A Method for Purification of Listeriolysin O from a Hypersecretor Strain ofListeria monocytogenes

1999 ◽  
Vol 15 (2) ◽  
pp. 243-245 ◽  
Author(s):  
Cherie M. Walton ◽  
Catherine H. Wu ◽  
George Y. Wu
Keyword(s):  
Listeriolysin O ◽  
Oflisteria Monocytogenes

scholarly journals Role of Listeriolysin O in Cell-to-Cell Spread ofListeria monocytogenes

2000 ◽  
Vol 68 (2) ◽  
pp. 999-1003 ◽  
Author(s):  
Margaret M. Gedde ◽  
Darren E. Higgins ◽  
Lewis G. Tilney ◽  
Daniel A. Portnoy
Keyword(s):  
Bacterial Pathogen ◽  
Listeriolysin O ◽  
Genetic Approach ◽  
Wild Type ◽  
Intracellular Growth ◽  
Double Membrane ◽  
Vacuolar Compartment ◽  
Oflisteria Monocytogenes ◽  
Cell Spread

ABSTRACT Listeria monocytogenes is a facultative intracellular bacterial pathogen that escapes from a host vacuolar compartment and grows rapidly in the cytosol. Listeriolysin O (LLO) is a secreted pore-forming protein essential for the escape of L. monocytogenes from the vacuole formed upon initial internalization. However, its role in intracellular growth and cell-to-cell spread events has not been testable by a genetic approach. In this study, purified six-His-tagged LLO (HisLLO) was noncovalently coupled to the surface of nickel-treated LLO-negative mutants. Bound LLO mediated vacuolar escape in approximately 2% of the mutants. After 5.5 h of growth, cytosolic bacteria were indistinguishable from wild-type bacteria with regard to formation of pseudopod-like extensions, here termed listeriopods, and spread to adjacent cells. However, bacteria in adjacent cells failed to multiply and were found in double-membrane vacuoles. Addition of bound LLO to mutants lacking LLO and two distinct phospholipases C (PLCs) also resulted in spread to adjacent cells, but these triple mutants became trapped in multiple-membrane vacuoles that are reminiscent of autophagocytic vacuoles. These studies show that neither LLO nor the PLCs are necessary for listeriopod formation and uptake of bacteria into neighboring cells but that LLO is required for the escape ofL. monocytogenes from the double-membrane vacuole that forms upon cell-to-cell spread.

scholarly journals Critical role of the N-terminal residues of listeriolysin O in phagosomal escape and virulence ofListeria monocytogenes

2002 ◽  
Vol 46 (2) ◽  
pp. 367-379 ◽  
Author(s):  
Marie-Annick Lety ◽  
Claude Frehel ◽  
Patrick Berche ◽  
Alain Charbit
Keyword(s):  
Critical Role ◽  
Listeriolysin O ◽  
Oflisteria Monocytogenes

scholarly journals Stress-Induced ClpP Serine Protease ofListeria monocytogenes Is Essential for Induction of Listeriolysin O-Dependent Protective Immunity

2001 ◽  
Vol 69 (8) ◽  
pp. 4938-4943 ◽  
Author(s):  
Olivier Gaillot ◽  
Søren Bregenholt ◽  
Francis Jaubert ◽  
James P. Di Santo ◽  
Patrick Berche
Keyword(s):  
Immune Response ◽  
Serine Protease ◽  
Protective Immunity ◽  
Listeriolysin O ◽  
Intracellular Growth ◽  
Lethal Challenge ◽  
Protective Antigens ◽  
Oflisteria Monocytogenes

ABSTRACT The stress-induced protease ClpP is required for virulence of the facultative intracellular pathogen Listeria monocytogenes. We previously found that in the absence of ClpP, the virulence of this pathogen was strongly reduced, mainly due to the decreased production of functional listeriolysin O (LLO), a major immunodominant virulence factor promoting intracellular growth. In this work, a clpP deletion mutant of L. monocytogenes was used to study the generation of anti-Listeria protective immunity. We found that ClpP is required for the intracellular growth of L. monocytogenes in resident macrophages in vivo. Mice infected with doses as high as 106 clpP mutant bacteria were not protected against a lethal challenge of wild-type bacteria and did not develop any detectable LLO-specific cytolytic T cells or antibodies, suggesting that the amount of LLO produced in infected mice under these conditions was too low to induce a specific immune response. However, in contrast to the results obtained with a mutant with a disrupted hly gene, this lack of protection was overcome by inoculation of very high infecting doses ofclpP mutant bacteria (5 × 108), thus producing sufficient amounts of LLO to stimulate anti-Listeria immunity. The role of ClpP was confirmed by showing that anti-Listeria immunity was restored in mice infected with a clpP-complemented mutant. These results indicate that the stress-induced serine protease ClpP is a potential target for modulating the presentation of protective antigens such as LLO and thereby the immune response against L. monocytogenes.

Myricetin Preferentially Binds to Interfacial Regions in Domains 1 – 3 to Inhibit Cholesterol-Dependent Cytolysins: A Molecular Docking Study

2020 ◽  
Author(s):  
Rafael Espiritu
Keyword(s):  
Molecular Docking ◽  
Structural Changes ◽  
Docking Study ◽  
Listeriolysin O ◽  
Molecular Docking Study ◽  
Docking Analysis ◽  
Streptolysin O ◽  
Molecule Inhibitor ◽  
Human Cd59 ◽  
Anthrolysin O

<p>Cholesterol-dependent cytolysins (CDCs) are proteinaceous toxins secreted as monomers by some Gram-positive and Gram-negative bacteria that contribute to their pathogenicity. These toxins bind to either cholesterol or human CD59, leading to massive structural changes, toxin oligomerization, formation of very large pores, and ultimately cell death, making these proteins promising targets for inhibition. Myricetin, and its related flavonoids, have been previously identified as a candidate small molecule inhibitor of specific CDCs such as listeriolysin O (LLO) and suilysin (SLY), interfering with their oligomerization. In this work, molecular docking was performed to assess the interaction of myricetin with other CDCs whose crystal structures are already known. Results indicated that although myricetin bound to the hitherto identified cavity in domain 4 (D4), much more efficient and stable binding was obtained in sites along the interfacial regions of domains 1 – 3 (D1 – D3). This was common among the tested CDCs, which was primarily due to much more extensive stabilizing intermolecular interactions, as indicated by post-docking analysis. Specifically, myricetin bound to (1) the interface of the three domains in anthrolysin O (ALO), perfringolysin O (PFO), pneumolysin (PLY), SLY, and vaginolysin (VLY), (2) at/near the D1/D3 interface in LLO and streptolysin O (SLO), and (3) along the D2/D3 interface in intermedilysin (ILY). These findings provide theoretical basis on the possibility of using myricetin and its related compounds as a broad-spectrum inhibitor of CDCs to potentially address the diseases associated with these pathogens.</p>

Su.78. Analysis of T-Cell Responses to Listeria Monocytogenes Listeriolysin O in Healthy Adults

2006 ◽  
Vol 119 ◽  
pp. S186
Author(s):  
Johannes Hampl ◽  
Shruti Mathur ◽  
Weiqun Liu ◽  
Peter Lauer ◽  
Thomas Dubensky ◽  
...  
Keyword(s):  
Listeria Monocytogenes ◽  
T Cell ◽  
T Cell Responses ◽  
Healthy Adults ◽  
Listeriolysin O ◽  
Cell Responses

scholarly journals Effect of lactic acid bacteria on Listeria monocytogenes infection and innate immunity in rabbits

2020 ◽  
Vol 65 (No. 1) ◽  
pp. 23-30 ◽  
Author(s):  
Heping Zhao ◽  
Feike Zhang ◽  
Jun Chai ◽  
Jianping Wang
Keyword(s):  
Lactic Acid ◽  
Listeria Monocytogenes ◽  
Lactic Acid Bacteria ◽  
Positive Control ◽  
Negative Control ◽  
Listeriolysin O ◽  
Serum Iga ◽  
Probiotic Lactic Acid Bacteria ◽  
Spleen And Lymph Nodes ◽  
Proinflammatory Factors

The present study aimed to investigate the effect of probiotic lactic acid bacteria (LAB) addition on Listeria monocytogenes translocation and its toxin listeriolysin O (LLO), proinflammatory factors, immune organ indexes and serum immunoglobulins in farmed rabbits. Five treatments included negative control (NC), positive control (PC) with L. monocytogenes infection and supplemental LAB at 3.0 × 10<sup>6 </sup>(low-LAB, L-LAB), 3.0 × 10<sup>8</sup> (medium-LAB, M-LAB) and 3.0 × 10<sup>10 </sup>(high-LAB, H-LAB) CFU/kg of diet, respectively. The LAB was a mixture of equal amounts of Lactobacillus acidophilus (ACCC11073), Lactobacillus plantarum (CICC21863) and Enterococcus faecium (CICC20430). A total of 180 weaned rabbits (negative for L. monocytogenes) were randomly assigned to 5 groups with 6 replicates of 6 rabbits each in response to the 5 treatments. L. monocytogenes infection occurred on the first day of feeding trial and dietary LAB supplementation lasted for 14 days. The results showed that on days 7 and 14 post administration, L. monocytogenes in caecum, liver, spleen and lymph nodes was reduced in M-LAB and H-LAB compared to PC (P &lt; 0.05), and linear and quadratic reducing trends were found in liver on day 7 (P ≤ 0.002). On day 14, mucosa LLO mRNA expression and serum TNFα, IL1β and IFNγ were reduced in the three LAB treatments (P &lt; 0.05), and linear and quadratic trends were found on TNFα and IL1β (P ≤ 0.025); indexes of thymus and spleen, serum IgA and IgG were increased in the LAB treatments (P &lt; 0.05). It is concluded that LAB can be used to alleviate L. monocytogenes infection and to improve the immune function of farmed animals.

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