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Detecting the Dominant T and B Epitopes of Klebsiella pneumoniae Ferric Enterobactin Protein (FepA) and Introducing a Single Epitopic Peptide as Vaccine Candidate.

ABSTRACT: Klebsiella pneumoniae causes various human infections. Ferric enterobactin protein (FepA) is a conserved protein of K. pneumoniae with high immunogenicity. In the present study, using comprehensive in silico approaches the T and B cell-specific epitopes of K. pneumoniae FepA were identified. The T (both class I and class II) and B (both linear and conformational) epitopes of FepA were predicted using prediction tools. The predicted epitopes were screened for human similarity, immunogenicity, antigenicity, allergenicity, toxicity, conservancy, structural and physicochemical suitability, and in case of T epitopes binding to HLA alleles, using numerous immune-informatics, homology modeling, and molecular docking approaches. These analyses led to introduce the most dominant FepA epitopes that are appropriate for vaccine development. Furthermore, we introduced an antigenic peptide containing both T and B epitopes which comprises suitable structural and physiochemical properties needed for vaccine development and it is conserved in many bacteria. Altogether, here the highly immunogenic T and B epitopes of FepA as well as a final epitopic peptide containing both T and B epitopes were found and introduced for future vaccine development studies. It is suggested that the actual efficiency and efficacy of our final epitopic peptide be investigated by in vitro/in vivo testing.

Supplementary information

The online version contains supplementary material available at 10.1007/s10989-021-10247-3.

SUBMITTER: Nemati Zargaran F

PROVIDER: S-EPMC8243051 | biostudies-literature |

REPOSITORIES: biostudies-literature

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Project description:The siderophore enterobactin (Ent) is produced by many species of enteric bacteria to mediate iron uptake. This iron scavenger can be reincorporated by the bacteria as the ferric complex [Fe(III)(Ent)](3)(-) and is subsequently hydrolyzed by an esterase to facilitate intracellular iron release. Recent literature reports on altered protein recognition and binding of modified enterobactin increase the significance of understanding the structural features and solution chemistry of ferric enterobactin. The structure of the neutral protonated ferric enterobactin complex [Fe(III)(H(3)Ent)](0) has been the source of some controversy and confusion in the literature. To demonstrate the proposed change of coordination from the tris-catecholate [Fe(III)(Ent)](3)(-) to the tris-salicylate [Fe(III)(H(3)Ent)](0) upon protonation, the coordination chemistry of two new model compounds N,N',N''-tris[2-(hydroxybenzoyl)carbonyl]cyclotriseryl trilactone (SERSAM) and N,N',N''-tris[2-hydroxy,3-methoxy(benzoyl)carbonyl]cyclotriseryl trilactone (SER(3M)SAM) was examined in solution and solid state. Both SERSAM and SER(3M)SAM form tris-salicylate ferric complexes with spectroscopic and solution thermodynamic properties (with log beta(110)() values of 39 and 38 respectively) similar to those of [Fe(III)(H(3)Ent)](0). The fits of EXAFS spectra of the model ferric complexes and the two forms of ferric enterobactin provided bond distances and disorder factors in the metal coordination sphere for both coordination modes. The protonated [Fe(III)(H(3)Ent)](0) complex (d(Fe)(-)(O) = 1.98 A, sigma(2)(stat)(O) = 0.00351(10) A(2)) exhibits a shorter average Fe-O bond length but a much higher static Debye-Waller factor for the first oxygen shell than the catecholate [Fe(III)(Ent)](3)(-) complex (d(Fe)(-)(O) = 2.00 A, sigma(2)(stat)(O) = 0.00067(14) A(2)). (1)H NMR spectroscopy was used to monitor the amide bond rotation between the catecholate and salicylate geometries using the gallic complexes of enterobactin: [Ga(III)(Ent)](3)(-) and [Ga(III)(H(3)Ent)](0). The ferric salicylate complexes display quasi-reversible reduction potentials from -89 to -551 mV (relative to the normal hydrogen electrode NHE) which supports the feasibility of a low pH iron release mechanism facilitated by biological reductants.

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Detecting the Dominant T and B Epitopes of Klebsiella pneumoniae Ferric Enterobactin Protein (FepA) and Introducing a Single Epitopic Peptide as Vaccine Candidate.

Supplementary information

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