L-2 cells produce defective doughnut shaped particles covered with about 10x the level of gp120, compared to wild type HIV-I on its surface. Ten years later the entire L-2 genome has been re-sequenced and a remarkable stability in sequence identity compared to the 1997 published sequence of 5 mutations was observed. The three additional mutations that have been defined in the new, complete sequence analysis are; one in Vif, one in RT and a repeat of P1 in the gag region. These regions may be crucial for L-2 function. In addition the 10 amino acid deletions in gp120 seen in 1997 are altered to 5 and a gp41 mutation K to R is replaced by the original K at Env amino acid position 660. This is about 130 amino acids upstream of the maintained gp41 amino acid position 36 of G which appears involved in alteration of the fusion domain. The latter mutation has been maintained over the 10 year period. It has become difficult to imagine that a classic HIV neutralizing and mucosal prophylactic vaccine can be produced because of the widespread and continuing recombination of the HIV genome. The increased level of gp120 on L-2 particles; its defective nature and stability of L-2 as well as the discovery of plasmid pL2, which also produce L-2 particles and allow the ability to add multiple Clades to the envelope through cassette mutagenesis, could be a step in this direction.