced virulence of a Listeri ...... the zinc metalloprotease gene.
@en
P2093
Beretti JL
Gaillard JL
Geoffroy C
Raveneau J
P2860
P304
P407
P577
1992-03-01T00:00:00Z