The 150-Loop Restricts the Host Specificity of Human H10N8 Influenza Virus

Tzarum, Netanel; de Vries, Robert P.; Peng, Wenjie; Thompson, Andrew J.; Bouwman, Kim M.; McBride, Ryan; Yu, Wenli; Zhu, Xueyong; Verheije, Monique H.; Paulson, James C.; Wilson, Ian A.

doi:10.1016/j.celrep.2017.03.054

Title: The 150-Loop Restricts the Host Specificity of Human H10N8 Influenza Virus

Full Record
Other Related Research

Authors:: Tzarum, Netanel; de Vries, Robert P.; Peng, Wenjie; Thompson, Andrew J.; Bouwman, Kim M.; McBride, Ryan; Yu, Wenli; Zhu, Xueyong; Verheije, Monique H.; Paulson, James C.; Wilson, Ian A.

Publication Date:: Sat Apr 01 00:00:00 EDT 2017

Sponsoring Org.:: USDOE

OSTI Identifier:: 1351015

Grant/Contract Number:: AC02-06CH11357; P41GM103393; P41RR001209

Resource Type:: Published Article

Journal Name:: Cell Reports

Additional Journal Information:: Journal Name: Cell Reports Journal Volume: 19 Journal Issue: 2; Journal ID: ISSN 2211-1247

Publisher:: Elsevier

Country of Publication:: Netherlands

Language:: English

Citation Formats


                    Tzarum, Netanel, de Vries, Robert P., Peng, Wenjie, Thompson, Andrew J., Bouwman, Kim M., McBride, Ryan, Yu, Wenli, Zhu, Xueyong, Verheije, Monique H., Paulson, James C., and Wilson, Ian A. The 150-Loop Restricts the Host Specificity of Human H10N8 Influenza Virus.  Netherlands: N. p., 2017. 
Web.  doi:10.1016/j.celrep.2017.03.054.

Copy to clipboard


                    Tzarum, Netanel, de Vries, Robert P., Peng, Wenjie, Thompson, Andrew J., Bouwman, Kim M., McBride, Ryan, Yu, Wenli, Zhu, Xueyong, Verheije, Monique H., Paulson, James C., & Wilson, Ian A. The 150-Loop Restricts the Host Specificity of Human H10N8 Influenza Virus.  Netherlands.  https://doi.org/10.1016/j.celrep.2017.03.054

Copy to clipboard


                    Tzarum, Netanel, de Vries, Robert P., Peng, Wenjie, Thompson, Andrew J., Bouwman, Kim M., McBride, Ryan, Yu, Wenli, Zhu, Xueyong, Verheije, Monique H., Paulson, James C., and Wilson, Ian A. Sat .  
"The 150-Loop Restricts the Host Specificity of Human H10N8 Influenza Virus".  Netherlands.  https://doi.org/10.1016/j.celrep.2017.03.054.

Copy to clipboard


                    
@article{osti_1351015,

  title        = {The 150-Loop Restricts the Host Specificity of Human H10N8 Influenza Virus},

  author       = {Tzarum, Netanel and de Vries, Robert P. and Peng, Wenjie and Thompson, Andrew J. and Bouwman, Kim M. and McBride, Ryan and Yu, Wenli and Zhu, Xueyong and Verheije, Monique H. and Paulson, James C. and Wilson, Ian A.},

  abstractNote = {},

  doi          = {10.1016/j.celrep.2017.03.054},

  journal      = {Cell Reports},

  number       = 2,

  volume       = 19,

  place        = {Netherlands},

  year         = {Sat Apr 01 00:00:00 EDT 2017},

  month        = {Sat Apr 01 00:00:00 EDT 2017}

}

Copy to clipboard

Journal Article:

Free Publicly Available Full Text

Publisher's Version of Record
https://doi.org/10.1016/j.celrep.2017.03.054

Other availability

Search WorldCat to find libraries that may hold this journal

Citation Metrics:

Cited by: 26 works

Citation information provided by
Web of Science

Save / Share:

Export Metadata

Save to My Library

Similar Records in DOE PAGES and OSTI.GOV collections:

The 150-Loop Restricts the Host Specificity of Human H10N8 Influenza Virus

Journal Article Tzarum, Netanel ; de Vries, Robert P. ; Peng, Wenjie ; ... - Cell Reports
https://doi.org/10.1016/j.celrep.2017.03.054
A Human-Infecting H10N8 Influenza Virus Retains a Strong Preference for Avian-type Receptors

Journal Article Zhang, Heng ; de Vries, Robert P. ; Tzarum, Netanel ; ... - Cell Host & Microbe

Recent avian-origin H10N8 influenza A viruses that have infected humans pose a potential pandemic threat. Alterations in the viral surface glycoprotein, hemagglutinin (HA), typically are required for influenza A viruses to cross the species barrier for adaptation to a new host, but whether H10N8 contains adaptations supporting human infection remains incompletely understood. In this paper, we investigated whether H10N8 HA can bind human receptors. Sialoside glycan microarray analysis showed that the H10 HA retains a strong preference for avian receptor analogs and negligible binding to human receptor analogs. Crystal structures of H10 HA with avian and human receptor analogs revealedmore »« less
Cited by 48
https://doi.org/10.1016/j.chom.2015.02.006
Three mutations switch H7N9 influenza to human-type receptor specificity

Journal Article de Vries, Robert P. ; Peng, Wenjie ; Grant, Oliver C. ; ... - PLoS Pathogens

The avian H7N9 influenza outbreak in 2013 resulted from an unprecedented incidence of influenza transmission to humans from infected poultry. The majority of human H7N9 isolates contained a hemagglutinin (HA) mutation (Q226L) that has previously been associated with a switch in receptor specificity from avian-type (NeuAcα2-3Gal) to human-type (NeuAcα2-6Gal), as documented for the avian progenitors of the 1957 (H2N2) and 1968 (H3N2) human influenza pandemic viruses. While this raised concern that the H7N9 virus was adapting to humans, the mutation was not sufficient to switch the receptor specificity of H7N9, and has not resulted in sustained transmission in humans. Tomore »« less
Cited by 67
https://doi.org/10.1371/journal.ppat.1006390

Full Text Available
Broadly protective human antibodies that target the active site of influenza virus neuraminidase

Journal Article Stadlbauer, Daniel ; Zhu, Xueyong ; McMahon, Meagan ; ... - Science

Better vaccines against influenza virus are urgently needed to provide broader protection against diverse strains, subtypes, and types. Such efforts are assisted by the identification of novel broadly neutralizing epitopes targeted by protective antibodies. Influenza vaccine development has largely focused on the hemagglutinin, but the other major surface antigen, the neuraminidase, has reemerged as a potential target for universal vaccines. We describe three human monoclonal antibodies isolated from an H3N2-infected donor that bind with exceptional breadth to multiple different influenza A and B virus neuraminidases. These antibodies neutralize the virus, mediate effector functions, are broadly protective in vivo, and inhibitmore »« less
Cited by 98
https://doi.org/10.1126/science.aay0678
N-Glycolylneuraminic Acid as a Receptor for Influenza A Viruses

Journal Article Broszeit, Frederik ; Tzarum, Netanel ; Zhu, Xueyong ; ... - Cell Reports

A species barrier for the influenza A virus is the differential expression of sialic acid, which can either be α2,3-linked for avians or α2,6-linked for human viruses. The influenza A virus hosts also express other species-specific sialic acid derivatives. One major modification at C-5 is N-glycolyl (NeuGc), instead of N-acetyl (NeuAc). N-glycolyl is mammalian specific and expressed in pigs and horses, but not in humans, ferrets, seals, or dogs. Hemagglutinin (HA) adaptation to either N-acetyl or N-glycolyl is analyzed on a sialoside microarray containing both α2,3- and α2,6-linkage modifications on biologically relevant N-glycans. Binding studies reveal that avian, human, andmore »« less
Cited by 44
https://doi.org/10.1016/j.celrep.2019.05.048

Similar Records