In Silico Targeting and Immunological Profiling of PpiA in Mycobacterium tuberculosis: A Computational Approach DOI Creative Commons
Mohammad Javad Nasiri,

Lily Rogowski,

Vishwanath Venketaraman

и другие.

Pathogens, Год журнала: 2025, Номер 14(4), С. 370 - 370

Опубликована: Апрель 9, 2025

Tuberculosis (TB) remains a leading cause of mortality, with drug resistance highlighting the need for new vaccine targets. Peptidyl-prolyl isomerase A (PpiA), conserved Mycobacterium tuberculosis (Mtb) protein, plays role in bacterial stress adaptation and immune evasion, making it potential target immunotherapy. This study uses computational methods to assess PpiA’s antigenicity, structural integrity, immunogenic potential. The PpiA sequence was retrieved from NCBI analyzed antigenicity allergenicity using VaxiJen, AllerTOP, AllergenFP. Physicochemical properties were evaluated ProtParam, models generated through PSIPRED SWISS-MODEL. Structural validation performed MolProbity, QMEANDisCo, ProSA-Web. B-cell epitopes predicted BepiPred 2.0 IEDB, while T-cell mapped via IEDB’s MHC-I MHC-II tools. Epitope conservation across Mtb strains confirmed ConSurf. Results indicate is highly antigenic, non-allergenic, stable, several identified both B- T-cells. supports as promising TB development.

Язык: Английский

In Silico Targeting and Immunological Profiling of PpiA in Mycobacterium tuberculosis: A Computational Approach DOI Creative Commons
Mohammad Javad Nasiri,

Lily Rogowski,

Vishwanath Venketaraman

и другие.

Pathogens, Год журнала: 2025, Номер 14(4), С. 370 - 370

Опубликована: Апрель 9, 2025

Tuberculosis (TB) remains a leading cause of mortality, with drug resistance highlighting the need for new vaccine targets. Peptidyl-prolyl isomerase A (PpiA), conserved Mycobacterium tuberculosis (Mtb) protein, plays role in bacterial stress adaptation and immune evasion, making it potential target immunotherapy. This study uses computational methods to assess PpiA’s antigenicity, structural integrity, immunogenic potential. The PpiA sequence was retrieved from NCBI analyzed antigenicity allergenicity using VaxiJen, AllerTOP, AllergenFP. Physicochemical properties were evaluated ProtParam, models generated through PSIPRED SWISS-MODEL. Structural validation performed MolProbity, QMEANDisCo, ProSA-Web. B-cell epitopes predicted BepiPred 2.0 IEDB, while T-cell mapped via IEDB’s MHC-I MHC-II tools. Epitope conservation across Mtb strains confirmed ConSurf. Results indicate is highly antigenic, non-allergenic, stable, several identified both B- T-cells. supports as promising TB development.

Язык: Английский

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