Entamoeba histolytica Specific Neutra™ Antibody Products

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Are you challenged by low diagnostic sensitivity, ineffective therapeutic targeting, or limited tools for studying Entamoeba histolytica pathogenesis? Creative Biolabs' E. histolytica specific Neutra™ antibody products leverage advanced phage display libraries and high-throughput epitope mapping to deliver antibodies with unmatched specificity, enabling precise detection, functional neutralization, and mechanistic exploration of E. histolytica virulence factors.

Introduction to Entamoeba histolytica

Entamoeba histolytica, a protozoan parasite, is the causative agent of amoebiasis, a global health burden linked to 50 million infections annually. Its pathogenesis hinges on stage-specific molecular adaptations and host-pathogen interactions.

Mechanisms of colonization and invasion by E. histolytica trophozoites and host immune responses to suppress and control amebic infection. (OA Literature) Fig.1 Immune response during amebic infection.1

  • Basic Information

E. histolytica exists in two forms: the invasive trophozoite and the environmentally resistant cyst. Transmission occurs via ingestion of cysts through contaminated food or water. Post-excystation, trophozoites colonize the colon, leveraging virulence factors like galactose/N-acetylgalactosamine (Gal/GalNAc)-specific lectin to adhere to and lyse host cells.

  • Structure

The trophozoite membrane is enriched with surface proteins critical for invasion, including the Gal/GalNAc lectin heterodimer (170 kDa heavy chain, 35 kDa light chain), cysteine proteases, and amoebapores. The lectin mediates host cell adherence via carbohydrate recognition, while cysteine proteases degrade extracellular matrix components. Cryo-EM studies reveal lectin's trimeric arrangement, which facilitates clustering at the parasite-host interface to stabilize adhesion.

  • Related Signaling Pathways

E. histolytica disrupts host immune defenses by modulating NF-κB and MAPK pathways. The Gal/GalNAc lectin activates host apoptotic cascades via caspase-3, while parasite-secreted prostaglandin E2 suppresses IL-8 production in epithelial cells, impairing neutrophil recruitment. Additionally, trophozoites induce Ca²⁺-dependent cytoskeletal remodeling in host cells, promoting phagocytosis of cellular debris.

  • Related Diseases

Amoebiasis manifests as asymptomatic colonization, dysentery, or extraintestinal complications like liver abscesses. Invasive trophozoites breach the intestinal mucosa, causing ulceration, hemorrhagic diarrhea, and systemic dissemination. Untreated hepatic amoebiasis carries a mortality rate exceeding 10%, particularly in resource-limited settings.

Applications of Anti-E. histolytica Neutralizing Antibodies

  • Diagnostic Development

Anti-lectin mAbs underpin ELISA and lateral flow assays for detecting fecal Gal/GalNAc antigens, achieving >95% sensitivity in differentiating E. histolytica from non-pathogenic strains.

  • Therapeutic Discovery

Neutralizing mAbs reduce hepatic abscess formation in murine models by 70–80% when administered prophylactically. Bispecific formats combining anti-lectin and anti-amoebapore antibodies show synergistic activity in clearing disseminated infections.

  • Vaccine Efficacy Monitoring

Quantify neutralizing antibody titers in serum from vaccine trials using lectin-coated SPR biosensors. High-titer responses correlate with protection against experimental challenge in primates.

  • Host-Pathogen Interaction Studies

Visualize trophozoite invasion in real-time using fluorophore-conjugated antibodies. Anti-lectin Fab fragments labeled with fluorescent dye enable tracking of parasite motility and membrane dynamics during colonic penetration.

Our Anti-E. histolytica Antibodies

Neutralizing antibodies targeting Gal/GalNAc lectin or cysteine proteases are pivotal for blocking invasion. Monoclonal antibodies (mAbs) against the lectin's intermediate subunit (e.g., monoclonal IgG1 clones) inhibit trophozoite adherence by >90% in vitro, while anti-protease antibodies reduce colonic tissue damage by neutralizing enzymatic activity. E. histolytica specific antibodies are validated for:

- Surface staining: Quantify lectin expression across parasite life stages.

- Functional neutralization: Block host cell adhesion and cytolysis in invasion assays.

- Immunoprecipitation: Isolate lectin complexes for structural studies.

Creative Biolabs' E. histolytica specific Neutra™ antibody products equip researchers with rigorously validated tools to dissect amoebiasis mechanisms and accelerate therapeutic innovation. Our antibodies are engineered for reproducibility across WB, ELISA, flow cytometry, and functional neutralization assays. Contact our team today to discuss custom development for your E. histolytica research program.

REFERENCE

  1. Nakada-Tsukui, Kumiko, and Tomoyoshi Nozaki. "Immune response of amebiasis and immune evasion by Entamoeba histolytica." Frontiers in immunology 7 (2016): 175. Distributed under Open Access license CC BY 4.0, without modification. https://doi.org/10.3389/fimmu.2016.00175
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Recombinant Anti-E. histolytica Antibody (V3S-1022-YC1659) (CAT#: V3S-1022-YC1659)

Target: E. histolytica

Host Species: Human

Target Species: Entamoeba histolytica,

Application: IF,WB,FC,

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Recombinant Mouse Anti-E. histolytica Antibody (V3S-1022-YC5380) (CAT#: V3S-1022-YC5380)

Target: E. histolytica

Host Species: Mouse

Target Species: Entamoeba histolytica,

Application: IA,

For research use only, not directly for clinical use.


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