Abstract:
:Animal influenza viruses pose a clear threat to public health. Transmissibility among humans is a prerequisite for a novel influenza virus to cause a human pandemic. A novel reassortant swine influenza virus acquired sustained human-to-human transmissibility and caused the 2009 influenza pandemic. However, the molecular aspects of influenza virus transmission remain poorly understood. Here, we show that an amino acid in hemagglutinin (HA) is important for the 2009 H1N1 influenza pandemic virus (2009/H1N1) to bind to human virus receptors and confer respiratory droplet transmissibility in mammals. We found that the change from glutamine (Q) to arginine (R) at position 226 of HA, which causes a switch in receptor-binding preference from human α-2,6 to avian α-2,3 sialic acid, resulted in a virus incapable of respiratory droplet transmission in guinea pigs and reduced the virus's ability to replicate in the lungs of ferrets. The change from alanine (A) to threonine (T) at position 271 of PB2 also abolished the virus's respiratory droplet transmission in guinea pigs, and this mutation, together with the HA Q226R mutation, abolished the virus's respiratory droplet transmission in ferrets. Furthermore, we found that amino acid 271A of PB2 plays a key role in virus acquisition of the mutation at position 226 of HA that confers human receptor recognition. Our results highlight the importance of both the PB2 and HA genes on the adaptation and transmission of influenza viruses in humans and provide important insights for monitoring and evaluating the pandemic potential of field influenza viruses.
journal_name
J Viroljournal_title
Journal of virologyauthors
Zhang Y,Zhang Q,Gao Y,He X,Kong H,Jiang Y,Guan Y,Xia X,Shu Y,Kawaoka Y,Bu Z,Chen Hdoi
10.1128/JVI.00958-12subject
Has Abstractpub_date
2012-09-01 00:00:00pages
9666-74issue
18eissn
0022-538Xissn
1098-5514pii
JVI.00958-12journal_volume
86pub_type
杂志文章abstract:UNLABELLED:Influenza virus hemagglutinin (HA) mediates virus entry by binding to cell surface receptors and fusing the viral and endosomal membranes following uptake by endocytosis. The acidic environment of endosomes triggers a large-scale conformational change in the transmembrane subunit of HA (HA2) involving a loop...
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pub_type: 杂志文章
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pub_type: 杂志文章
doi:10.1128/JVI.63.12.5354-5363.1989
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journal_title:Journal of virology
pub_type: 杂志文章
doi:10.1128/JVI.69.8.4914-4923.1995
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journal_title:Journal of virology
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