Fusobacterium nucleatum

Overview

Fusobacterium nucleatum (Fn) is a Gram-negative, obligate anaerobic, non-spore-forming, non-motile, fusiform (spindle-shaped) rod that is abundant in human oral biofilms and functions ecologically as a “bridge” organism that coaggregates with early and late colonizers, promoting mature multispecies plaque architecture and dysbiosis.^[1] Under conditions of impaired host barriers or microbial imbalance, F. nucleatum can behave as a pathobiont that translocates beyond the mouth to extra-oral niches (including the gastrointestinal tract and placenta) and is implicated in periodontal disease, adverse pregnancy outcomes, inflammatory bowel disease (IBD), and multiple cancers, most notably colorectal cancer (CRC).^[2] Mechanistically, F. nucleatum is unusually “transboundary”: it adheres tightly to epithelial and immune cells, thrives in polymicrobial consortia and biofilms, and deploys adhesins and immunomodulatory factors that promote inflammation, barrier disruption, immune evasion, and pro-tumor signaling.^[3][4][5] A major translational theme is that F. nucleatum is not merely a passive biomarker; experimental models show that reducing F. nucleatum burden can attenuate tumor growth and inflammatory phenotypes, motivating therapeutic strategies that target F. nucleatum itself (antimicrobials, phage, vaccines, anti-adhesin approaches, microbiome interventions) or its host-pathway consequences (e.g., immunosuppression and chemoresistance).^[6]

Antibiotic resistance

F. nucleatum is generally susceptible to several anti-anaerobic agents used clinically (e.g., nitroimidazoles), but resistance is clinically important and mechanistically diverse. A classic and well-documented phenotype is β-lactam resistance driven by β-lactamase production, with isolates showing high penicillin MICs while retaining susceptibility to β-lactam/β-lactamase inhibitor combinations (e.g., amoxicillin-clavulanate), metronidazole, and other agents in vitro.^[7][8] Beyond canonical AMR genes, recent functional genetics demonstrates that core metabolic pathways can modulate antibiotic sensitivity and virulence: disruption of hydrogen sulfide (H₂S) biosynthesis enzymes (e.g., MegL and related cysteine metabolism enzymes) reduces fitness and virulence and alters antibiotic susceptibility, indicating that “metabolic AMR” and stress physiology can influence treatment outcomes even when classic resistance genes are absent.^[9][10] In CRC-associated contexts, F. nucleatum can also indirectly undermine therapy effectiveness by promoting chemoresistance through host-pathway rewiring (TLR4/MYD88-linked microRNA suppression and autophagy activation), so “antibiotic resistance” in practice may include both microbial drug resistance and F. nucleatum-mediated tolerance/therapy failure at the disease-system level.^[11]

Pathogenicity

F. nucleatum pathogenicity is best understood as a multi-stage process integrating colonization, polymicrobial synergy, host barrier disruption, immune modulation, and tumor-promoting biology. In oral disease, F. nucleatum’s high coaggregation capacity helps scaffold dysbiotic biofilms and amplify inflammatory damage; its outer membrane components and secreted/vesicle-associated factors stimulate innate receptors and cytokine cascades, while physical proximity in biofilms enables metabolic cross-feeding and cooperative virulence.^[12][13] In the gut, Fn can adhere to and invade epithelial cells and disrupt barrier integrity via adhesin-driven interactions and inflammatory signaling; a defining CRC mechanism is FadA binding to epithelial E-cadherin, activating β-catenin/Wnt signaling and inducing oncogenic and inflammatory gene programs that support tumor growth.^[14][15] Fn also selectively enriches in tumors through Fap2 binding to tumor-associated glycans (Gal-GalNAc), and can suppress anti-tumor immunity by engaging inhibitory receptors on NK/T cells (e.g., TIGIT), shifting the tumor microenvironment toward immune evasion.^[16] Additionally, Fn can promote disease persistence and poor outcomes by driving therapy resistance pathways—metronidazole can reduce Fn load and tumor growth in xenografts, yet Fn can also enhance chemoresistance via autophagy-linked circuitry, illustrating why Fn is increasingly treated as a causal modifier of disease rather than a bystander.^[17][18]

Morphology

Fn cells are classically described as long, slender, spindle-shaped (fusiform) Gram-negative rods with tapered ends, typically ~5–10 µm in length, and are obligate anaerobes that do not form spores and are non-motile.^[19] This morphology is functionally relevant: the fusiform shape and surface architecture support intimate contact with host cells and neighboring bacteria in biofilms, while the Gram-negative outer membrane contributes potent immunostimulatory potential via LPS/LOS and provides a platform for outer membrane proteins and autotransporter-like adhesins implicated in tissue tropism and immune interactions.^[20] At the population level, Fn is genetically heterogeneous, historically described as multiple subspecies with differences in genome content and disease associations; more recent genome-based taxonomic revisions have elevated some former subspecies and emphasized that strain/subtype variation can strongly influence virulence factor repertoires, tissue distribution, and clinical outcomes, so morphology is conserved, but pathogenic potential is not.^[21]

Virulence Factors

Fusobacterium nucleatum (Fn) virulence is dominated by surface-exposed adhesins and outer membrane proteins that mediate (i) coaggregation and biofilm maturation, (ii) epithelial adhesion/invasion and barrier disruption, (iii) immune activation and immune evasion, and (iv) delivery of inflammatory/pro-tumor cargo via outer membrane vesicles (OMVs). Many factors are multifunctional, with distinct roles depending on niche (oral vs gut vs tumor microenvironment) and strain background.^[22][23]

Virulence factor	Description and role in pathogenicity
FadA (Fusobacterium adhesin A)	Major adhesin/invasin that binds E-cadherin on epithelial cells, enabling adhesion/invasion and activating β-catenin/Wnt signaling with downstream oncogenic and inflammatory transcriptional programs in CRC models.[24][25]
Fap2 (autotransporter-like outer membrane protein)	Mediates tumor enrichment by binding Gal-GalNAc overexpressed on CRC cells and can promote immune evasion by engaging inhibitory receptors (including TIGIT) on NK/T cells, dampening anti-tumor activity.[26][27]
RadD (adhesin/OMP)	Contributes to bacterial–bacterial coaggregation in oral biofilms and has emerging evidence for roles in tumor colonization and pathogenic synergy; recent focused reviews highlight RadD as a key “connector” adhesin within F. nucleatum biology.[28]
FomA (major outer membrane porin/OMP)	A prominent OMP implicated in adhesion and host interaction; commonly discussed as an antigenic surface component relevant to host responses and potential vaccine/diagnostic targeting in oral/extraoral disease contexts.[29]
Outer membrane vesicles (OMVs/EVs)	Fn releases vesicles that can traverse mucus and deliver immunostimulatory cargo (proteins, nucleic acids), activating inflammasome pathways and amplifying mucosal inflammation; implicated in IBD/UC progression and immune dysregulation.[30]
Fn-Dps (Dps-like multifunctional factor)	Identified as a virulence factor that supports intracellular survival and promotes CRC cell migration/metastasis programs in vivo, linking bacterial stress biology/iron handling to pathogenic outcomes.[31]
LPS/LOS (outer membrane endotoxin)	Drives innate immune activation (TLR pathways), cytokine induction, and inflammatory tissue injury; contributes to macrophage polarization and tumor-microenvironment remodeling described in gut/CRC-focused reviews.[32]
H₂S biosynthesis enzymes	Cysteine metabolism enzymes generate H₂S; genetic disruption reduces fitness/virulence and changes antibiotic sensitivity, tying volatile sulfur metabolism to pathogenic potential and treatment response.[33]
TLR4/MYD88-linked pro-survival signaling induction	Fn can activate host innate signaling that reshapes microRNA expression and autophagy, promoting CRC chemoresistance and survival under therapy, functioning as a “virulence program” at the host-pathway level rather than a single molecule.[34]
Immune cell killing/impairment via OMPs (Fap2/RadD)	Fap2 and RadD were reported to induce human lymphocyte cell death and are homologous to autotransporter secretion regions, highlighting direct immunopathogenic mechanisms beyond simple adhesion.[35]

Metallomics

Fusobacterium nucleatum (Fn) metallomics is driven by life as an anaerobe in host-associated niches: it must acquire iron (often via heme), manage metal toxicity, and maintain redox balance under intermittent oxidative stress. Evidence is strongest for iron/heme acquisition and iron-linked stress proteins, with additional support for metal-dependent oxidative stress responses and metal-tuned metabolic/virulence phenotypes.^[36][37]

Metal / ion	Key features in F. nucleatum
Iron (Fe)	Central nutrient and stressor: Fn expresses a dedicated heme uptake/utilization locus (hmu) and enzymes that release Fe²⁺ from heme under anaerobic conditions, supporting growth in iron-restricted host environments.[38]
Heme (Fe-protoporphyrin IX; iron source complex)	Fn uses anaerobic heme catabolism machinery (including HmuW and associated proteins) to access iron without oxygen, consistent with adaptation to anaerobic mucosal/tumor niches.[39]
Iron storage/iron handling (Dps-linked)	Fn-Dps links stress protection and virulence; Dps-family proteins typically bind/sequester iron to reduce oxidative damage, and Fn-Dps is experimentally tied to intracellular survival and CRC progression phenotypes.[40]
Host micronutrient limitation as selective pressure (nutritional immunity)	Reviews emphasize Fn’s adaptation to fluctuating host conditions and mucosal environments where metal sequestration by the host is a key defense, making metal acquisition/handling systems plausible determinants of strain fitness and virulence.[41][42]

Vulnerabilities

F. nucleatum vulnerabilities cluster into (i) physiological constraints (strict anaerobiosis; redox stress sensitivity), (ii) dependence on specific colonization factors (adhesins; glycan binding), (iii) dependence on nutrient acquisition systems (heme/iron), and (iv) reliance on polymicrobial biofilms (disrupting community structure can destabilize Fn). These vulnerabilities can be exploited by antimicrobials, anti-adhesin strategies, immune-directed approaches, and microbiome interventions.^[43]

Vulnerability of F. nucleatum	Potential therapeutic / preventive opportunity
Dependence on Fap2–Gal-GalNAc tumor binding	Block Gal-GalNAc interactions (glycan-targeted decoys, antibodies, or competitive ligands) or target Fap2 directly to reduce tumor colonization/enrichment.[44][45]
FadA–E-cadherin binding is central to invasion/pro-tumor signaling	Anti-FadA vaccines/antibodies or small molecules/biologics that disrupt FadA–E-cadherin engagement could reduce invasion and downstream β-catenin/Wnt activation.[46]
Reliance on heme/iron acquisition (hmu locus)	Inhibit heme uptake/catabolism components (e.g., HmuW-linked pathway) or starve Fn via iron limitation strategies that selectively impact anaerobic heme-dependent growth in niches.[47]
H₂S biosynthesis supports fitness/virulence and alters antibiotic sensitivity	Target MegL/CysK-pathway enzymes to weaken Fn and potentially resensitize to antibiotics; validated genetically as affecting virulence and susceptibility.[48]
Strict anaerobe with limited oxidative stress defenses	Local redox modulation (oxygenation, ROS-generating antiseptics in oral settings) plus biofilm disruption can create hostile conditions that reduce viability and biofilm persistence.[49]
Susceptibility to nitroimidazoles in vivo tumor models	In CRC xenografts, metronidazole reduced Fn load and tumor growth, supports targeted antimicrobial trials where Fn is demonstrably abundant.[50]
Biofilm “bridge” role creates dependence on coaggregation networks	Disrupt coaggregation (e.g., anti-adhesin targeting of RadD and related OMPs) or destabilize partner species to collapse community structure supporting Fn expansion.[51][52]
Immune evasion via TIGIT engagement (Fap2)	Therapeutically, disrupting Fap2–TIGIT interaction or combining Fn-targeted reduction with immunotherapies may restore NK/T function in Fn-high tumors.[53][54]

Interventions

Fusobacterium nucleatum intervention strategies span direct eradication/suppression, anti-colonization measures, and ecological approaches (probiotics, biofilm disruption, microbiome remodeling). Mechanistic selection should be driven by site (oral cavity vs gut/tumor), Fn load (biomarker-guided), and desired outcome including reduce inflammation, prevent invasion, reverse chemoresistance, or improve immunotherapy response.^[55][56][57]

Intervention	Mechanism
Metronidazole (context-specific, Fn-high CRC models)	Reduced Fn burden and tumor growth in CRC xenografts, supporting antimicrobial depletion as an adjunct strategy where Fn is implicated causally.[58]
Anti-FadA strategies (vaccine/antibody; anti-adhesion)	Neutralize FadA to block epithelial adherence/invasion and reduce β-catenin/Wnt activation associated with CRC promotion.[59][60]
Anti-Fap2 strategies (vaccine/antibody; glycan binding blockade)	Block tumor targeting via Gal-GalNAc and mitigate immune suppression via TIGIT engagement; reduces enrichment and may improve immune surveillance.[61][62]
Targeting H₂S biosynthesis	Genetically validated pathway influencing fitness, virulence, and antibiotic sensitivity, pharmacologic inhibition is a rational antivirulence approach.[63]
Microbiome/probiotic approaches (selected Lactobacillus spp.)	Multiple studies and reviews discuss probiotic strains that inhibit Fn growth or dampen Fn-associated inflammation, aiming to shift community ecology away from Fn-supported dysbiosis.[64]
OMV/EV-focused mitigation	If vesicle-mediated inflammasome activation drives inflammation (e.g., UC contexts), strategies that reduce vesiculation, neutralize vesicle cargo, or block downstream inflammasome activation may reduce pathology.[65]
Combination with cancer therapy optimization (autophagy/innate signaling context)	Fn can promote chemoresistance via TLR4/MYD88-linked microRNA suppression and autophagy activation; combining Fn reduction with autophagy-targeting or pathway-targeting approaches is mechanistically justified.[66]

Research Feed

References

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2. Fusobacterium nucleatum: ecology, pathogenesis and clinical implications.. Jiang, SS., Chen, YX. & Fang, JY.. (Nat Rev Microbiol 24, 197–214 (2026).)
3. Fusobacterium nucleatum: a transboundary pathogen in host-microbiota networks.. Gao, X., Cao, F., Li, Y. et al.. (Gut Pathog 17, 92 (2025).)
4. Fap2 Mediates Fusobacterium nucleatum Colorectal Adenocarcinoma Enrichment by Binding to Tumor-Expressed Gal-GalNAc.. Abed, J., Emgård, J. E., Zamir, G., Faroja, M., Almogy, G., Grenov, A., Sol, A., Naor, R., Pikarsky, E., Atlan, K. A., Mellul, A., Chaushu, S., Manson, A. L., Earl, A. M., Ou, N., Brennan, C. A., Garrett, W. S., & Bachrach, G. (2016).. (Cell Host & Microbe, 20(2), 215-225.)
5. Fusobacterium nucleatum Promotes Colorectal Carcinogenesis by Modulating E-Cadherin/β-Catenin Signaling via its FadA Adhesin.. Rubinstein, M. R., Wang, X., Liu, W., Hao, Y., Cai, G., & Han, Y. W. (2013).. (Cell Host & Microbe, 14(2), 195-206.)
6. Adhesin RadD: the secret weapon of Fusobacterium nucleatum.. Jia, D., & Chen, S. (2024).. (Gut Microbes, 16(1).)
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11. Fusobacterium nucleatum promotes chemoresistance to colorectal cancer by modulating autophagy.. Yu, T., Guo, F., Yu, Y., Sun, T., Ma, D., Han, J., Qian, Y., Kryczek, I., Sun, D., Nagarsheth, N., Chen, Y., Chen, H., Hong, J., Zou, W., & Fang, J.-Y. (2017).. (Cell, 170(3), 548–563.)
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13. Fusobacterium nucleatum-derived extracellular vesicles carrying virulence factor DNA trigger AIM2 inflammasome activation to facilitate UC progression.. Zhao, Y., Wu, R., Duan, Y. et al.. (Cell Mol Biol Lett 30, 138 (2025).)
14. Fusobacterium nucleatum Promotes Colorectal Carcinogenesis by Modulating E-Cadherin/β-Catenin Signaling via its FadA Adhesin.. Rubinstein, M. R., Wang, X., Liu, W., Hao, Y., Cai, G., & Han, Y. W. (2013).. (Cell Host & Microbe, 14(2), 195-206.)
15. FadA antigen of Fusobacterium nucleatum: implications for ceRNA network in colorectal cancer and adenomatous polyps progression.. Sama Rezasoltani, Elahe Shams, Moein Piroozkhah, Yaser Aidi, Mehdi Azizmohammad Looha, Parmida Bagheri, Roudabeh Behzadi Andouhjerdi, Amir Sadeghi, Leili Rejali, Ehsan Nazemalhosseini-Mojarad. (Discov Onc 16, 58 (2025).)
16. Fap2 Mediates Fusobacterium nucleatum Colorectal Adenocarcinoma Enrichment by Binding to Tumor-Expressed Gal-GalNAc.. Abed, J., Emgård, J. E., Zamir, G., Faroja, M., Almogy, G., Grenov, A., Sol, A., Naor, R., Pikarsky, E., Atlan, K. A., Mellul, A., Chaushu, S., Manson, A. L., Earl, A. M., Ou, N., Brennan, C. A., Garrett, W. S., & Bachrach, G. (2016).. (Cell Host & Microbe, 20(2), 215-225.)
17. Fusobacterium nucleatum promotes chemoresistance to colorectal cancer by modulating autophagy.. Yu, T., Guo, F., Yu, Y., Sun, T., Ma, D., Han, J., Qian, Y., Kryczek, I., Sun, D., Nagarsheth, N., Chen, Y., Chen, H., Hong, J., Zou, W., & Fang, J.-Y. (2017).. (Cell, 170(3), 548–563.)
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19. Identification of Fusobacterium nucleatum in primary and secondary endodontic infections and its association with clinical features by using two different methods.. Brenda P. F. A. Gomes, Juliana D. Bronzato, Rebecca F. Almeida-Gomes, Ericka T. Pinheiro, Ezilmara L. R. Sousa & Rogério C. Jacinto. (Clin Oral Invest 25, 6249–6258 (2021).)
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22. Fusobacterium nucleatum: a transboundary pathogen in host-microbiota networks.. Gao, X., Cao, F., Li, Y. et al.. (Gut Pathog 17, 92 (2025).)
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24. Fusobacterium nucleatum: a transboundary pathogen in host-microbiota networks.. Gao, X., Cao, F., Li, Y. et al.. (Gut Pathog 17, 92 (2025).)
25. Fusobacterium nucleatum Promotes Colorectal Carcinogenesis by Modulating E-Cadherin/β-Catenin Signaling via its FadA Adhesin.. Rubinstein, M. R., Wang, X., Liu, W., Hao, Y., Cai, G., & Han, Y. W. (2013).. (Cell Host & Microbe, 14(2), 195-206.)
26. Fusobacterium nucleatum: a transboundary pathogen in host-microbiota networks.. Gao, X., Cao, F., Li, Y. et al.. (Gut Pathog 17, 92 (2025).)
27. Fap2 Mediates Fusobacterium nucleatum Colorectal Adenocarcinoma Enrichment by Binding to Tumor-Expressed Gal-GalNAc.. Abed, J., Emgård, J. E., Zamir, G., Faroja, M., Almogy, G., Grenov, A., Sol, A., Naor, R., Pikarsky, E., Atlan, K. A., Mellul, A., Chaushu, S., Manson, A. L., Earl, A. M., Ou, N., Brennan, C. A., Garrett, W. S., & Bachrach, G. (2016).. (Cell Host & Microbe, 20(2), 215-225.)
28. Adhesin RadD: the secret weapon of Fusobacterium nucleatum.. Jia, D., & Chen, S. (2024).. (Gut Microbes, 16(1).)
29. Fusobacterium nucleatum: a transboundary pathogen in host-microbiota networks.. Gao, X., Cao, F., Li, Y. et al.. (Gut Pathog 17, 92 (2025).)
30. Fusobacterium nucleatum-derived extracellular vesicles carrying virulence factor DNA trigger AIM2 inflammasome activation to facilitate UC progression.. Zhao, Y., Wu, R., Duan, Y. et al.. (Cell Mol Biol Lett 30, 138 (2025).)
31. Fn-Dps, a novel virulence factor of Fusobacterium nucleatum, disrupts erythrocytes and promotes metastasis in colorectal cancer.. Yixian Wu, Songhe Guo, Fangfang Chen, Yiqiu Li, Yuying Huang, Wanli Liu, Ge Zhang (2023). (PLoS Pathog 19(1): e1011096.)
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33. Genetic Determinants of Hydrogen Sulfide Biosynthesis in Fusobacterium nucleatum Are Required for Bacterial Fitness, Antibiotic Sensitivity, and Virulence.. Chen Y, Camacho MI, Chen Y, Bhat AH, Chang C, Peluso EA, Wu C, Das A, Ton-That H,,2022.. (mBio13:e01936-22.)
34. Fusobacterium nucleatum promotes chemoresistance to colorectal cancer by modulating autophagy.. Yu, T., Guo, F., Yu, Y., Sun, T., Ma, D., Han, J., Qian, Y., Kryczek, I., Sun, D., Nagarsheth, N., Chen, Y., Chen, H., Hong, J., Zou, W., & Fang, J.-Y. (2017).. (Cell, 170(3), 548–563.)
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36. A new member of the flavodoxin superfamily from Fusobacterium nucleatum that functions in heme trafficking and reduction of anaerobilin. Alexandra K. McGregor, Anson C.K. Chan, Megan D. Schroeder, Long T.M. Do, Gurpreet Saini, Michael E.P. Murphy, Kirsten R. Wolthers. (Journal of Biological Chemistry, Volume 299, Issue 7, 104902)
37. Fn-Dps, a novel virulence factor of Fusobacterium nucleatum, disrupts erythrocytes and promotes metastasis in colorectal cancer.. Yixian Wu, Songhe Guo, Fangfang Chen, Yiqiu Li, Yuying Huang, Wanli Liu, Ge Zhang (2023). (PLoS Pathog 19(1): e1011096.)
38. A new member of the flavodoxin superfamily from Fusobacterium nucleatum that functions in heme trafficking and reduction of anaerobilin. Alexandra K. McGregor, Anson C.K. Chan, Megan D. Schroeder, Long T.M. Do, Gurpreet Saini, Michael E.P. Murphy, Kirsten R. Wolthers. (Journal of Biological Chemistry, Volume 299, Issue 7, 104902)
39. A new member of the flavodoxin superfamily from Fusobacterium nucleatum that functions in heme trafficking and reduction of anaerobilin. Alexandra K. McGregor, Anson C.K. Chan, Megan D. Schroeder, Long T.M. Do, Gurpreet Saini, Michael E.P. Murphy, Kirsten R. Wolthers. (Journal of Biological Chemistry, Volume 299, Issue 7, 104902)
40. Fn-Dps, a novel virulence factor of Fusobacterium nucleatum, disrupts erythrocytes and promotes metastasis in colorectal cancer.. Yixian Wu, Songhe Guo, Fangfang Chen, Yiqiu Li, Yuying Huang, Wanli Liu, Ge Zhang (2023). (PLoS Pathog 19(1): e1011096.)
41. Fusobacterium nucleatum: ecology, pathogenesis and clinical implications.. Jiang, SS., Chen, YX. & Fang, JY.. (Nat Rev Microbiol 24, 197–214 (2026).)
42. Fusobacterium nucleatum: a transboundary pathogen in host-microbiota networks.. Gao, X., Cao, F., Li, Y. et al.. (Gut Pathog 17, 92 (2025).)
43. Analysis of Fusobacterium persistence and antibiotic response in colorectal cancer.. Susan Bullman et al.. (Science358,1443-1448(2017))
44. Fap2 Mediates Fusobacterium nucleatum Colorectal Adenocarcinoma Enrichment by Binding to Tumor-Expressed Gal-GalNAc.. Abed, J., Emgård, J. E., Zamir, G., Faroja, M., Almogy, G., Grenov, A., Sol, A., Naor, R., Pikarsky, E., Atlan, K. A., Mellul, A., Chaushu, S., Manson, A. L., Earl, A. M., Ou, N., Brennan, C. A., Garrett, W. S., & Bachrach, G. (2016).. (Cell Host & Microbe, 20(2), 215-225.)
45. Adhesin RadD: the secret weapon of Fusobacterium nucleatum.. Jia, D., & Chen, S. (2024).. (Gut Microbes, 16(1).)
46. Fusobacterium nucleatum Promotes Colorectal Carcinogenesis by Modulating E-Cadherin/β-Catenin Signaling via its FadA Adhesin.. Rubinstein, M. R., Wang, X., Liu, W., Hao, Y., Cai, G., & Han, Y. W. (2013).. (Cell Host & Microbe, 14(2), 195-206.)
47. A new member of the flavodoxin superfamily from Fusobacterium nucleatum that functions in heme trafficking and reduction of anaerobilin. Alexandra K. McGregor, Anson C.K. Chan, Megan D. Schroeder, Long T.M. Do, Gurpreet Saini, Michael E.P. Murphy, Kirsten R. Wolthers. (Journal of Biological Chemistry, Volume 299, Issue 7, 104902)
48. Genetic Determinants of Hydrogen Sulfide Biosynthesis in Fusobacterium nucleatum Are Required for Bacterial Fitness, Antibiotic Sensitivity, and Virulence.. Chen Y, Camacho MI, Chen Y, Bhat AH, Chang C, Peluso EA, Wu C, Das A, Ton-That H,,2022.. (mBio13:e01936-22.)
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50. Analysis of Fusobacterium persistence and antibiotic response in colorectal cancer.. Susan Bullman et al.. (Science358,1443-1448(2017))
51. Analysis of Fusobacterium persistence and antibiotic response in colorectal cancer.. Susan Bullman et al.. (Science358,1443-1448(2017))
52. Adhesin RadD: the secret weapon of Fusobacterium nucleatum.. Jia, D., & Chen, S. (2024).. (Gut Microbes, 16(1).)
53. Fusobacterium-associated molecular and immunological alterations in colorectal cancer: Insights from a Norwegian cohort.. Citation: Omran TA, Subirats Camacho JL, Senthakumaran T, Gundersen G, Alte AK, Randen U, Tunsjø HS, Sæther PC and Bemanian V (2025). (Front. Immunol. 16:1601423.)
54. Adhesin RadD: the secret weapon of Fusobacterium nucleatum.. Jia, D., & Chen, S. (2024).. (Gut Microbes, 16(1).)
55. Fusobacterium nucleatum: ecology, pathogenesis and clinical implications.. Jiang, SS., Chen, YX. & Fang, JY.. (Nat Rev Microbiol 24, 197–214 (2026).)
56. Analysis of Fusobacterium persistence and antibiotic response in colorectal cancer.. Susan Bullman et al.. (Science358,1443-1448(2017))
57. Fusobacterium nucleatum promotes chemoresistance to colorectal cancer by modulating autophagy.. Yu, T., Guo, F., Yu, Y., Sun, T., Ma, D., Han, J., Qian, Y., Kryczek, I., Sun, D., Nagarsheth, N., Chen, Y., Chen, H., Hong, J., Zou, W., & Fang, J.-Y. (2017).. (Cell, 170(3), 548–563.)
58. Analysis of Fusobacterium persistence and antibiotic response in colorectal cancer.. Susan Bullman et al.. (Science358,1443-1448(2017))
59. Fusobacterium nucleatum Promotes Colorectal Carcinogenesis by Modulating E-Cadherin/β-Catenin Signaling via its FadA Adhesin.. Rubinstein, M. R., Wang, X., Liu, W., Hao, Y., Cai, G., & Han, Y. W. (2013).. (Cell Host & Microbe, 14(2), 195-206.)
60. FadA antigen of Fusobacterium nucleatum: implications for ceRNA network in colorectal cancer and adenomatous polyps progression.. Sama Rezasoltani, Elahe Shams, Moein Piroozkhah, Yaser Aidi, Mehdi Azizmohammad Looha, Parmida Bagheri, Roudabeh Behzadi Andouhjerdi, Amir Sadeghi, Leili Rejali, Ehsan Nazemalhosseini-Mojarad. (Discov Onc 16, 58 (2025).)
61. Fap2 Mediates Fusobacterium nucleatum Colorectal Adenocarcinoma Enrichment by Binding to Tumor-Expressed Gal-GalNAc.. Abed, J., Emgård, J. E., Zamir, G., Faroja, M., Almogy, G., Grenov, A., Sol, A., Naor, R., Pikarsky, E., Atlan, K. A., Mellul, A., Chaushu, S., Manson, A. L., Earl, A. M., Ou, N., Brennan, C. A., Garrett, W. S., & Bachrach, G. (2016).. (Cell Host & Microbe, 20(2), 215-225.)
62. Adhesin RadD: the secret weapon of Fusobacterium nucleatum.. Jia, D., & Chen, S. (2024).. (Gut Microbes, 16(1).)
63. Genetic Determinants of Hydrogen Sulfide Biosynthesis in Fusobacterium nucleatum Are Required for Bacterial Fitness, Antibiotic Sensitivity, and Virulence.. Chen Y, Camacho MI, Chen Y, Bhat AH, Chang C, Peluso EA, Wu C, Das A, Ton-That H,,2022.. (mBio13:e01936-22.)
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