Raman signatures of type A and B influenza viruses: molecular origin of the "" inactivation mechanism mediated by micrometric silicon nitride powder.

A multiomic study of the structural characteristics of type A and B influenza viruses by means of highly spectrally resolved Raman spectroscopy is presented. Three virus strains, A H1N1, A H3N2, and B98, were selected because of their known structural variety and because they have co-circulated with variable relative prevalence within the human population since the re-emergence of the H1N1 subtype in 1977. Raman signatures of protein side chains tyrosine, tryptophan, and histidine revealed unequivocal and consistent differences for pH characteristics at the virion surface, while different conformations of two C-S bond configurations in and methionine rotamers provided distinct low-wavenumber fingerprints for different virus lineages/subtypes.