Preparation and Purification of Recombinant Protein Fragment OmpA240-356 from <i>Acinetobacter baumannii</i> as a Novel Epitope for Vaccination

AuthorMasoud Dadashien
AuthorAlireza Salimi Chiranien
AuthorHossein Goudarzien
AuthorElnaz Sadat Mirsamadien
AuthorShahin Bolorien
AuthorZohreh Ghalavanden
AuthorBahareh Hajikhanien
OrcidMasoud Dadashi [0000-0002-4800-2078]en
OrcidBahareh Hajikhani [0000-0001-7966-6267]en
Issued Date2019-10-31en
AbstractAcinetobacter baumannii has gained attention for years as a significant clinical problem due to the increase of antibiotic-resistant strain. Indeed, A. baumannii OmpA is one of the highly conserved membrane proteins among Gram-negative bacteria that has multiple roles in interacting with the host during infection, thereby representing an effective target for the development of novel antibacterial or vaccination therapies. Nowadays, finding suitable epitope-specific antigens inside the conserved proteins such as OmpA is a promising method for successful vaccination programs. Therefore, in the present study, the coding sequence of the 240 to 356 amino acid residues of A. baumannii OmpA (AbOmpA240-356) was cloned into the vector pET-28a and purified using nickel affinity chromatography. In addition, the anti-His tag antibody is used to validate its production. This system of protein expression and purification may be useful for further characterization of AbOmpA240-356 protein fraction. Therefore, this study can lead to the introduction of suitable candidates for the development of an effective vaccine based on OmpA against this bacterium for further analysis.en
DOIhttps://doi.org/10.5812/archcid.85933en
Keyword<i>Acinetobacter baumannii</i>en
KeywordOmpAen
KeywordRecombinant Proteinen
PublisherBrieflandsen
TitlePreparation and Purification of Recombinant Protein Fragment OmpA240-356 from <i>Acinetobacter baumannii</i> as a Novel Epitope for Vaccinationen
TypeResearch Articleen

Files