This work is part of a longitudinal study on the evolutionary pressure at the arginine dimer of the SARS-CoV-2 S-protein polybasic furin cleavage site. When a virus precursor acquired that furin site, it was not only a huge gain-of-function, but it was also the origin of a species (SARS-CoV-2). At molecular level, the furin site opened up two conceptually highly opposed landscapes. First (favourable for the virus), at protein level, the arginine dimer within the furin site provides an additional positive charge to the S protein that is crucial for the human furin activity. Second (no favourable for the virus), at gene level, this arginine dimer is CGG-CGG encoded. The CGG arginine codon is the arginine codon less favourable in the virus genome (arginine has six codons). The arginine codon usage bias could be a viral strategy to optimize that arginine dimer code. Results shown here thus suggest. They refer to a set of SARS-CoV-2 genomes (0.18 %), from a sample the last days of July, 2022, with a genetically optimized furin site.