Recombinant Salmonella heidelberg ATP synthase subunit b (atpF) refers to a synthetically produced version of the atpF protein, which is a subunit of the ATP synthase enzyme found in Salmonella heidelberg . ATP synthase is an essential enzyme complex responsible for producing adenosine triphosphate (ATP), the primary energy currency of cells, through oxidative phosphorylation . The "b" subunit, or atpF, is a component of the F0 sector of the ATP synthase, which is embedded in the cell membrane and facilitates proton transport .
The recombinant form of this protein is typically produced in a host organism such as E. coli, yeast, baculovirus, or mammalian cells, using genetic engineering techniques . The gene encoding the Salmonella heidelberg atpF subunit is inserted into a vector and expressed in the host organism, which then produces the protein . The recombinant protein can then be isolated and purified for various research and industrial applications .
Vaccine Development: Recombinant Salmonella proteins, including atpF, are used in vaccine development . Attenuated Salmonella strains can be used as oral delivery systems for recombinant vaccine antigens .
Enzyme-Linked Immunosorbent Assays (ELISAs): Recombinant proteins are utilized in ELISAs to detect and quantify antibodies targeting specific Salmonella antigens .
ATP Synthase Research: The atpF subunit is crucial for understanding the structure and function of ATP synthase . Studies on this subunit can provide insights into the mechanism of ATP synthesis and proton translocation .
Type-III Secretion System (T3SS) Studies: Research indicates that ATP hydrolysis is not always essential for type-III protein secretion in Salmonella . The energy of the proton motive force can compensate for the absence of ATPase activity in certain conditions .
In vitro Diagnostics: Recombinant Salmonella antigen proteins are used for in vitro diagnostics .
F1F0 ATP synthase synthesizes ATP from ADP using a proton or sodium gradient. This enzyme comprises two domains: the F1 domain, containing the extramembranous catalytic core; and the F0 domain, containing the membrane proton channel. These domains are connected by a central and a peripheral stalk. ATP synthesis in the F1 catalytic domain is coupled to proton translocation via a rotary mechanism of the central stalk subunits. This protein is a component of the F0 channel and forms part of the peripheral stalk, linking F1 to F0.
KEGG: seh:SeHA_C4200