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In silico design of a novel hybrid epitope-based antigen harboring highly exposed immunogenic peptides of BamA, OmpA, and Omp34 against Acinetobacter baumannii.
Hessami, Anahita; Mogharari, Zahra; Rahim, Fatemeh; Khalesi, Bahman; Jamal Nassrullah, Othman; Reza Rahbar, Mohammad; Khalili, Saeed; Jahangiri, Abolfazl.
Afiliación
  • Hessami A; School of Pharmacy, Shiraz University of Medical Sciences, Shiraz, Iran.
  • Mogharari Z; Faculty of Agriculture, Shahed University, Tehran, Iran.
  • Rahim F; Department of Molecular Genetics, Faculty of Biological Sciences, Tarbiat Modares, P.O. Box: 14115-154, Tehran, Iran.
  • Khalesi B; Department of Research and Production of Poultry Viral Vaccine, Razi Vaccine and Serum Research Institute, Agricultural Research Education and Extension Organization, Karaj, Iran.
  • Jamal Nassrullah O; College of Veterinary Medicine, Sulaimani University, Kurdistan Region, Iraq.
  • Reza Rahbar M; Pharmaceutical Sciences Research Center, Shiraz University of Medical Sciences, Shiraz, Iran.
  • Khalili S; Department of Biology Sciences, Shahid Rajaee Teacher Training University, Tehran, Iran.
  • Jahangiri A; Applied Microbiology Research Center, Biomedicine Technologies Institute, Baqiyatallah University of Medical Sciences, Tehran, Iran. Electronic address: jahangiri.fazel@gmail.com.
Int Immunopharmacol ; 142(Pt A): 113066, 2024 Sep 05.
Article en En | MEDLINE | ID: mdl-39241518
ABSTRACT
Acinetobacter baumannii, is among the highest priority bacteria according to the WHO categorization which necessitate the exploration of alternative strategies such as vaccination. OmpA, BamA, and Omp34 are assigned as appropriate antigens to serve in vaccine development against this pathogen. Experimentally validated exposed epitopes of OmpA and Omp34 along with selected exposed epitopes predicted by an integrative in silico approach were represented by the barrel domain of BamA as a scaffold. Among the 8 external loops of BamA, 5 loops were replaced with selected loops of OmpA and Omp34. The designed antigen was analyzed regarding the physicochemical properties, antigenicity, epitope retrieval, topology, structure, and safety. BamA is a two-domain OMP with a 16-stranded barrel in which L4, L6, and L7 were the longest loops of BamA in order. The designed antigen consisted of 478 amino acids with antigen probability of 0.7793. The novel antigen was a 16-stranded barrel. No identical 8-meric peptides were found in the human proteome against the designed antigen sequence. The designed construct was safe regarding the allergenicity, toxicity, and human proteome reactivity. The designed antigen could develop higher protection against A. baumannii in comparison to either OmpA, BamA, or Omp34 alone.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Int Immunopharmacol Asunto de la revista: ALERGIA E IMUNOLOGIA / FARMACOLOGIA Año: 2024 Tipo del documento: Article País de afiliación: Irán Pais de publicación: Países Bajos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Int Immunopharmacol Asunto de la revista: ALERGIA E IMUNOLOGIA / FARMACOLOGIA Año: 2024 Tipo del documento: Article País de afiliación: Irán Pais de publicación: Países Bajos