Punctuated Evolution of Influenza Virus Neuraminidase (A/H1N1) under Opposing Migration and Vaccination Pressures

Table 1

Strain-averaged panoramic average hydropathicities ⟨𝜓⟩ for the two scales ⟨MZ⟩ and ⟨KD⟩ in the text.

	⟨MZ⟩	𝜎(⟨MZ⟩)	⟨KD⟩	𝜎(⟨KD⟩)
Lyso. (C)	153.1
Lyso. (H)	154.7
Adren. (H)	154.7
Rhodop. (L)	167.1
Rhodop. (C)	167.6
Rhodop. (H)	167.8
NA	151.5	0.4	159.7	0.3
HA	148.9	0.6	156.5	0.7

The standard deviations 𝜎 for NA are taken over the panorama plateaus 1945–2011. For HA the year 1996 was used to estimate 𝜎. Also shown are lysozyme 𝑐, adrenergic (𝛽1), and rhodopsin values of ⟨MZ⟩ and ⟨KD⟩ for several species (lamprey (L), chicken (C), and human (H)). In general evolution stabilizes proteins by compacting them and increasing ⟨𝜓⟩. Note that rhodopsin is exceptionally stable with a larger ⟨𝜓⟩ for the two scales, as it must be able to receive and process optical signals. NA is noticeably hydrophilic, and HA is even more hydrophilic (smallest ⟨𝜓⟩). The ⟨𝜓⟩ trends shown here are interesting, but the opposing viral effects of migration and vaccination pressures can be recognized only in the context of the more sophisticated discussion in the text.