The mechanism of poly-galloyl-glucoses preventing Influenza A virus entry into host cells.
Hemagglutinin (HA) is essential for Influenza A virus infection, but its diversity of subtypes presents an obstacle to developing broad-spectrum HA inhibitors. In this study, we investigated the molecular mechanisms by which poly-galloyl glucose (pGG) analogs inhibit influenza hemagglutinin (HA) in...
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2014
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oai:doaj.org-article:ca460c7486ee4abd8e69d2c760c704682021-11-18T08:24:06ZThe mechanism of poly-galloyl-glucoses preventing Influenza A virus entry into host cells.1932-620310.1371/journal.pone.0094392https://doaj.org/article/ca460c7486ee4abd8e69d2c760c704682014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24718639/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Hemagglutinin (HA) is essential for Influenza A virus infection, but its diversity of subtypes presents an obstacle to developing broad-spectrum HA inhibitors. In this study, we investigated the molecular mechanisms by which poly-galloyl glucose (pGG) analogs inhibit influenza hemagglutinin (HA) in vitro and in silico. We found that (1) star-shaped pGG analogs exhibit HA-inhibition activity by interacting with the conserved structural elements of the receptor binding domain (RBD); (2) HA inhibition depends on the number of galloyl substituents in a pGG analog; the best number is four; and when PGG binds with two HA trimers at their conserved receptor binding domains (loop 130, loop 220, and 190-α-helix), PGG acts as a molecular glue by aggregating viral particles so as to prevent viral entry into host cells (this was revealed via an in silico simulation on the binding of penta-galloyl-glucose (PGG) with HA). pGGs are also effective on a broad-spectrum influenza A subtypes (including H1, H3, H5, H7); this suggests that pGG analogs can be applied to most influenza A subtypes as a prophylactic against influenza viral infections.Hu GeGe LiuYang-Fei XiangYu WangChao-Wan GuoNan-Hao ChenYing-Jun ZhangYi-Fei WangKaio KitazatoJun XuPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 4, p e94392 (2014) |
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Medicine R Science Q |
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Medicine R Science Q Hu Ge Ge Liu Yang-Fei Xiang Yu Wang Chao-Wan Guo Nan-Hao Chen Ying-Jun Zhang Yi-Fei Wang Kaio Kitazato Jun Xu The mechanism of poly-galloyl-glucoses preventing Influenza A virus entry into host cells. |
| description |
Hemagglutinin (HA) is essential for Influenza A virus infection, but its diversity of subtypes presents an obstacle to developing broad-spectrum HA inhibitors. In this study, we investigated the molecular mechanisms by which poly-galloyl glucose (pGG) analogs inhibit influenza hemagglutinin (HA) in vitro and in silico. We found that (1) star-shaped pGG analogs exhibit HA-inhibition activity by interacting with the conserved structural elements of the receptor binding domain (RBD); (2) HA inhibition depends on the number of galloyl substituents in a pGG analog; the best number is four; and when PGG binds with two HA trimers at their conserved receptor binding domains (loop 130, loop 220, and 190-α-helix), PGG acts as a molecular glue by aggregating viral particles so as to prevent viral entry into host cells (this was revealed via an in silico simulation on the binding of penta-galloyl-glucose (PGG) with HA). pGGs are also effective on a broad-spectrum influenza A subtypes (including H1, H3, H5, H7); this suggests that pGG analogs can be applied to most influenza A subtypes as a prophylactic against influenza viral infections. |
| format |
article |
| author |
Hu Ge Ge Liu Yang-Fei Xiang Yu Wang Chao-Wan Guo Nan-Hao Chen Ying-Jun Zhang Yi-Fei Wang Kaio Kitazato Jun Xu |
| author_facet |
Hu Ge Ge Liu Yang-Fei Xiang Yu Wang Chao-Wan Guo Nan-Hao Chen Ying-Jun Zhang Yi-Fei Wang Kaio Kitazato Jun Xu |
| author_sort |
Hu Ge |
| title |
The mechanism of poly-galloyl-glucoses preventing Influenza A virus entry into host cells. |
| title_short |
The mechanism of poly-galloyl-glucoses preventing Influenza A virus entry into host cells. |
| title_full |
The mechanism of poly-galloyl-glucoses preventing Influenza A virus entry into host cells. |
| title_fullStr |
The mechanism of poly-galloyl-glucoses preventing Influenza A virus entry into host cells. |
| title_full_unstemmed |
The mechanism of poly-galloyl-glucoses preventing Influenza A virus entry into host cells. |
| title_sort |
mechanism of poly-galloyl-glucoses preventing influenza a virus entry into host cells. |
| publisher |
Public Library of Science (PLoS) |
| publishDate |
2014 |
| url |
https://doaj.org/article/ca460c7486ee4abd8e69d2c760c70468 |
| work_keys_str_mv |
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| _version_ |
1718421889726021632 |