Phylogenetic analysis and docking study of neuraminidase gene of influenza A/H1N1 viruses circulating in Iran from 2010 to 2019.

Influenza A viruses (H1N1) have been consistently one of the most evolving viruses that escape from vaccine-induced immunity. Although there has been a rapid rise in human influenza virus knowledge since the 2009 pandemic, the molecular information about Iranian strains is still inadequate. The aim of this study was to analyze the neuraminidase (NA) segment of the Iranian isolates in terms of phylogenetic, antiviral resistance, and vaccine efficiency. Ninety-three NA sequences collected among 1758 nasopharyngeal swab samples during the 2015-2016 influenza season were sequenced and submitted to NCBI. Moreover, all the submitted Iranian influenza H1N1 NA sequences since 2010 till 2019 were included in the study. Software including MEGA-X, MODELLER, UCSF ChimeraX, Auto-Dock 4.2, and other online tools were used to analyze the phylogenetic relationship, vaccine efficiency, and binding affinity to sialic acid of the selected NA proteins. Moreover, the information about antiviral drug resistance mutations of NA were gathered and compared to the Iranian NA segments to check the presence of antiviral drug-resistant strains. The phylogenetic study showed that most Iranian NA sequences (between 2015 and 2016) were located in a single clade and following years were located in its subclade by 3 major mutations (G77R/K, V81A, and J188T). Resistant mutations in drug targets of NA including I117M, D151E, I223V, and S247N were ascertained in 10 isolates during the 2015-2016 flu seasons. Investigation of vaccination effect revealed that Iranian isolates in 2017 and 2018 were best matched to A/Brisbane/02/2018 (H1N1), and in 2019 to A/Guangdong-Maonan/SWL1536/2019 (H1N1). Furthermore, we performed an in-silico analysis of NA enzymatic activity of all Iranian sequences by assessment of enzyme stability, ligand affinity, and active site availability. Overall, the enzyme activity of four Iranian strains (AUG84119, AUG84157, AUG84095, and AUG84100) was assumed as the maximum enzyme activity. This study highlighted the evolutionary trend of influenza A virus/H1N1 circulating in Iran, which provides a preliminary viewpoint for a better comprehension of new emerging strains' virulence and thus, more appropriate monitoring of influenza virus A/H1N1 during each outbreak season.

Prevalence of human influenza virus in Iran: Evidence from a systematic review and meta-analysis.

This systematic review and meta-analysis was conducted to consolidate the information on the prevalence of the human influenza virus, including H1N1 and H3N2 as well as B-type influenza across Iran from 2000 to December 2016. The literature search was based on keywords including "influenza and Iran", "human influenza", "prevalence", "relative frequency", "incidence", and "drug" in MEDLINE (PubMed), Web of Science, Scopus, ScienceDirect, the Iranian Research Institute for Information Science and Technology (IranDoc), the Regional Information Centre for Science & Technology (RICeST), and the Scientific Information Database (SID). The literature search revealed 25 prevalence and seven drug resistance studies. In order to investigate the publication bias among studies, funnel plots and Egger's test were used. Additionally, the statistical tests of I2, Chi2, and Tau2 were computed, and the results were visualized with forest plots. A high level of I2 and Chi2 were obtained among studies, which are representative of the high variation and remarkable heterogeneity between studies. This may be because of various methodologies applied in the studies such as study design, age groups, and different populations. The prevalence of influenza H1N1, H3N2, and B in Iran have not yet been well evaluated. The heterogeneity among studies reveals that more attention should be paid to considering various factors, including gender, population size, and underlying conditions.

Confined water dissociation in microporous defective silicates: mechanism, dipole distribution, and impact on substrate properties.

Interest in microporous materials has risen in recent years, as they offer a confined environment that is optimal to enhance chemical reactions. Calcium silicate hydrate (C-S-H) gel, the main component of cement, presents a layered structure with sub-nanometer-size disordered pores filled with water and cations. The size of the pores and the hydrophilicity of the environment make C-S-H gel an excellent system to study the possibility of confined water reactions. To investigate it, we have performed molecular dynamics simulations using the ReaxFF force field. The results show that water does dissociate to form hydroxyl groups. We have analyzed the water dissociation mechanism, as well as the changes in the structure and water affinity of the C-S-H matrix and water polarization, comparing the results with the behavior of water in a defective zeolite. Finally, we establish a relationship between water dissociation in C-S-H gel and the increase of hardness due to a transformation from a two- to a three-dimensional structure.