Journal
SCIENCE
Volume 342, Issue 6155, Pages 243-247Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1242917
Keywords
-
Categories
Funding
- China Ministry of Science and Technology National 973 Project [2011CB504703]
- National Natural Science Foundation of China (NSFC) [81290342]
- Chinese Academy of Sciences [KSZD-EW-Z-002]
- NSFC Innovative Research Group [81021003]
- NSFC Medical Science Department [81341002]
Ask authors/readers for more resources
An avian-origin human-infecting influenza (H7N9) virus was recently identified in China. We have evaluated the viral hemagglutinin (HA) receptor-binding properties of two human H7N9 isolates, A/Shanghai/1/2013 (SH-H7N9) (containing the avian-signature residue Gln(226)) and A/Anhui/1/2013 (AH-H7N9) (containing the mammalian-signature residue Leu(226)). We found that SH-H7N9 HA preferentially binds the avian receptor analog, whereas AH-H7N9 HA binds both avian and human receptor analogs. Furthermore, an AH-H7N9 mutant HA (Leu(226) -> Gln) was found to exhibit dual receptor-binding property, indicating that other amino acid substitutions contribute to the receptor-binding switch. The structures of SH-H7N9 HA, AH-H7N9 HA, and its mutant in complex with either avian or human receptor analogs show how AH-H7N9 can bind human receptors while still retaining the avian receptor-binding property.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available