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Pathogenicity and Virulence
Published in Julius P. Kreier, Infection, Resistance, and Immunity, 2022
Listeria monocytogenes induces its own endocytosis by epithelial cells via an 80kD surface protein, internalin A, that binds to E-cadherin, a cell adhesion molecule that normally functions as a receptor for one of the integrins. The binding of internalin to its receptor initiates a “zippering” of the host cell membrane around the bacterial cell and the subsequent internalization of the microbe within a host membrane-bound vesicle. Internalin B, another member of the internalin family, enables L. monocytogenes to enter hepatacytes. The receptor for this invasin has not yet been determined.
Mucosal interactions with enteropathogenic bacteria
Published in Phillip D. Smith, Richard S. Blumberg, Thomas T. MacDonald, Principles of Mucosal Immunology, 2020
Nadine Cerf-Bensussan, Pamela Schnupf, Valérie Gaboriau-Routhiau, Philippe J. Sansonetti
Listeria monocytogenes is a food-borne gram-positive bacterium that makes use of two surface proteins, Internalin A and B, to engage in a species-specific manner host adhesion molecules E-cadherin and hepatocyte growth factor receptor Met, respectively, and to induce its internalization. After entry within epithelial cells, L. monocytogenes can spread from cell to cell and disseminate to its target organs, the blood-brain and placental barriers in humans. Analysis of inl mutants indicates that only Internalin A is critical for crossing the intestinal epithelial barrier. Internalin A and B both participate in a minor way to bacterial crossing of the placenta, while another recently described internalin, InlP, is critical. Internalin A is covalently anchored to the bacterial surface and possesses a leucine-rich repeat that interacts with the first ectodomain of human E-cadherin, a transmembrane glycoprotein that mediates homophilic interactions below tight junctions of polarized epithelial cells and is inaccessible to luminal bacteria. However, L. monocytogenes is able to use E-cadherin that is luminally accessible around mucus-expelling goblet cells to hijack the endogenous transcytosis pathway in goblet cells in order to reach the basolateral side of the intestinal epithelial monolayer. The Internalin A and E-cadherin interaction and molecular details of the signaling pathways involved in L. monocytogenes epithelial cell entry have been well characterized (see Figure 25.4).
Listeria monocytogenes
Published in Dongyou Liu, Laboratory Models for Foodborne Infections, 2017
L. monocytogenes mediates its own uptake into nonphagocytic cells via a family of surface-exposed proteins called internalins. Internalin A (InlA) binds to E-cadherin and internalin B (InlB) binds to c-Met, and engagement of these receptors results in bacterial internalization via clathrin-mediated endocytosis.16L. monocytogenes contained within host cell phagocytic or endocytic vacuoles produces listeriolysin O (LLO), a cholesterol-dependent pore-forming toxin that lyses the vacuole, releasing the bacterium into the cytosol.17–19L. monocytogenes multiplies rapidly in the cytosol and begins to nucleate actin filaments via the surface-exposed protein ActA. L. monocytogenes can move through the cytoplasm by actin-based motility towards the cell membrane and can be enveloped in pseudopod-like structures and then phagocytosed by neighboring cells.20,21 This results in a cell-to-cell spread of L. monocytogenes without exposure to the extracellular environment.
Downbeat Nystagmus as a Presenting Manifestation of Neurolisteriosis in a Pregnant Woman
Published in Neuro-Ophthalmology, 2023
Ritwik Ghosh, Moisés León-Ruiz, Sona Singh Sardar, Padavi Lalsing D, Julián Benito-León
Maternal-neonatal listeriosis is mostly reported during the second and third trimesters of pregnancy, as sporadic cases or in the context of outbreaks.5 Pregnancy-associated listeriosis can lead to devastating consequences to premature and newborn babies.5 Timely diagnosis and treatment should be performed in neonates.5 Early detection of LM-infected cases, particularly in the prenatal stage, remains a major challenge.5 Strains belonging to clonal complexes 1, 4, and 6, classified as hypervirulent clones, are mostly associated with maternal-neonatal listeriosis.5 Maternal-neonatal listeriosis is a direct consequence of LM-specific placental tropism, which is mediated by the conjugated action of two proteins of LM, the Internalins A and B, at the placental barrier.5 Other key virulence factors of LM, such as the actin assembly-inducing protein and the listeriolysin O, are also involved in LM replication in the placental and dissemination into fetal tissues in a non-specific manner, as is Internalin P.5 LM pathogenicity island 4 is also involved in placental and CNS infection by unknown mechanisms.10
Fatal Listeria monocytogenes septicemia and meningitis complicated by Candida glabrata fungemia: a case report
Published in Current Medical Research and Opinion, 2022
Pierfrancesco Grima, Caterina Urciuoli, Giuseppe Simone, Anna Gloria Palazzo, Milva Nuzzo, Maurizio Quarta, Immacolata Carraturo, Anna Maria Maci, Salvatore Marinaci, Gerolamo Portaccio, Marcello Guido, Antonella Zizza, Anacleto Romano
It crosses the intestinal epithelium barrier, colonizes the gut lumen, and, can infect the spleen and liver. The internalin A (InlA), a protein on the bacterial surface, interacts with E-cadherin (Ecad), a receptor of the host surface, and allows the bacterium to enter into intestinal epithelial cells. The Listeria adhesion protein (LAP) binding to the surface receptor, Hsp60, initiates a complex signaling cascade, which leads to the cellular redistribution of cell-to-cell junctional proteins for the translocation of L. monocytogenes. These pathways allow for L. monocytogenes to bypass the intestinal barrier and successfully infect the host.2,3
Regulation of Th17 cells by P. UF1 against systemic Listeria monocytogenes infection
Published in Gut Microbes, 2018
Natacha Colliou, Yong Ge, Minghao Gong, Mojgan Zadeh, Jing Li, Francis Alonzo, Mansour Mohamadzadeh
The transformations of the P. UF1 were performed, as described previously.8 The Listeria monocytogenes 10403S (L. m) harbors two amino acid substitutions in the bacterial invasion protein, Internalin A (InlAm- S192N, Y363S), thereby rendering the bacterium more efficient at invading murine gut epithelial cells.5,9,10L. m was grown in Brain Heart Infusion (BHI) medium (Difco Laboratories, 299070) at 37°C. Antibiotics were added at the following final concentrations: 5 μg/mL chloramphenicol and 1 mg/mL hygromycin B (Corning, 30–240CR) for P. UF1 strains; 200 µg/mL streptomycin (Fisher, BP910-5) for L. m.