Virology. 2016 Apr 7;493:238-246. doi: 10.1016/j.virol.2016.03.025. [Epub ahead of print]
1918 Influenza receptor binding domain variants bind and replicate in primary human airway cells regardless of receptor specificity.
Davis AS1, Chertow DS2, Kindrachuk J3, Qi L4, Schwartzman LM4, Suzich J2, Alsaaty S3, Logun C3, Shelhamer JH3, Taubenberger JK5.
Author information
Abstract
The 1918 influenza pandemic caused ~50 million deaths. Many questions remain regarding the origin, pathogenicity, and mechanisms of human adaptation of this virus. Avian-adapted influenza A viruses preferentially bind α2,3-linked sialic acids (Sia) while human-adapted viruses preferentially bind α2,6-linked Sia. A change in Sia preference from α2,3 to α2,6 is thought to be a requirement for human adaptation of avian influenza viruses. Autopsy data from 1918 cases, however, suggest that factors other than Sia preference played a role in viral binding and entry to human airway cells. Here, we evaluated binding and entry of five 1918 influenza receptor binding domain variants in a primary human airway cell model along with control avian and human influenza viruses. We observed that all five variants bound and entered cells efficiently and that Sia preference did not predict entry of influenza A virus to primary human airway cells evaluated in this model.
Published by Elsevier Inc.
KEYWORDS:
Hemagglutinin; Influenza A virus; Pandemic; Receptor binding
PMID: 27062579 [PubMed - as supplied by publisher]
1918 Influenza receptor binding domain variants bind and replicate in primary human airway cells regardless of receptor specificity.
Davis AS1, Chertow DS2, Kindrachuk J3, Qi L4, Schwartzman LM4, Suzich J2, Alsaaty S3, Logun C3, Shelhamer JH3, Taubenberger JK5.
Author information
Abstract
The 1918 influenza pandemic caused ~50 million deaths. Many questions remain regarding the origin, pathogenicity, and mechanisms of human adaptation of this virus. Avian-adapted influenza A viruses preferentially bind α2,3-linked sialic acids (Sia) while human-adapted viruses preferentially bind α2,6-linked Sia. A change in Sia preference from α2,3 to α2,6 is thought to be a requirement for human adaptation of avian influenza viruses. Autopsy data from 1918 cases, however, suggest that factors other than Sia preference played a role in viral binding and entry to human airway cells. Here, we evaluated binding and entry of five 1918 influenza receptor binding domain variants in a primary human airway cell model along with control avian and human influenza viruses. We observed that all five variants bound and entered cells efficiently and that Sia preference did not predict entry of influenza A virus to primary human airway cells evaluated in this model.
Published by Elsevier Inc.
KEYWORDS:
Hemagglutinin; Influenza A virus; Pandemic; Receptor binding
PMID: 27062579 [PubMed - as supplied by publisher]