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Structure and Receptor Specificity of the Hemagglutinin from an H5N1 Influenza Virus
TLDR
The hemagglutinin structure at 2.9 angstrom resolution, from a highly pathogenic Vietnamese H5N1 influenza virus, is more related to the 1918 and other human H1 HAs than to a 1997 duck H5 HA, which suggests a path for this H 5N1 virus to gain a foothold in the human population. Expand
Cross-reactive antibody responses to the 2009 pandemic H1N1 influenza virus.
TLDR
Vaccination with recent seasonal nonadjuvanted or adjuvanted influenza vaccines induced little or no cross-reactive antibody response to 2009 H1N1 in any age group. Expand
Transmission and Pathogenesis of Swine-Origin 2009 A(H1N1) Influenza Viruses in Ferrets and Mice
TLDR
Although results were variable, it seems that the 2009 A(H1N1) virus may be less efficiently transmitted by respiratory droplets in comparison to the highly transmissible seasonal H1n1 virus, suggesting that additional virus adaptation in mammals may be required before the authors see phenotypes observed in earlier pandemics. Expand
H5N1 and 1918 Pandemic Influenza Virus Infection Results in Early and Excessive Infiltration of Macrophages and Neutrophils in the Lungs of Mice
TLDR
Investigation of the cellular immune response to infection in the mouse lung by flow cytometry shows that infection with HP influenza viruses such as H5N1 and the 1918 pandemic virus leads to a rapid cell recruitment of macrophages and neutrophils into the lungs, suggesting that these cells play a role in acute lung inflammation associated with HP virus infection. Expand
A Two-Amino Acid Change in the Hemagglutinin of the 1918 Influenza Virus Abolishes Transmission
TLDR
These findings confirm an essential role of hemagglutinin receptor specificity for the transmission of influenza viruses among mammals and suggest that a predominant human α-2,6 sialic acid binding preference is essential for optimal transmission of this pandemic virus. Expand
A Single Mutation in the PB1-F2 of H5N1 (HK/97) and 1918 Influenza A Viruses Contributes to Increased Virulence
TLDR
Data show that a single amino acid substitution in PB1-F2 can result in increased viral pathogenicity and could be one of the factors contributing to the high lethality seen with the 1918 pandemic virus. Expand
Pathogenicity of Influenza Viruses with Genes from the 1918 Pandemic Virus: Functional Roles of Alveolar Macrophages and Neutrophils in Limiting Virus Replication and Mortality in Mice
TLDR
Results indicate that a human influenza H1N1 virus possessing the 1918 HA and NA glycoproteins can induce severe lung inflammation consisting of AMs and neutrophils, which play a role in controlling the replication and spread of 1918 HA/NA:Tx/91 virus after intranasal infection of mice. Expand
A Single Amino Acid Substitution in 1918 Influenza Virus Hemagglutinin Changes Receptor Binding Specificity
TLDR
It is shown that the hemagglutinin (HA) of the virus that caused the 1918 influenza pandemic has strain-specific differences in its receptor binding specificity. Expand
Cellular transcriptional profiling in influenza A virus-infected lung epithelial cells: The role of the nonstructural NS1 protein in the evasion of the host innate defense and its potential
TLDR
The results suggest that the cellular response to influenza A virus infection in human lung cells is significantly influenced by the sequence of theNS1 gene, demonstrating the importance of the NS1 protein in regulating the host cell response triggered by virus infection. Expand
Early and sustained innate immune response defines pathology and death in nonhuman primates infected by highly pathogenic influenza virus
TLDR
The H5N1 virus was exceptional for the extent of tissue damage, cytokinemia, and interference with immune regulatory mechanisms, which may help explain the extreme virulence of HPAI viruses in humans. Expand
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