ArticlePharmaceutical research2010
Rational design of multiple TB antigens TB10.4 and TB10.4-Ag85B as subunit vaccine candidates against Mycobacterium tuberculosis.
Article in Pharmaceutical research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Article
- In Silico Targeting and Immunological Profiling of PpiA inPathogens (Basel, Switzerland) · 2025Article
- Ensilication Improves the Thermal Stability of the Tuberculosis Antigen Ag85b and an Sbi-Ag85b Vaccine Conjugate.Scientific reports · 2019Article
- Recovery of recombinant Mycobacterium tuberculosis antigens fused with cell wall-anchoring motif (LysM) from inclusion bodies using non-denaturing reagent (N-laurylsarcosine).BMC biotechnology · 2019Article
- Recombinant O-mannosylated protein production (PstS-1) from Mycobacterium tuberculosis in Pichia pastoris (Komagataella phaffii) as a tool to study tuberculosis infection.Microbial cell factories · 2019Article
- Proof of concept in utilizing in-trans surface display system of Lactobacillus plantarum as mucosal tuberculosis vaccine via oral administration in mice.BMC biotechnology · 2018Article
- Nanoscale Peptide Self-assemblies Boost BCG-primed Cellular Immunity Against Mycobacterium tuberculosis.Scientific reports · 2018Article
- Optimizing Escherichia coli as a protein expression platform to produce Mycobacterium tuberculosis immunogenic proteins.Microbial cell factories · 2013Article
- PLGA microparticles in respirable sizes enhance an in vitro T cell response to recombinant Mycobacterium tuberculosis antigen TB10.4-Ag85B.Pharmaceutical research · 2010Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
purposeRational design of recombinant antigens TB10.4 and TB10.4-Ag85B as subunit vaccine candidates against Mycobacterium tuberculosis. The main purpose is to obtain a large quantity of soluble antigens.
methodsRecombinant antigens were cloned in frame with the N-terminal thioredoxin and expressed in E. coli. The thioredoxin tag was removed by TEV protease. Nickel-affinity and size-exclusion chromatography were used to purify antigens to homogeneity. Antigen stability at different pH levels was studied by photon correlation spectrometry. Circular dichroism was used to probe antigen secondary structure and thermal stability.
resultsN-terminal thioredoxin fusion dramatically increased antigen solubility. Soluble TB10.4 and TB10.4-Ag85B were purified to homogeneity and obtained in milligram quantity. Co-expression of bacteria chaperons increased the yield of TB10.4-Ag85B. Soluble TB10.4 and TB10.4-Ag85B purified from the inclusion body showed a reversible structure change. However, Ag85B and soluble TB10.4-Ag85B showed a clear melting temperature, above which the secondary structure was lost dramatically.
conclusionSoluble TB10.4 and TB10.4-Ag85B were purified from the E. coli in significant quantities. The methods to purify and characterize these recombinant antigens were established, which paved the way for further vaccine development based on these antigens.
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