Result: According to our results, other less frequent mutations were associated to changes in the physico-chemical profile and potential protein domains: the T142I mutation was associated to the loss of a N-glycosylation site and to a decrease in antigenicity; the F159S mutation presented a more hydrophilic and flexible profile, associated to the insertion of a N-Myristilation site; and the H290D, C289R and F141S mutations were characterized by an increase in hydrophilicity and flexibility, the opposite of the D197N mutation which was associated to a decrease in flexibility (Data not shown).

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Result: The 197 amino acid site, which was already associated to the decrease in cellular fusion, was mutated (D197N) in two clone sequences in our data set: o

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