Salmonella Enteritidis is a serovar of Salmonella enterica, a Gram-negative bacterium belonging to the Enterobacteriaceae family. It is a significant pathogen responsible for foodborne illnesses in humans. The outer membrane proteins (OMPs) of Salmonella play crucial roles in its pathogenicity, including adhesion, invasion, and evasion of the host immune system. One such protein is the Outer Membrane Protein-A (OmpA), which has been studied for its potential as a vaccine candidate and its role in immune response modulation.
OmpA is a well-conserved protein found in the outer membrane of Gram-negative bacteria. It consists of an N-terminal β-barrel domain that spans the outer membrane and a C-terminal periplasmic domain. The β-barrel domain forms a pore that allows the passage of small molecules, while the periplasmic domain interacts with peptidoglycan, providing structural stability to the bacterial cell wall.
In Salmonella Enteritidis, OmpA is involved in various functions:
Recombinant OmpA refers to the protein produced through recombinant DNA technology. This involves cloning the gene encoding OmpA into an expression vector, which is then introduced into a host organism, such as Escherichia coli, to produce the protein in large quantities. The recombinant OmpA can be purified and used for various applications, including vaccine development and immunological studies.