Disease relevance of OR6A2

• Role of the I7 protein in proteolytic processing of vaccinia virus membrane and core components [1].

High impact information on OR6A2

• In contrast, rescue did not occur when the putative protease active site residue histidine 241 or cysteine 328 of I7 was converted to alanine [1].
• In the absence of an inducer, the synthesis of I7 was repressed, proteolytic processing of the A17 membrane protein and the L4 core protein was inhibited, and virus morphogenesis was blocked [1].
• In conclusion, we provide evidence that I7 is a viral protease that is required for AG/X-specific cleavages of viral membrane and core proteins, which occur at early and late stages of virus assembly, respectively [1].
• The OR I7 is immobilized on a gold electrode by multilayer bioengineering based on a mixed self-assembled monolayer and biotin/avidin system, which allows for a well-controlled immobilization of the bioreceptor within its lipid environment [2].
• The results for QCM coated with cells containing the olfactory receptor showed that the expressed protein I7 strongly interacted with octyl aldehyde (octanal), which is an odorant specific to the I7 protein [3].

Anatomical context of OR6A2

• Functional expression of the rat I7 OR and its trafficking to the plasma membrane was achieved under optimized experimental conditions in the budding yeast Saccharomyces cerevisiae [4].

Analytical, diagnostic and therapeutic context of OR6A2

• Surprisingly, however, by Western blotting (immunoblotting) the I7 protein was present in similar amounts in the defective particles and in the IMVs isolated at the permissive temperature [5].
• The biosensor was probed with an array of odorants to demonstrate that the yeast-borne I7 OR retains its specificity and selectivity towards ligands [4].

References