Prediction of biological functions on glycosylation site migrations in human influenza H1N1 viruses.
Protein glycosylation alteration is typically employed by various viruses for escaping immune pressures from their hosts. Our previous work had shown that not only the increase of glycosylation sites (glycosites) numbers, but also glycosite migration might be involved in the evolution of human seaso...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2012-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3280219?pdf=render |
| _version_ | 1818989987722428416 |
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| author | Shisheng Sun Qinzhe Wang Fei Zhao Wentian Chen Zheng Li |
| author_facet | Shisheng Sun Qinzhe Wang Fei Zhao Wentian Chen Zheng Li |
| author_sort | Shisheng Sun |
| collection | DOAJ |
| description | Protein glycosylation alteration is typically employed by various viruses for escaping immune pressures from their hosts. Our previous work had shown that not only the increase of glycosylation sites (glycosites) numbers, but also glycosite migration might be involved in the evolution of human seasonal influenza H1N1 viruses. More importantly, glycosite migration was likely a more effectively alteration way for the host adaption of human influenza H1N1 viruses. In this study, we provided more bioinformatics and statistic evidences for further predicting the significant biological functions of glycosite migration in the host adaptation of human influenza H1N1 viruses, by employing homology modeling and in silico protein glycosylation of representative HA and NA proteins as well as amino acid variability analysis at antigenic sites of HA and NA. The results showed that glycosite migrations in human influenza viruses have at least five possible functions: to more effectively mask the antigenic sites, to more effectively protect the enzymatic cleavage sites of neuraminidase (NA), to stabilize the polymeric structures, to regulate the receptor binding and catalytic activities and to balance the binding activity of hemagglutinin (HA) with the release activity of NA. The information here can provide some constructive suggestions for the function research related to protein glycosylation of influenza viruses, although these predictions still need to be supported by experimental data. |
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| format | Article |
| id | doaj.art-946c038984444cd182eca4272004b2f9 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-20T19:47:13Z |
| publishDate | 2012-01-01 |
| publisher | Public Library of Science (PLoS) |
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| series | PLoS ONE |
| spelling | doaj.art-946c038984444cd182eca4272004b2f92022-12-21T19:28:24ZengPublic Library of Science (PLoS)PLoS ONE1932-62032012-01-0172e3211910.1371/journal.pone.0032119Prediction of biological functions on glycosylation site migrations in human influenza H1N1 viruses.Shisheng SunQinzhe WangFei ZhaoWentian ChenZheng LiProtein glycosylation alteration is typically employed by various viruses for escaping immune pressures from their hosts. Our previous work had shown that not only the increase of glycosylation sites (glycosites) numbers, but also glycosite migration might be involved in the evolution of human seasonal influenza H1N1 viruses. More importantly, glycosite migration was likely a more effectively alteration way for the host adaption of human influenza H1N1 viruses. In this study, we provided more bioinformatics and statistic evidences for further predicting the significant biological functions of glycosite migration in the host adaptation of human influenza H1N1 viruses, by employing homology modeling and in silico protein glycosylation of representative HA and NA proteins as well as amino acid variability analysis at antigenic sites of HA and NA. The results showed that glycosite migrations in human influenza viruses have at least five possible functions: to more effectively mask the antigenic sites, to more effectively protect the enzymatic cleavage sites of neuraminidase (NA), to stabilize the polymeric structures, to regulate the receptor binding and catalytic activities and to balance the binding activity of hemagglutinin (HA) with the release activity of NA. The information here can provide some constructive suggestions for the function research related to protein glycosylation of influenza viruses, although these predictions still need to be supported by experimental data.http://europepmc.org/articles/PMC3280219?pdf=render |
| spellingShingle | Shisheng Sun Qinzhe Wang Fei Zhao Wentian Chen Zheng Li Prediction of biological functions on glycosylation site migrations in human influenza H1N1 viruses. PLoS ONE |
| title | Prediction of biological functions on glycosylation site migrations in human influenza H1N1 viruses. |
| title_full | Prediction of biological functions on glycosylation site migrations in human influenza H1N1 viruses. |
| title_fullStr | Prediction of biological functions on glycosylation site migrations in human influenza H1N1 viruses. |
| title_full_unstemmed | Prediction of biological functions on glycosylation site migrations in human influenza H1N1 viruses. |
| title_short | Prediction of biological functions on glycosylation site migrations in human influenza H1N1 viruses. |
| title_sort | prediction of biological functions on glycosylation site migrations in human influenza h1n1 viruses |
| url | http://europepmc.org/articles/PMC3280219?pdf=render |
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