Listeria monocytogenes

Overview

Listeria monocytogenes is a small, Gram-positive rod and the cause of listeriosis, a severe foodborne infection.^[1] It is a facultative intracellular pathogen that thrives in diverse environments, including soil, water, and decaying vegetation, and can grow at refrigeration temperatures (0–4°C). This ability to survive in cold environments allows it to contaminate refrigerated foods like soft cheeses, deli meats, unpasteurized dairy, and produce.^[2] Although listeriosis is rare, it has a high fatality rate, particularly in vulnerable populations, such as pregnant women, neonates, the elderly, and immunocompromised individuals.^[3] In healthy people, it may cause mild gastrointestinal symptoms, but in high-risk groups, it can lead to septicemia, meningitis, or maternal-fetal infections, including miscarriage or stillbirth.^[4] Transmission occurs primarily through the consumption of contaminated food, and L. monocytogenes can survive in cold environments, making refrigeration insufficient to eliminate it. Control measures focus on food safety practices like pasteurization, cooking meats, and preventing cross-contamination.^[5] Taxonomically, L. monocytogenes belongs to the genus Listeria and is classified into several serotypes, with 1/2a, 1/2b, and 4b being the most common human pathogens.^[6]

Antibiotic Resistance

L. monocytogenes has historically remained susceptible to most antibiotics used for Gram-positive infections, and ampicillin (often combined with gentamicin) is still the standard first-line treatment for invasive listeriosis.^[7] A key clinical point is its intrinsic resistance to all cephalosporins, meaning drugs like ceftriaxone are ineffective and empiric meningitis regimens must include ampicillin when Listeria is a concern; it also shows intrinsic reduced susceptibility to agents such as fosfomycin and fusidic acid, partly linked to native determinants like fosX.^[8] Acquired resistance was long considered rare, with early reports emerging in the late 1980s and 1990s mostly involving older antibiotics (e.g., tetracyclines, macrolides, chloramphenicol) and occasional trimethoprim resistance, while resistance to penicillins and gentamicin was uncommon.^[9] More recent surveillance has documented increasing resistance signals (including MDR strains in some regions), likely driven by selective pressures such as antibiotic/biocide exposure and biofilm-associated gene exchange, often involving efflux mechanisms and stress-resistance-linked plasmids.^[10] Importantly, clinical isolates in humans remain largely drug-susceptible, with no consistent evidence of treatment failure due to acquired resistance, and recent reviews still report no clinically meaningful acquired resistance in human disease.^[11] However, Listeria’s capacity to acquire resistance genes via mobile genetic elements (plasmids, transposons, phage-mediated transfer) and to recombine these across strains underscores the need for continued antimicrobial and genomic surveillance to prevent future emergence of clinically problematic resistance.

Pathogenicity

L. monocytogenes is a facultative intracellular pathogen that enters the body through the gastrointestinal tract after ingestion of contaminated food.^[12] It survives harsh stomach acid and bile, aided by acid tolerance genes and bile salt hydrolase enzymes. Once in the intestines, it uses surface proteins, internalins InlA and InlB, to invade non-phagocytic cells, enabling it to cross the intestinal barrier and disseminate via macrophages.^[13] Inside host cells, it escapes phagosomal vacuoles using the pore-forming toxin listeriolysin O (LLO) and phospholipases, allowing it to replicate in the cytoplasm.^[14]L. monocytogenes then utilizes actin-based motility to spread directly from cell to cell, avoiding immune detection. It can cross the blood-brain barrier and the placenta, leading to serious conditions such as meningitis, encephalitis, or fetal infection.^[15] Listeria primarily triggers cell-mediated immunity, relying on T cell responses for clearance, as its intracellular lifestyle limits the effectiveness of antibodies. Its ability to evade immune detection and spread throughout the body makes it a highly invasive and deadly pathogen, particularly in vulnerable populations like pregnant women, neonates, and the immunocompromised.^[16]

Morphology

L. monocytogenes is a small, Gram-positive rod that is motile, β-hemolytic, and catalase-positive, with a unique ability to grow at refrigerator temperatures.^[17][18] It appears as short rods (0.5 × 1–2 µm), often in chains or pairs, and can be mistaken for streptococci on Gram stain.^[19] The bacterium exhibits tumbling motility at room temperature due to peritrichous flagella, which is downregulated at 37°C.^[20] On blood agar, it forms small grey-white colonies with a narrow zone of β-hemolysis, primarily caused by listeriolysin O.^[21]L. monocytogenes is facultative anaerobic, halotolerant (growing in up to 10% NaCl), and can thrive in a wide temperature range (0–45°C), making it resilient in refrigerated, salty foods.^[22] The bacterium is classified into serotypes based on somatic and flagellar antigens, with serotypes 1/2a, 1/2b, and 4b being the primary human pathogens.^[23]

Virulence Factors

L. monocytogenes owes its pathogenicity to a repertoire of virulence factors that mediate each step of infection, from host cell invasion to intracellular survival and spread.

Virulence Factor	Description and Role in Pathogenicity
Internalin A (InlA)	InlA is crucial for crossing the intestinal barrier and the placenta; mutants lacking InlA have reduced invasion of gut and cannot efficiently cause fetoplacental infection.[24] InlA’s species specificity (binds human E-cadherin but not mouse E-cadherin) explains why standard lab mice are relatively resistant to oral Listeria infection.[25]
Internalin B (InlB)	InlB facilitates invasion of a wide range of cell types (hepatocytes, endothelial cells) and contributes to Listeria’s ability to disseminate beyond the intestine.[26]
InlC (Internalin C)	InlC disrupts the host cytoskeleton and cell–cell junctions, facilitating bacterial movement between cells. It also interacts with the IκB kinase complex to dampen NF-κB signaling, reducing proinflammatory responses.[27] InlC is thus considered a virulence factor that helps Listeria evade immune detection and promote cell-to-cell spread in epithelial layers.
Listeriolysin O (LLO)	LLO is acid-activated and perforates the phagosome membrane, allowing Listeria to escape into the host cell cytosol. It also causes the β-hemolysis seen on blood agar. Beyond its role in vacuole escape, LLO can induce apoptosis of host cells and modulate immune responses (high levels of LLO are cytotoxic).[28]
ActA (Actin assembly-inducing protein)	ActA recruits the Arp2/3 complex and promotes formation of an actin “rocket tail” that propels Listeria through the cytoplasm and into adjacent cells. This actin-based motility enables direct cell-to-cell spread, helping Listeria disseminate in tissues while hidden from extracellular immune factors.[29]
Phospholipases C (PlcA & PlcB)	PlcA is a phosphatidylinositol-specific PLC active on the primary phagosome membrane, while PlcB is a broad-spectrum PLC (activated by proteolytic cleavage by Mpl metalloprotease) that helps dissolve the double-membrane vacuole during cell-to-cell spread. Together with LLO, these Plc enzymes enable Listeria to rupture vacuolar membranes and enter the cytosol. Inactivation of plcA or plcB impairs virulence but to a lesser extent than LLO.[30]
PrfA (Positive Regulatory Factor A)	When Listeria enters a host and senses the environment (e.g., via glutathione or other cofactors), PrfA gets activated and upregulates the virulence factors needed for intracellular survival. Mutations that inactivate prfA render Listeria essentially non-virulent since the downstream effectors are not produced.[31]
P60 (Iap, invasion-associated protein)	P60 is also released into the medium and can act as an adhesin – it mediates attachment to host cells and can induce cell invasion (particularly in fibroblasts). Mutants lacking P60 have chaining phenotypes and reduced invasiveness. P60 likely interacts with host receptors or ECM components to promote Listeria entry.[32]
Ami (Autolysin amidase)	Another cell wall hydrolase (autolysin) that, beyond its role in cell wall remodeling, contributes to host cell adhesion. Ami binds to fibronectin on host cells and may assist Listeria in colonizing host surfaces.[33] It has been implicated in the initial attachment of Listeria to intestinal mucosa.
FbpA (Fibronectin-binding protein)	By tethering Listeria to the host extracellular matrix, FbpA can enhance the efficiency of host cell invasion (similar to how some staphylococcal fibronectin-binding proteins work).[34][35] Though not as critical as internalins, FbpA provides an auxiliary pathway for adhesion and invasion.
Listeriolysin S (LLS)	LLS is a small thiol-activated cytotoxin that may enhance survival in the gut by attacking competing microbiota or modulating host cells. LLS contributes to the hypervirulence of certain clonal complexes (e.g. CC4 strains).[36] However, not all L. monocytogenes isolates have LLS.
Stress tolerance factors	Listeria’s ability to cause disease is also aided by general stress-response factors that are not classical “virulence factors” but are necessary for survival in the host. These include SigB (σ^B alternative sigma factor controlling >300 stress genes) which helps Listeria survive acid, osmotic, and oxidative stress[37] bile salt hydrolase (bsh gene) for bile resistance; and antioxidant enzymes like catalase and superoxide dismutase that help the bacterium endure oxidative burst inside macrophages.

Metallomics

Metal ions play a dual and pivotal role in the biology of L. monocytogenes, they are essential nutrients that the bacterium must acquire from the host, yet many metals can be toxic in excess. The term metallomics here refers to how L. monocytogenes manages and utilizes metal ions. Like all pathogens, Listeria must carefully regulate metal homeostasis to survive both in the external environment and inside a host

Metal / Ion	Key Features in L. monocytogenes
Iron (Fe)	Iron is essential for Listeria (cofactor in enzymes, electron transport, etc.), but host tissues strictly limit free iron through nutritional immunity.[38]L. monocytogenes does not produce its own siderophore, yet it has multiple systems to scavenge iron from the host. It can uptake ferric iron bound to siderophores (e.g. via the Fhu receptor for ferrichrome siderophores) and can utilize heme and hemoglobin as iron sources (via the HupDGC heme uptake system).[39] Iron acquisition is regulated by the Ferric Uptake Regulator Fur, which represses iron transport genes when iron is plentiful.[40] Inside the host, Listeria induces siderophore receptors and heme-binding proteins to steal iron from transferrin, lactoferrin, or hemoglobin.[41]
Manganese (Mn)	Zn is an essential trace element, required for function of numerous proteins (zinc-dependent enzymes, DNA binding proteins, etc.). However, the host manipulates Zn availability during infection: it sequesters Zn in some contexts (zinc sequestration) and uses it as a weapon in others (zinc poisoning in the phagosome). L. monocytogenes is equipped with Zn uptake systems such as ZnuABC/ZinABC (high-affinity zinc transporters) to import zinc when it’s scarce. A Zn-responsive transcriptional regulator Zur senses zinc levels and regulates zinc transporter expression. Inside macrophage phagosomes, the host may pump in excess Zn2+ as an antimicrobial stress – Listeria’s defense includes efflux pumps and metallothionein-like proteins to handle Zn toxicity. In fact, L. monocytogenes has to precisely control cellular Zn, as noted in studies highlighting that dysregulation of Zn homeostasis severely impairs its growth.
Zinc (Zn)	Zn is an essential trace element, required for function of numerous proteins. However, the host manipulates Zn availability during infection: it sequesters Zn in some contexts (zinc sequestration) and uses it as a weapon in others (zinc poisoning in the phagosome).[42]L. monocytogenes is equipped with Zn uptake systems such as ZnuABC/ZinABC (high-affinity zinc transporters) to import zinc when it’s scarce. A Zn-responsive transcriptional regulator Zur senses zinc levels and regulates zinc transporter expression.[43]
Copper (Cu)	Copper is a redox-active metal that is essential in small amounts but highly toxic when in excess. The host exploits Cu toxicity as a microbial poison, for instance, macrophages pump Cu into phagolysosomes to kill engulfed bacteria.[44]L. monocytogenes therefore must expel or sequester excess copper. It possesses a copper efflux ATPase CopA and a copper chaperone CopZ, which together remove Cu+ from the cytoplasm. A copper-responsive repressor CsoR regulates the expression of these copper resistance genes.[45] Interestingly, L. monocytogenes is notably copper-tolerant compared to many Gram-positives – one study found it had the highest copper resistance among tested Listeria, Enterococcus, Streptococcus, and Bacillus species.[46] Excess Cu damages proteins and membranes via oxidative mechanisms; Listeria’s strategies (CopA efflux, likely periplasmic Cu-binding) mitigate this.[47]
Cadmium (Cd)	Cadmium is a non-essential, toxic heavy metal. Cd^2+ can be encountered in soil, water, or certain foods (from contamination) and also in industrial or agricultural settings. L. monocytogenes has no biological need for cadmium, but many strains carry cadmium resistance determinants to survive Cd exposure. Two main systems are cadmium-efflux pumps encoded by cadA1 and cadA2, usually found on plasmids or genomic islands. cadA encodes a P-type ATPase that extrudes Cd^2+ from the cell, and is often coupled with cadC (a regulatory gene). These were historically so common that cadmium resistance was used as a subtyping marker for Listeria.[48] Surveys show a large fraction of food and clinical isolates (especially serotype 1/2a and 4b) are cadmium-resistant. While cadmium resistance per se may not directly increase virulence, it is hypothesized to contribute to environmental persistence (e.g. in food processing facilities with sanitizer residues). Notably, cadmium resistance genes often reside on the SSI-2 genomic islet or plasmids that also carry other stress resistance genes.[49]
Arsenic (As)	Arsenic is another toxic metalloid thatL. monocytogenes frequently encounters in certain environments (e.g. agricultural soils with arsenate, or contaminated water). Many Listeria strains, particularly those in serotype 4b (epidemic clones), harbor arsenic resistance (ars) operons on the chromosome. The typical ars cluster (e.g. arsRDABC) encodes an arsenate reductase (ArsC) that converts arsenate (As5+) to arsenite (As3+), and an arsenite efflux pump (ArsA/ArsB) that expels the arsenite. Regulatory proteins ArsR and ArsD control expression of the operon. These systems allow Listeria to survive in arsenic-rich soils or animal guts with arsenic compounds.[50]

Vulnerabilities

Notable vulnerabilities of L. monocytogenes and how they could be exploited clinically or in public health. Because Listeria must carefully balance metal uptake and efflux, therapies that alter metal availability (nutrient limitation or intoxication) could tip the balance and inhibit bacterial growth.^[51] Listeria’s reliance on a few indispensable virulence factors (like LLO, ActA) makes it susceptible to strategies that neutralize these factors, similar to defanging the pathogen. The organism is also still largely sensitive to antibiotics, meaning traditional antimicrobial therapy (if administered early) is very effective at clearing infection.^[52] Finally, from a prevention standpoint, Listeria’s lack of hardy spores and its susceptibility to heat and disinfectants make food safety measures (like pasteurization and sanitation) highly effective at controlling it, a clear vulnerability in its otherwise notable hardiness.

Vulnerability of L. monocytogenes	Potential Therapeutic/Preventive Opportunity
Dependence on precise metal homeostasis	Exploiting nutritional immunity by enhancing host metal-binding defenses (e.g. therapeutically supplementing calprotectin or using iron-chelating drugs) could starve the bacteria of needed nutrients. Conversely, delivering toxic levels of copper or zinc in a targeted manner (e.g., copper ionophores) might kill intracellular Listeria. This approach aims to capitalize on Listeria’s Achilles’ heel of requiring a narrow optimal range of metals.[53]
Critical virulence factors are druggable	An exciting proof-of-concept is neutralizing antibodies: passive immunization with monoclonal antibodies against LLO and ActA protected mice from lethal Listeria infection (reducing bacterial load and improving survival).[54] This suggests that targeting Listeria’s virulence factors, either with antibodies or inhibitors, is a viable therapeutic strategy to disarm the pathogen without needing to kill it outright.
Cell-mediated immunity can clear infection	Enhancing the host’s T-cell immune response offers a way to prevent or mitigate listeriosis. There is currently no licensed Listeria vaccine, but experimental vaccines (including live-attenuated Listeria strains, protein subunits, and novel approaches like mRNA vaccines targeting Listeria antigens) are under investigation.[55] For high-risk groups (such as transplant patients or pregnant women), a vaccine inducing strong cellular immunity could be a game-changer.
Broad antibiotic susceptibility	Timely administration of effective antibiotics is highly successful in treating listeriosis, exploiting Listeria’s lack of resistance. Ampicillin (or penicillin G) plus gentamicin is synergistic and bactericidal.[56] In cases of penicillin allergy, TMP-SMX reliably clears Listeria. This vulnerability means that unlike some other superbugs, proper antibiotic therapy almost always works if started early, preventing the bacteria from causing overwhelming infection.[57]

Interventions

Antibiotic regimens (ampicillin ± gentamicin, TMP-SMX) are highly effective treatments, reflecting Listeria’s vulnerability to these drugs.^[58] Novel approaches like phage therapy use Listeria-specific bacteriophages to reduce contamination or even treat infections, offering a precise antibacterial tool.^[59][60] Immunotherapies such as passive antibodies targeting virulence factors demonstrate an alternative way to curb infection without traditional antibiotics. Meanwhile, vaccination is an active area of research aiming to exploit the host’s immune defenses for long-term protection.^[61] Finally, rigorous food safety interventions (pasteurization, disinfection, monitoring) act at the population level to prevent L. monocytogenes exposure in the first place – an arguably most effective “intervention” given the organism’s ubiquity in the environment and high mortality if ingested by susceptible people. Each of these interventions addresses a different weak link in the chain of infection, collectively helping to manage and reduce the threat of listeriosis.

Intervention	Mechanism
Ampicillin + Gentamicin (Standard Antibiotic Therapy)	Clinical standard of care for invasive listeriosis in humans. Ampicillin (an aminopenicillin) 2 g IV q4h plus Gentamicin (an aminoglycoside) 1 mg/kg IV q8h is a typical regimen for synergy.[62] This combination is bactericidal – ampicillin disrupts cell wall synthesis and gentamicin penetrates Listeria’s cell to inhibit protein synthesis. Gentamicin alone doesn’t effectively reach Listeria inside cells, but combined with ampicillin it can enter dying bacteria. Clinical studies and case series have shown excellent survival rates when therapy is started early, especially in meningitis.[63] Ampicillin remains the cornerstone of treatment, with gentamicin providing synergistic kill. The need for ampicillin (or penicillin) is crucial given Listeria’s cephalosporin resistance; many empirical meningitis regimens add ampicillin specifically to cover Listeria.[64]
Trimethoprim-Sulfamethoxazole (TMP-SMX) Alternative	Used in human listeriosis cases when β-lactams are contraindicated (e.g. penicillin-allergic patients). High-dose TMP-SMX IV (e.g. Trimethoprim 10–20 mg/kg/day split q6-12h) is given.[65] TMP-SMX is bactericidal against Listeria in vitro and in vivo, achieving cure in cases of meningitis and brain abscess. For example, a study noted successful outcomes in CNS listeriosis treated with TMP-SMX monotherapy in allergic patients.[66][67]
Listeria-specific Bacteriophages (Phage Biocontrol)	One example is the FDA-approved Listeria phage P100, used as a spray on ready-to-eat foods. Also, custom phage cocktails have been tested in vitro and in animal models. Phage P100 can dramatically reduce L. monocytogenes on food-contact surfaces and in foods (5-log CFU reductions reported on treated products).[68] In a simulated GI model, a phage cocktail significantly protected human gut cells from Listeria invasion, outperforming even ampicillin in reducing intracellular Listeria.[69]
Passive Immunization (Anti-LLO & Anti-ActA antibodies)	In an experimental immunotherapy, mice were given high doses of monoclonal antibodies against Listeria’s listeriolysin O (LLO) and ActA proteins, either before or shortly after a lethal Listeria challenge. Mice that received the antibody cocktail had significantly higher survival than controls when infected with L. monocytogenes.[70] Bacterial counts in spleens and livers were dramatically lower in treated mice. Mechanistically, anti-LLO antibodies neutralized LLO toxin, preventing phagosomal escape (keeping bacteria trapped in vacuoles), while anti-ActA antibodies interfered with actin tail formation and cell-to-cell spread.[71]
Vaccines (Investigational)	Various experimental Listeria vaccines in animal models – including live-attenuated Listeria strains, peptide subunit vaccines, and newer platforms like Listeria antigen-encoding mRNA vaccines.[72] For instance, a live attenuated Listeria candidate (L. monocytogenes with deletions in prfA and other genes) has been tested in rabbits, and an mRNA vaccine design based on Listeria’s immunopeptidome was recently described.[73] Live attenuated vaccines induced robust T-cell responses in animals and protected against subsequent Listeria challenge, preventing death and lowering bacterial burdens.

Research Feed

References

1. Listeria Monocytogenes. [Updated 2023 Jul 4].. Rogalla D, Bomar PA.. (In: StatPearls [Internet]. Treasure Island (FL): StatPearls Publishing; 2025 Jan-.)
2. Listeriosis.. Disson, O., Charlier, C., Pérot, P., Leclercq, A., Paz, R. N., Kathariou, S., Tsai, Y. H., & Lecuit, M. (2025).. (Nature Reviews Disease Primers, 11(1), 71.)
3. Heavy Metal Resistance Determinants of the Foodborne Pathogen Listeria monocytogenes.. Parsons, C., Lee, S., & Kathariou, S. (2018).. (Genes, 10(1).)
4. Pregnancy-associated listeriosis in England and Wales.. AWOFISAYO, A., AMAR, C., RUGGLES, R., ELSON, R., ADAK, G. K., MOOK, P., & GRANT, K. A. (2014).. (Epidemiology and Infection, 143(2), 249.)
5. Listeria monocytogenes Biofilms in the Food Industry: Is the Current Hygiene Program Sufficient to Combat the Persistence of the Pathogen?. Mazaheri, T., H Cervantes-Huamán, B. R., Bermúdez-Capdevila, M., Ripolles-Avila, C., & Rodríguez-Jerez, J. J. (2021).. (Microorganisms, 9(1), 181.)
6. Genomic and pathogenicity islands of Listeria monocytogenes—Overview of selected aspects.. Wiktorczyk-Kapischke, N., Skowron, K., & Wałecka-Zacharska, E. (2023).. (Frontiers in Molecular Biosciences, 10, 1161486.)
7. Gentamicin combination treatment is associated with lower mortality in patients with invasive listeriosis: A retrospective analysis.. Sutter, J. P., Kocheise, L., Kempski, J., Christner, M., Wichmann, D., Pinnschmidt, H., Schmiedel, S., Lohse, A. W., Huber, S., & Brehm, T. T. (2024).. (Infection, 52(4), 1601.)
8. Antimicrobial Resistance in Listeria Species.. Luque-Sastre L.Arroyo C.Fox EM.McMahon BJ.Bai L.Li F.Fanning S.2018.. (Microbiol Spectr6:10.1128/microbiolspec.arba-0031-2017.)
9. Investigation of Antimicrobial Resistance Genes in Listeria monocytogenes from 2010 through to 2021.. Hanes, R. M., & Huang, Z. (2022).. (International Journal of Environmental Research and Public Health, 19(9).)
10. Investigation of Antimicrobial Resistance Genes in Listeria monocytogenes from 2010 through to 2021.. Hanes, R. M., & Huang, Z. (2022).. (International Journal of Environmental Research and Public Health, 19(9).)
11. Phenotypic and genotypic antimicrobial resistance of Listeria monocytogenes: An observational study in France.. Moura, A., Leclercq, A., Vales, G., Tessaud-Rita, N., Bracq-Dieye, H., Thouvenot, P., Madec, Y., Charlier, C., & Lecuit, M. (2023).. (The Lancet Regional Health - Europe, 37, 100800.)
12. Listeriosis.. Disson, O., Charlier, C., Pérot, P., Leclercq, A., Paz, R. N., Kathariou, S., Tsai, Y. H., & Lecuit, M. (2025).. (Nature Reviews Disease Primers, 11(1), 71.)
13. Listeriosis.. Disson, O., Charlier, C., Pérot, P., Leclercq, A., Paz, R. N., Kathariou, S., Tsai, Y. H., & Lecuit, M. (2025).. (Nature Reviews Disease Primers, 11(1), 71.)
14. Avoiding death by autophagy: Interactions of Listeria monocytogenes with the macrophage autophagy system.. Birmingham, C. L., Higgins, D. E., & Brumell, J. H. (2008).. (Autophagy, 4(3), 368–371.)
15. Heavy Metal Resistance Determinants of the Foodborne Pathogen Listeria monocytogenes.. Parsons, C., Lee, S., & Kathariou, S. (2018).. (Genes, 10(1).)
16. Avoiding death by autophagy: Interactions of Listeria monocytogenes with the macrophage autophagy system.. Birmingham, C. L., Higgins, D. E., & Brumell, J. H. (2008).. (Autophagy, 4(3), 368–371.)
17. The Genetic Determinants of Listeria monocytogenes Resistance to Bacteriocins Produced by Lactic Acid Bacteria.. Zawiasa, A., & Olejnik-Schmidt, A. (2025).. (Genes, 16(1).)
18. Listeria Monocytogenes. [Updated 2023 Jul 4].. Rogalla D, Bomar PA.. (In: StatPearls [Internet]. Treasure Island (FL): StatPearls Publishing; 2025 Jan-.)
19. Significance and Characteristics of Listeria monocytogenes in Poultry Products.. Jamshidi, A., & Zeinali, T. (2019).. (International Journal of Food Science, 2019, 7835253.)
20. Listeria monocytogenes Flagella Are Used for Motility, Not as Adhesins, To Increase Host Cell Invasion.. Marquis, H. (2006).. (Infection and Immunity, 74(12), 6675.)
21. Listeria Monocytogenes. [Updated 2023 Jul 4].. Rogalla D, Bomar PA.. (In: StatPearls [Internet]. Treasure Island (FL): StatPearls Publishing; 2025 Jan-.)
22. Why does Listeria monocytogenes survive in food and food-production environments?. Osek, J., & Wieczorek, K. (2023).. (Journal of Veterinary Research, 67(4), 537.)
23. Genomic and pathogenicity islands of Listeria monocytogenes—Overview of selected aspects.. Wiktorczyk-Kapischke, N., Skowron, K., & Wałecka-Zacharska, E. (2023).. (Frontiers in Molecular Biosciences, 10, 1161486.)
24. Targeting and crossing of the human maternofetal barrier by Listeria monocytogenes: Role of internalin interaction with trophoblast E-cadherin.. Lecuit, M., Nelson, D. M., Smith, S. D., Khun, H., Huerre, M., Vacher-Lavenu, M. C., Gordon, J. I., & Cossart, P. (2004).. (Proceedings of the National Academy of Sciences of the United States of America, 101(16), 6152.)
25. Listeria monocytogenes Internalin and E-cadherin: From Bench to Bedside.. Bonazzi, M., Lecuit, M., & Cossart, P. (2009).. (Cold Spring Harbor Perspectives in Biology, 1(4), a003087.)
26. Role of internalin proteins in the pathogenesis of Listeria monocytogenes.. Ireton, K., Mortuza, R., Gyanwali, G. C., Gianfelice, A., & Hussain, M. (2021).. (Molecular Microbiology, 116(6), 1407-1419.)
27. The Listeria monocytogenes InlC protein interferes with innate immune responses by targeting the IκB kinase subunit IKKα.. Gouin, E., Adib-Conquy, M., Balestrino, D., Nahori, M. A., Villiers, V., Colland, F., Dramsi, S., Dussurget, O., & Cossart, P. (2010).. (Proceedings of the National Academy of Sciences of the United States of America, 107(40), 17333.)
28. The Pore-Forming Toxin Listeriolysin O Mediates a Novel Entry Pathway of L. monocytogenes into Human Hepatocytes.. Vadia S, Arnett E, Haghighat A-C, Wilson-Kubalek EM, Tweten RK, Seveau S (2011). (PLoS Pathog 7(11): e1002356.)
29. Listeria monocytogenes hijacks CD147 to ensure proper membrane protrusion formation and efficient bacterial dissemination.. Dhanda, A.S., Lulic, K.T., Yu, C. et al.. (Cell. Mol. Life Sci. 76, 4165–4178 (2019).)
30. The molecular mechanisms of listeriolysin O-induced lipid membrane damage.. Petrišič, N., Kozorog, M., Aden, S., Podobnik, M., & Anderluh, G. (2021).. (Biochimica et Biophysica Acta (BBA) - Biomembranes, 1863(7), 183604.)
31. Genomic and pathogenicity islands of Listeria monocytogenes—Overview of selected aspects.. Wiktorczyk-Kapischke, N., Skowron, K., & Wałecka-Zacharska, E. (2023).. (Frontiers in Molecular Biosciences, 10, 1161486.)
32. Passive immunization with anti-ActA and anti-listeriolysin O antibodies protects against Listeria monocytogenes infection in mice.. Asano, K., Sashinami, H., Osanai, A., Hirose, S., Ono, H. K., Narita, K., Hu, D. L., & Nakane, A. (2016).. (Scientific Reports, 6(1), 39628.)
33. Passive immunization with anti-ActA and anti-listeriolysin O antibodies protects against Listeria monocytogenes infection in mice.. Asano, K., Sashinami, H., Osanai, A., Hirose, S., Ono, H. K., Narita, K., Hu, D. L., & Nakane, A. (2016).. (Scientific Reports, 6(1), 39628.)
34. Passive immunization with anti-ActA and anti-listeriolysin O antibodies protects against Listeria monocytogenes infection in mice.. Asano, K., Sashinami, H., Osanai, A., Hirose, S., Ono, H. K., Narita, K., Hu, D. L., & Nakane, A. (2016).. (Scientific Reports, 6(1), 39628.)
35. How Listeria monocytogenes organizes its surface for virulence.. Carvalho, F., Sousa, S., & Cabanes, D. (2014).. (Frontiers in Cellular and Infection Microbiology, 4, 48.)
36. Listeriolysin S: A bacteriocin from epidemic Listeria monocytogenes strains that targets the gut microbiota.. Quereda, J. J., Meza-Torres, J., Cossart, P., & Pizarro-Cerdá, J. (2017).. (Gut Microbes, 8(4), 384.)
37. Genomic and pathogenicity islands of Listeria monocytogenes—Overview of selected aspects.. Wiktorczyk-Kapischke, N., Skowron, K., & Wałecka-Zacharska, E. (2023).. (Frontiers in Molecular Biosciences, 10, 1161486.)
38. The impact of iron on Listeria monocytogenes; inside and outside the host.. McLaughlin, H. P., Hill, C., & Gahan, C. G. (2011).. (Current Opinion in Biotechnology, 22(2), 194-199.)
39. An update on the transport and metabolism of iron in Listeria monocytogenes: The role of proteins involved in pathogenicity.. Lechowicz, J., & Krawczyk-Balska, A. (2015).. (Biometals, 28(4), 587.)
40. An update on the transport and metabolism of iron in Listeria monocytogenes: The role of proteins involved in pathogenicity.. Lechowicz, J., & Krawczyk-Balska, A. (2015).. (Biometals, 28(4), 587.)
41. Shared and distinct mechanisms of iron acquisition by bacterial and fungal pathogens of humans.. Caza, M., & Kronstad, J. W. (2013).. (Frontiers in Cellular and Infection Microbiology, 3, 80.)
42. Metal ion homeostasis in Listeria monocytogenes and importance in host-pathogen interactions.. Jesse HE, Roberts IS, Cavet JS.. (Adv Microb Physiol. 2014;65:83-123)
43. Two Zinc Uptake Systems Contribute to the Full Virulence of Listeria monocytogenes during Growth In Vitro and In Vivo.. Corbett, D., Wang, J., Schuler, S., Lopez-Castejon, G., Glenn, S., Brough, D., Andrew, P. W., Cavet, J. S., & Roberts, I. S. (2012).. (Infection and Immunity, 80(1), 14.)
44. Metal ion homeostasis in Listeria monocytogenes and importance in host-pathogen interactions.. Jesse HE, Roberts IS, Cavet JS.. (Adv Microb Physiol. 2014;65:83-123)
45. The combined actions of the copper-responsive repressor CsoR and copper-metallochaperone CopZ modulate CopA-mediated copper efflux in the intracellular pathogen Listeria monocytogenes.. Corbett, D., Schuler, S., Glenn, S., Andrew, P. W., Cavet, J. S., & Roberts, I. S. (2011).. (Molecular Microbiology, 81(2), 457-472.)
46. Heavy Metal Resistance Determinants of the Foodborne Pathogen Listeria monocytogenes.. Parsons, C., Lee, S., & Kathariou, S. (2018).. (Genes, 10(1).)
47. Heavy Metal Resistance Determinants of the Foodborne Pathogen Listeria monocytogenes.. Parsons, C., Lee, S., & Kathariou, S. (2018).. (Genes, 10(1).)
48. Heavy Metal Resistance Determinants of the Foodborne Pathogen Listeria monocytogenes.. Parsons, C., Lee, S., & Kathariou, S. (2018).. (Genes, 10(1).)
49. Genomic and pathogenicity islands of Listeria monocytogenes—Overview of selected aspects.. Wiktorczyk-Kapischke, N., Skowron, K., & Wałecka-Zacharska, E. (2023).. (Frontiers in Molecular Biosciences, 10, 1161486.)
50. Heavy Metal Resistance Determinants of the Foodborne Pathogen Listeria monocytogenes.. Parsons, C., Lee, S., & Kathariou, S. (2018).. (Genes, 10(1).)
51. Metal ion homeostasis in Listeria monocytogenes and importance in host-pathogen interactions.. Jesse HE, Roberts IS, Cavet JS.. (Adv Microb Physiol. 2014;65:83-123)
52. Listeriosis.. Disson, O., Charlier, C., Pérot, P., Leclercq, A., Paz, R. N., Kathariou, S., Tsai, Y. H., & Lecuit, M. (2025).. (Nature Reviews Disease Primers, 11(1), 71.)
53. Metal ion homeostasis in Listeria monocytogenes and importance in host-pathogen interactions.. Jesse HE, Roberts IS, Cavet JS.. (Adv Microb Physiol. 2014;65:83-123)
54. Passive immunization with anti-ActA and anti-listeriolysin O antibodies protects against Listeria monocytogenes infection in mice.. Asano, K., Sashinami, H., Osanai, A., Hirose, S., Ono, H. K., Narita, K., Hu, D. L., & Nakane, A. (2016).. (Scientific Reports, 6(1), 39628.)
55. Passive immunization with anti-ActA and anti-listeriolysin O antibodies protects against Listeria monocytogenes infection in mice.. Asano, K., Sashinami, H., Osanai, A., Hirose, S., Ono, H. K., Narita, K., Hu, D. L., & Nakane, A. (2016).. (Scientific Reports, 6(1), 39628.)
56. Listeria Monocytogenes. [Updated 2023 Jul 4].. Rogalla D, Bomar PA.. (In: StatPearls [Internet]. Treasure Island (FL): StatPearls Publishing; 2025 Jan-.)
57. A case report of oral sulfamethoxazole in the treatment of posttransplant Listeria monocytogenes meningitis.. Ma, Y., Hu, W., & Song, W. (2023).. (Translational Andrology and Urology, 12(3), 524.)
58. Listeria Monocytogenes. [Updated 2023 Jul 4].. Rogalla D, Bomar PA.. (In: StatPearls [Internet]. Treasure Island (FL): StatPearls Publishing; 2025 Jan-.)
59. Listeria Monocytogenes. [Updated 2023 Jul 4].. Rogalla D, Bomar PA.. (In: StatPearls [Internet]. Treasure Island (FL): StatPearls Publishing; 2025 Jan-.)
60. A Bacteriophage Cocktail Significantly Reduces Listeria monocytogenes without Deleterious Impact on the Commensal Gut Microbiota under Simulated Gastrointestinal Conditions.. Jakobsen, R. R., Trinh, J. T., Bomholtz, L., Brok-Lauridsen, S. K., Sulakvelidze, A., & Nielsen, D. S. (2022).. (Viruses, 14(2), 190.)
61. Passive immunization with anti-ActA and anti-listeriolysin O antibodies protects against Listeria monocytogenes infection in mice.. Asano, K., Sashinami, H., Osanai, A., Hirose, S., Ono, H. K., Narita, K., Hu, D. L., & Nakane, A. (2016).. (Scientific Reports, 6(1), 39628.)
62. Listeria Monocytogenes. [Updated 2023 Jul 4].. Rogalla D, Bomar PA.. (In: StatPearls [Internet]. Treasure Island (FL): StatPearls Publishing; 2025 Jan-.)
63. Listeriosis.. Disson, O., Charlier, C., Pérot, P., Leclercq, A., Paz, R. N., Kathariou, S., Tsai, Y. H., & Lecuit, M. (2025).. (Nature Reviews Disease Primers, 11(1), 71.)
64. Listeria Monocytogenes. [Updated 2023 Jul 4].. Rogalla D, Bomar PA.. (In: StatPearls [Internet]. Treasure Island (FL): StatPearls Publishing; 2025 Jan-.)
65. Listeria Monocytogenes. [Updated 2023 Jul 4].. Rogalla D, Bomar PA.. (In: StatPearls [Internet]. Treasure Island (FL): StatPearls Publishing; 2025 Jan-.)
66. A case report of oral sulfamethoxazole in the treatment of posttransplant Listeria monocytogenes meningitis.. Ma, Y., Hu, W., & Song, W. (2023).. (Translational Andrology and Urology, 12(3), 524.)
67. Investigation of Antimicrobial Resistance Genes in Listeria monocytogenes from 2010 through to 2021.. Hanes, R. M., & Huang, Z. (2022).. (International Journal of Environmental Research and Public Health, 19(9).)
68. Bacteriophage P100 for control of Listeria monocytogenes in foods: Genome sequence, bioinformatic analyses, oral toxicity study, and application.. Carlton, R., Noordman, W., Biswas, B., De Meester, E., & Loessner, M. (2005).. (Regulatory Toxicology and Pharmacology, 43(3), 301-312.)
69. A Bacteriophage Cocktail Significantly Reduces Listeria monocytogenes without Deleterious Impact on the Commensal Gut Microbiota under Simulated Gastrointestinal Conditions.. Jakobsen, R. R., Trinh, J. T., Bomholtz, L., Brok-Lauridsen, S. K., Sulakvelidze, A., & Nielsen, D. S. (2022).. (Viruses, 14(2), 190.)
70. Passive immunization with anti-ActA and anti-listeriolysin O antibodies protects against Listeria monocytogenes infection in mice.. Asano, K., Sashinami, H., Osanai, A., Hirose, S., Ono, H. K., Narita, K., Hu, D. L., & Nakane, A. (2016).. (Scientific Reports, 6(1), 39628.)
71. Passive immunization with anti-ActA and anti-listeriolysin O antibodies protects against Listeria monocytogenes infection in mice.. Asano, K., Sashinami, H., Osanai, A., Hirose, S., Ono, H. K., Narita, K., Hu, D. L., & Nakane, A. (2016).. (Scientific Reports, 6(1), 39628.)
72. Passive immunization with anti-ActA and anti-listeriolysin O antibodies protects against Listeria monocytogenes infection in mice.. Asano, K., Sashinami, H., Osanai, A., Hirose, S., Ono, H. K., Narita, K., Hu, D. L., & Nakane, A. (2016).. (Scientific Reports, 6(1), 39628.)
73. Immunopeptidomics-based design of mRNA vaccine formulations against Listeria monocytogenes.. Mayer, R. L., Verbeke, R., Asselman, C., Aernout, I., Gul, A., Eggermont, D., Boucher, K., Thery, F., Maia, T. M., Demol, H., Gabriels, R., Martens, L., Bécavin, C., De Smedt, S. C., Vandekerckhove, B., Lentacker, I., & Impens, F. (2022).. (Nature Communications, 13(1), 6075.)