Background and Aims: Nonstructural (NS1) protein is mainly involved in virulence and replication of several viruses, including influenza virus A (H1N1); surveillance of the latter started in India in 2009. The objective of this study was to identify the new substitutions in NS1 protein from the influenza virus A (H1N1) pandemic 2009 (pdm09) strain isolated in India. Methods:The sequences of NS1 proteins from influenza A(H1N1) pdm09 strains isolated in India were obtained from publicly available databases. Multiple sequence alignment and phylogeny analyses were performed to confirm the "consistent substitutions" on NS1 protein from H1N1 (pdm09) Indian strains. Here, "consistent substitutions" were defined as the substitutions observed in all the sequences isolated in a year. Comparative analyses were performed among NS1 Indian sequences from A(H1N1) pdm09, A (H1N1) seasonal and A(H3N2) strains, and from A (H1N1) pdm09 global strains.Results: Eight substitutions were identified in the NS1 Indian sequence from the A(H1N1) pdm09 strain, two in RBD, five in ED, and one in the linker region. Three new substitutions were reported in this study at NS1 sequence positions 2, 80, and 155, which evolved within 2015-2019 and became "consistent." These new substitutions were associated with conservative paired substitutions in the alternative domains of the NS1 protein. Three paired substitutions were (i) D2E and E125D, (ii) T80A and A155T, and (iii) E55K and K131E. Conclusions: This study indicates the continuous evolution of NS1 protein from the influenza A virus. The new substitutions at positions 2 and 80 occurred in the RNA binding and eIF4GI binding domains. The D2E substitution evolved simultaneously with the E125D substitution that involved viral replication. The third new substitution at position 155 occurred in the PI3K binding domain. The possible
Perception is often the expected outcome of our actions, while at other times it emerges from unexpected changes in the scene. During spatial navigation, animals must differentiate between cues generated by self-motion from motion that originated externally. To reveal the neural basis of this perceptual ability, we examined the midbrain superior colliculus (SC), which contains an egocentric map of sensorimotor space. By simulating whisker-guided navigation through a dynamic landscape, we discovered a transient neural response that selectively emerged for unexpected, externally generated tactile motion. This transient response only emerged when external motion engaged different whiskers, arguing that sensorimotor predictions are specific to a somatotopic location. When external motion engaged the same whiskers, neurons encoded surface motion with shifts in spike timing correlated to self-generated tactile features. Thus, a persistent representation of self-generated touch may be necessary to encode spatial features finer than the receptor array. In conclusion, the SC contains complementary rate and temporal codes to differentiate external from self-generated spatial features during tactile localization.
The routine influenza (H1N1) surveillance in India started almost a decade ago. The fluctuation in the number of deaths and cases in different Indian states over the last decade presumably indicated the possible changes in the viral sequence and in the immune response of the host. To track these changes, we have chosen NS1 protein that invades host antiviral immune response. Objective of this study was to identify the recent mutations on NS1 protein from Indian isolates. The sequences of NS1 proteins from H1N1 strains isolated in India over a decade were obtained from publicly available databases. Multiple sequence alignment, phylogeny and surface hydrophilicity analyses were performed to confirm the consistent mutations on NS1 protein, evolved chronologically in India. Total eight mutations were identified, two in RNA-binding domain (RBD), five in effector domain (ED) and one in the linker region. Three mutations were reported first time in this study at the sequence positions, 2, 80 and 155; those evolved either in 2017 or in 2019. These recent mutations were associated with conservative substitutions in the alternative domains of NS1 protein, namely, i) D2E and E55D, ii) T80A and A155T and iii) E55K and K131E. A gradual shift of NS1 antigenic regions (surface hydrophilicity) was observed from ED to RBD domains along the time line. The possible consequences of these mutations on host-pathogen interactions were hypothesized based on the sequence positions of NS1 mutations belonging to various cellular-binding sub-domains. The hypothesis is subject to further experimental and computational verification.
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