scholarly journals Listeria monocytogenes Relies on the Heme-Regulated Transporter hrtAB to Resist Heme Toxicity and Uses Heme as a Signal to Induce Transcription of lmo1634, Encoding Listeria Adhesion Protein

2018 ◽  
Vol 9 ◽  
Author(s):  
Patrícia Teixeira dos Santos ◽  
Pernille Tholund Larsen ◽  
Pilar Menendez-Gil ◽  
Eva Maria Sternkopf Lillebæk ◽  
Birgitte Haahr Kallipolitis
Keyword(s):  
Listeria Monocytogenes ◽  
Adhesion Protein ◽  
Listeria Adhesion Protein

scholarly journals Listeria adhesion protein-expressing bioengineered probiotics prevent fetoplacental transmission of Listeria monocytogenes in a pregnant Guinea pig model

2021 ◽  
Vol 151 ◽  
pp. 104752
Author(s):  
Valerie E. Ryan ◽  
Taylor W. Bailey ◽  
Dongqi Liu ◽  
Tracy Vemulapalli ◽  
Bruce Cooper ◽  
...  
Keyword(s):  
Listeria Monocytogenes ◽  
Guinea Pig ◽  
Pig Model ◽  
Adhesion Protein ◽  
Listeria Adhesion Protein ◽  
Guinea Pig Model

scholarly journals Recombinant Probiotic Expressing Listeria Adhesion Protein Attenuates Listeria monocytogenes Virulence In Vitro

PLoS ONE ◽  
2012 ◽  
Vol 7 (1) ◽  
pp. e29277 ◽  
Author(s):  
Ok Kyung Koo ◽  
Mary Anne Roshni Amalaradjou ◽  
Arun K. Bhunia
Keyword(s):  
Listeria Monocytogenes ◽  
Adhesion Protein ◽  
Listeria Adhesion Protein

scholarly journals Listeria monocytogenes Uses Listeria Adhesion Protein (LAP) To Promote Bacterial Transepithelial Translocation and Induces Expression of LAP Receptor Hsp60

2010 ◽  
Vol 78 (12) ◽  
pp. 5062-5073 ◽  
Author(s):  
Kristin M. Burkholder ◽  
Arun K. Bhunia
Keyword(s):  
Plasma Membrane ◽  
Listeria Monocytogenes ◽  
Stress Response ◽  
Cell Model ◽  
Infection Process ◽  
Intestinal Epithelial ◽  
Necrosis Factor Alpha ◽  
Adhesion Protein ◽  
Hsp60 Expression

ABSTRACT Listeria monocytogenes interaction with the intestinal epithelium is a key step in the infection process. We demonstrated that Listeria adhesion protein (LAP) promotes adhesion to intestinal epithelial cells and facilitates extraintestinal dissemination in vivo. The LAP receptor is a stress response protein, Hsp60, but the precise role for the LAP-Hsp60 interaction during Listeria infection is unknown. Here we investigated the influence of physiological stressors and Listeria infection on host Hsp60 expression and LAP-mediated bacterial adhesion, invasion, and transepithelial translocation in an enterocyte-like Caco-2 cell model. Stressors such as heat (41°C), tumor necrosis factor alpha (TNF-α) (100 U), and L. monocytogenes infection (104 to 106 CFU/ml) significantly (P < 0.05) increased plasma membrane and intracellular Hsp60 levels in Caco-2 cells and consequently enhanced LAP-mediated L. monocytogenes adhesion but not invasion of Caco-2 cells. In transepithelial translocation experiments, the wild type (WT) exhibited 2.7-fold more translocation through Caco-2 monolayers than a lap mutant, suggesting that LAP is involved in transepithelial translocation, potentially via a paracellular route. Short hairpin RNA (shRNA) suppression of Hsp60 in Caco-2 cells reduced WT adhesion and translocation 4.5- and 3-fold, respectively, while adhesion remained unchanged for the lap mutant. Conversely, overexpression of Hsp60 in Caco-2 cells enhanced WT adhesion and transepithelial translocation, but not those of the lap mutant. Furthermore, initial infection with a low dosage (106 CFU/ml) of L. monocytogenes increased plasma membrane and intracellular expression of Hsp60 significantly, which rendered Caco-2 cells more susceptible to subsequent LAP-mediated adhesion and translocation. These data provide insight into the role of LAP as a virulence factor during intestinal epithelial infection and pose new questions regarding the dynamics between the host stress response and pathogen infection.

scholarly journals N-Terminal Gly224–Gly411 Domain in Listeria Adhesion Protein Interacts with Host Receptor Hsp60

PLoS ONE ◽  
2011 ◽  
Vol 6 (6) ◽  
pp. e20694 ◽  
Author(s):  
Balamurugan Jagadeesan ◽  
Amy E. Fleishman Littlejohn ◽  
Mary Anne Roshni Amalaradjou ◽  
Atul K. Singh ◽  
Krishna K. Mishra ◽  
...  
Keyword(s):  
Adhesion Protein ◽  
Listeria Adhesion Protein

scholarly journals Glucose and Nutrient Concentrations Affect the Expression of a 104-Kilodalton Listeria Adhesion Protein in Listeria monocytogenes

2002 ◽  
Vol 68 (10) ◽  
pp. 4876-4883 ◽  
Author(s):  
Ziad W. Jaradat ◽  
Arun K. Bhunia
Keyword(s):  
Listeria Monocytogenes ◽  
Brain Heart Infusion ◽  
Luria Bertani ◽  
Nutrient Concentrations ◽  
Enzyme Linked Immunosorbent Assay ◽  
Growth Media ◽  
Adhesion Protein ◽  
Sugar Fermentation ◽  
Rich Media ◽  
High Concentrations

ABSTRACT Growth media and environmental conditions influence the expression of adhesion and invasion proteins in Listeria monocytogenes. Here, the expression of the 104-kDa Listeria adhesion protein (LAP) was studied in nutrient-rich media (Trypticase soy broth [TSB] and brain heart infusion [BHI]), minimal medium (Luria-Bertani [LB]), or nutrient-deficient medium (peptone water [PW]) by immunoblotting, enzyme-linked immunosorbent assay (ELISA), and immunoelectron microscopy. Also, the effect of incorporating different concentrations of glucose on LAP expression was studied. Immunoblotting showed that LAP expression was at least twofold higher in LB medium than in TSB or BHI, while PW supported very poor cell growth and LAP expression. ELISA and immunoblotting results showed that higher concentrations of glucose (>1.6 g/liter) lowered the culture pH and suppressed LAP expression by more than 75%; however, the addition of K2HPO4 reduced this effect. L. monocytogenes cells grown in LB media with lower concentrations of glucose showed higher adhesion to Caco-2 cells (3,716 and 4,186 cpm of attached bacteria for 0 and 0.2 g of glucose/liter, respectively), while L. monocytogenes cells grown in LB with higher glucose concentrations exhibited lower adhesion (2,126 and 2,221 cpm for 1.6 and 3.2 g of glucose/liter, respectively). A LAP-negative L. monocytogenes strain (A572) showed low adhesion profiles regardless of the amount of glucose added. Transmission electron microscopy revealed that LAP is localized mainly in the cytoplasm, with only a few molecules located on the cell surface. Growth in LB with high glucose (3.2 g/liter) showed the presence of only a few molecules in the cells, corroborating the results observed with ELISA or immunoblotting. In summary, nutrient-rich media and high concentrations of glucose suppressed LAP expression, which possibly is due to the changes in the pH of the media during growth from the accumulation of sugar fermentation by-products.

scholarly journals Expression of Surface Protein LapB by a Wide Spectrum of Listeria monocytogenes Serotypes as Demonstrated with Anti-LapB Monoclonal Antibodies

2016 ◽  
Vol 82 (22) ◽  
pp. 6768-6778 ◽  
Author(s):  
Teela Boivin ◽  
Cathie Elmgren ◽  
Brian W. Brooks ◽  
Hongsheng Huang ◽  
Franco Pagotto ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Listeria Monocytogenes ◽  
Bioinformatics Analysis ◽  
Polyclonal Antibodies ◽  
Surface Protein ◽  
Surface Proteins ◽  
Content Type ◽  
Adhesion Protein ◽  
Gene Coding ◽  
Protein B

ABSTRACTProtein antigens expressed on the surface of all strains ofListeria monocytogenesand absent from nonpathogenicListeriaspp. are presumably useful targets for pathogen identification, detection, and isolation using specific antibodies (Abs). To seek such surface proteins expressed in various strains ofL. monocytogenesfor diagnostic applications, we focused on a set of surface proteins known to be involved or putatively involved inL. monocytogenesvirulence and identifiedListeriaadhesion protein B (LapB) as a candidate based on the bioinformatics analysis of whole-genome sequences showing that the gene coding for LapB was present inL. monocytogenesstrains and absent from strains of otherListeriaspp. Immunofluorescence microscopy (IFM), performed with rabbit polyclonal antibodies against the recombinant LapB protein (rLapB) ofL. monocytogenesserotype 4b strain L10521, confirmed expression of LapB on the surface. A panel of 48 mouse monoclonal antibodies (MAbs) to rLaB was generated, and 7 of them bound strongly to the surface ofL. monocytogenescells as demonstrated using IFM. Further characterization of these 7 anti-LapB MAbs, using an enzyme-linked immunosorbent assay (ELISA), revealed that 6 anti-LapB MAbs (M3484, M3495, M3500, M3509, M3517, and M3519) reacted strongly with 46 (86.8%) of 53 strains representing 10 of the 12 serotypes tested (1/2a, 1/2b, 1/2c, 3a, 3b, 3c, 4ab, 4b, 4d, and 4e). These results indicate that LapB, together with companion anti-LapB MAbs, can be targeted as a biomarker for the detection and isolation of variousL. monocytogenesstrains from contaminated foods.IMPORTANCEStrains ofL. monocytogenesare traditionally grouped into serotypes. Identification of a surface protein expressed in all or the majority of at least 12 serotypes would aid in the development of surface-binding monoclonal antibodies (MAbs) for detection and isolation ofL. monocytogenesfrom foods. Bioinformatics analysis revealed that the gene coding forListeriaadhesion protein B (LapB), a surface protein involved inL. monocytogenesvirulence, was present inL. monocytogenesstrains and absent from otherListeriaspp. Polyclonal antibodies against recombinant LapB (rLapB) detected the exposed epitopes on the surface ofL. monocytogenes. Production and extensive assessment of 48 MAbs to rLapB showed that 6 anti-LapB MAbs (M3484, M3495, M3500, M3509, M3517, and M3519) detected the expression of LapB in a wide range ofL. monocytogenesisolates representing 10 of 12 serotypes tested, suggesting that LapB, together with specific MAbs, can be targeted as a biomarker for pathogen detection and isolation.

Sign in / Sign up

Export Citation Format

Share Document