About: A multiepitopic theoretical fusion construct based on in-silico epitope screening of known vaccine candidates for protection against wide range of enterobacterial pathogens

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About: A multiepitopic theoretical fusion construct based on in-silico epitope screening of known vaccine candidates for protection against wide range of enterobacterial pathogens Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	A multiepitopic theoretical fusion construct based on in-silico epitope screening of known vaccine candidates for protection against wide range of enterobacterial pathogens
Creator	Kumar, Ashutosh Chhibber, Sanjay Harjai, Kusum
Source	Elsevier; Medline; PMC
abstract	Abstract Enterobacterial pathogens that have acquired antibiotic resistance genes are a leading cause of community and hospital acquired infections. In such a situation vaccination is considered as a better option to prevent such infections. In the current study reverse vaccinology approach has been used to select peptides from already known immunogenic proteins to design a chimeric construct. We selected Yersiniabactin receptor of Escherichia coli UMN026 and Flagellin of Stenotrophomonas maltophila. B-cell linear epitopes were predicted using Bepipred prediction tool. Peptide binding with reference sets of 27 alleles of MHC class I and class II was also analyzed. The predicted peptides-MHC complexes were further validated using simulation dynamics. The in-silico construction of chimera was done by restriction mapping and codon optimization. Chimera was evaluated using the immunoinformatic approach as done for the selected proteins. From the 673 amino acids of FyuA protein, a region from 1 to 492 was selected for containing more linear epitopes and the processing scores obtained were significant for MHC class I and class II binding. Similarly, from Flagellin, a region between 60 and 328 amino acids was selected and the peptides present in the selected region showed lower percentile ranks for binding with MHC molecules. The simulation studies validated the predictions of peptide-MHC complexes. The selected gene fragments accommodating maximum part of these peptides were used to design a chimaeric construct of 2454 bp. From the immunoinformatic analysis, the chimera was found to be more immunogenic in terms of increased number of B-cell and T-cell epitopes along with increased coverage of global populations with allelic variability.
has issue date	2019-07-31(xsd:dateTime)
bibo:doi	10.1016/j.humimm.2019.02.008
bibo:pmid	30769032
has license	els-covid
sha1sum (hex)	c40e0bbb4b43900b06fe7717b8a41e181a8607e5
schema:url	https://doi.org/10.1016/j.humimm.2019.02.008
resource representing a document's title	A multiepitopic theoretical fusion construct based on in-silico epitope screening of known vaccine candidates for protection against wide range of enterobacterial pathogens
has PubMed Central identifier	PMC7115567
has PubMed identifier	30769032
schema:publication	Human Immunology
resource representing a document's body	covid:c40e0bbb4b43900b06fe7717b8a41e181a8607e5#body_text
is schema:about of	named entity 'complexes' named entity 'MHC class I' named entity 'acquired' named entity 'hospital acquired infections' named entity 'chimera' named entity 'region' named entity 'amino acids' named entity 'WIDE' named entity 'CONSTRUCT' named entity 'PEPTIDE BINDING' named entity 'CURRENT' named entity 'TOOL' named entity 'CAUSE' named entity 'GLOBAL' named entity 'DYNAMICS' named entity 'CONSIDERED' named entity '328' named entity 'SITUATION' named entity 'PEPTIDES' named entity 'MHC CLASS I' named entity 'LINEAR' named entity 'SIMULATION' named entity 'ANTIBIOTIC RESISTANCE' named entity 'MAXIMUM' named entity 'FLAGELLIN' named entity 'FUSION' named entity 'IMMUNOGENIC' named entity 'VACCINE' named entity 'REFERENCE' named entity 'INCREASED NUMBER OF' named entity '673' named entity 'BINDING' named entity 'BASED' named entity 'SCREENING' named entity 'KNOWN' named entity 'THEORETICAL' named entity 'PATHOGENS' named entity 'PROTECTION' named entity 'EPITOPES' named entity 'AMINO ACIDS' named entity 'EVALUATED' named entity 'CONSTRUCT' named entity 'PROTEIN' named entity 'ACQUIRED' named entity 'YERSINIABACTIN' named entity 'PREDICTED' named entity 'CONTAINING' named entity 'ESCHERICHIA COLI UMN026' named entity 'PEPTIDE-MHC' named entity 'VALIDATED' named entity 'GENE' named entity 'SCORES' named entity 'REGION' named entity 'HAVE' named entity 'CODON OPTIMIZATION' named entity 'SELECT' named entity 'INFECTIONS' named entity 'FYUA' named entity 'OPTION' named entity 'VARIABILITY' named entity 'PROCESSING' named entity 'ALLELES' named entity 'LEADING' named entity 'VACCINATION' named entity 'EPITOPE' named entity 'RANGE' named entity 'TO PREVENT' named entity 'COMPLEXES' named entity 'STENOTROPHOMONAS MALTOPHILA' named entity 'KNOWN' named entity 'B-CELL' named entity 'T-CELL' named entity 'RESISTANCE GENES' named entity 'PROTEINS' named entity 'RECEPTOR' named entity 'MHC' named entity 'PART OF' named entity 'POPULATIONS' named entity 'INCREASED'

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