Recombinant Actinobacillus pleuropneumoniae serotype 5b ATP synthase subunit c (atpE)
Description
Introduction to Recombinant ATP Synthase Subunit c (atpE)
The recombinant ATP synthase subunit c (atpE) from Actinobacillus pleuropneumoniae serotype 5b is a genetically engineered protein derived from a critical component of the bacterial ATP synthase complex. ATP synthase is a membrane-bound enzyme responsible for converting proton gradients into ATP, essential for energy production in bacteria. Subunit c (atpE) is a core component of the F₀ sector, forming a proton channel that drives rotational energy coupling. This protein is expressed in heterologous systems (e.g., E. coli) for structural, functional, and vaccine-related studies .
Functional Role in ATP Synthase
Subunit c is integral to the F₀ sector, which translocates protons across the membrane, generating torque for ATP synthesis. In A. pleuropneumoniae, this process is vital for survival, particularly under energy-stress conditions. Mutations in ATP synthase genes or related energy metabolism pathways (e.g., dsbA, hemA) have been linked to attenuated virulence in swine models .
Production and Purification
The recombinant atpE is produced via bacterial expression systems with His-tagging for affinity chromatography. Purity is confirmed via SDS-PAGE, and the protein is stabilized with trehalose or glycerol for long-term storage .
Role in Pathogenesis and Vaccine Development
While not directly a virulence factor, ATP synthase subunits like atpE are critical for bacterial metabolism. Research on A. pleuropneumoniae has identified energy-related genes (e.g., tonB, hemA) as essential for survival in pigs . Though atpE itself is not a primary vaccine target, ATP synthase components are studied for their potential in subunit vaccine formulations, particularly when combined with other antigens like outer membrane proteins (OMPs) or Apx toxins .
Comparative Analysis of ATP Synthase Subunits
| Subunit | Role | F₀/F₁ Sector | Host Expression | Purity |
|---|---|---|---|---|
| atpE | Proton channel formation | F₀ | E. coli | >90% |
| atpB | Subunit a (proton translocation) | F₀ | E. coli | >90% |
| atpA | Subunit alpha (ATP binding) | F₁ | E. coli/yeast | >85% |
| atpD | Subunit beta (catalytic core) | F₁ | E. coli | >85% |
Data synthesized from product listings and gene annotations ( ).
Applications in Biomedical Research
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Structural Biology: Recombinant atpE facilitates crystallography or cryo-EM studies to resolve F₀ sector dynamics.
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Vaccine Development: Though not a direct target, ATP synthase subunits may enhance vaccine formulations by modulating immune responses to surface antigens .
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Diagnostic Tools: His-tagged atpE could serve as a reference antigen in serotyping assays for A. pleuropneumoniae .
Challenges and Limitations
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Low Direct Virulence Association: Unlike Apx toxins or OMPs, atpE is not a primary virulence factor, limiting its utility in therapeutic targeting.
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Expression Challenges: Small subunit size (84aa) may complicate folding or stability in heterologous systems.
Product Specs
Note: While we prioritize shipping the format currently in stock, we are happy to accommodate any specific format requirements. Please indicate your preference in the order notes section and we will do our best to fulfill your request.
Note: All our proteins are shipped with standard blue ice packs. If you require dry ice shipping, please inform us in advance as additional fees will apply.
Generally, liquid forms have a shelf life of 6 months at -20°C/-80°C. Lyophilized forms exhibit a shelf life of 12 months at -20°C/-80°C.
Target Background
KEGG: apl:APL_1651
STRING: 416269.APL_1651
