期刊
VIROLOGY
卷 562, 期 -, 页码 29-39出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2021.06.008
关键词
Influenza virus; Receptor; Hemagglutinin; Sulfated glycan; Egg-adaptation
类别
资金
- Japanese Initiative for Progress of Research on Infectious Disease for Global Epidemics (J-PRIDE) from the Japan Agency for Medical Research and Development (AMED) [JP17fm0208026]
- Ministry of Education, Culture, Sports, Science and Technology, Japan (MEXT)
The study revealed that human H1N1 viruses passaged in chicken embryos show enhanced binding to sulfated glycans, leading to increased production levels. This is attributed to the presence of 6-sulfo sialyl Lewis X and/or NeuAc alpha 2-3Gal beta 1-4(SO3-6)GlcNAc in the viruses, suggesting their involvement in efficient propagation in chicken embryos.
When human influenza viruses are isolated and passaged in chicken embryos, variants with amino acid substitutions around the receptor binding site of hemagglutinin (HA) are selected; however, the mechanisms that underlie this phenomenon have yet to be elucidated. Here, we analyzed the receptor structures that contributed to propagation of egg-passaged human H1N1 viruses. The analysis included seasonal and 2009 pandemic strains, both of which have amino acid substitutions of HA found in strains isolated or passaged in eggs. These viruses exhibited high binding to sulfated glycans containing NeuAc alpha 2-3Gal. In MDCK cells overexpressing the sulfotransferase that synthesize Gal beta 1-4(SO3--6)GlcNAc, production of human H1N1 viruses was increased up to 90 fold. Furthermore, these sulfated glycans were expressed on the allantoic and amniotic membranes of chicken embryos. These results suggest that 6-sulfo sialyl Lewis X and/or NeuAc alpha 2-3Gal beta 1-4(SO3--6)GlcNAc are involved in efficient propagation of human H1N1 viruses in chicken embryos.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据