<i>N</i>-Glycan Profiles of Neuraminidase from Avian Influenza Viruses
The cleavage of sialic acids by neuraminidase (NA) facilitates the spread of influenza A virus (IV) descendants. Understanding the enzymatic activity of NA aids research into the transmission of IVs. An effective method for purifying NA was developed using <i>p</i>-aminophenyloxamic acid...
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MDPI AG
2024-01-01
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| Series: | Viruses |
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| Online Access: | https://www.mdpi.com/1999-4915/16/2/190 |
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| author | Wentian Chen Tianran Ma Sinuo Liu Yaogang Zhong Hanjie Yu Jian Shu Xiurong Wang Zheng Li |
| author_facet | Wentian Chen Tianran Ma Sinuo Liu Yaogang Zhong Hanjie Yu Jian Shu Xiurong Wang Zheng Li |
| author_sort | Wentian Chen |
| collection | DOAJ |
| description | The cleavage of sialic acids by neuraminidase (NA) facilitates the spread of influenza A virus (IV) descendants. Understanding the enzymatic activity of NA aids research into the transmission of IVs. An effective method for purifying NA was developed using <i>p</i>-aminophenyloxamic acid-modified functionalized hydroxylated magnetic particles (AAMPs), and from 0.299 to 0.401 mg of NA from eight IV strains was isolated by 1 mg AAMP. A combination of lectin microarrays and MALDI-TOF/TOF-MS was employed to investigate the <i>N</i>-glycans of isolated NAs. We found that more than 20 <i>N</i>-glycans were identified, and 16 glycan peaks were identical in the strains derived from chicken embryo cultivation. Multi-antennae, bisected, or core-fucosylated <i>N</i>-glycans are common in all the NAs. The terminal residues of <i>N</i>-glycans are predominantly composed of galactose and <i>N</i>-acetylglucosamine residues. Meanwhile, sialic acid residue was uncommon in these <i>N</i>-glycans. Further computational docking analysis predicted the interaction mechanism between NA and <i>p</i>-aminophenyloxamic acid. |
| first_indexed | 2024-03-07T22:11:32Z |
| format | Article |
| id | doaj.art-e8af61fba0194bcea78784fa316b3015 |
| institution | Directory Open Access Journal |
| issn | 1999-4915 |
| language | English |
| last_indexed | 2024-03-07T22:11:32Z |
| publishDate | 2024-01-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Viruses |
| spelling | doaj.art-e8af61fba0194bcea78784fa316b30152024-02-23T15:37:26ZengMDPI AGViruses1999-49152024-01-0116219010.3390/v16020190<i>N</i>-Glycan Profiles of Neuraminidase from Avian Influenza VirusesWentian Chen0Tianran Ma1Sinuo Liu2Yaogang Zhong3Hanjie Yu4Jian Shu5Xiurong Wang6Zheng Li7Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi’an 710069, ChinaLaboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi’an 710069, ChinaLaboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi’an 710069, ChinaLaboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi’an 710069, ChinaLaboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi’an 710069, ChinaLaboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi’an 710069, ChinaNational Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Science, Harbin 150001, ChinaLaboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi’an 710069, ChinaThe cleavage of sialic acids by neuraminidase (NA) facilitates the spread of influenza A virus (IV) descendants. Understanding the enzymatic activity of NA aids research into the transmission of IVs. An effective method for purifying NA was developed using <i>p</i>-aminophenyloxamic acid-modified functionalized hydroxylated magnetic particles (AAMPs), and from 0.299 to 0.401 mg of NA from eight IV strains was isolated by 1 mg AAMP. A combination of lectin microarrays and MALDI-TOF/TOF-MS was employed to investigate the <i>N</i>-glycans of isolated NAs. We found that more than 20 <i>N</i>-glycans were identified, and 16 glycan peaks were identical in the strains derived from chicken embryo cultivation. Multi-antennae, bisected, or core-fucosylated <i>N</i>-glycans are common in all the NAs. The terminal residues of <i>N</i>-glycans are predominantly composed of galactose and <i>N</i>-acetylglucosamine residues. Meanwhile, sialic acid residue was uncommon in these <i>N</i>-glycans. Further computational docking analysis predicted the interaction mechanism between NA and <i>p</i>-aminophenyloxamic acid.https://www.mdpi.com/1999-4915/16/2/190avian influenza virusneuraminidase<i>N</i>-glycan profileslecin microarraysMALDI-TOF/TOF-MS |
| spellingShingle | Wentian Chen Tianran Ma Sinuo Liu Yaogang Zhong Hanjie Yu Jian Shu Xiurong Wang Zheng Li <i>N</i>-Glycan Profiles of Neuraminidase from Avian Influenza Viruses Viruses avian influenza virus neuraminidase <i>N</i>-glycan profiles lecin microarrays MALDI-TOF/TOF-MS |
| title | <i>N</i>-Glycan Profiles of Neuraminidase from Avian Influenza Viruses |
| title_full | <i>N</i>-Glycan Profiles of Neuraminidase from Avian Influenza Viruses |
| title_fullStr | <i>N</i>-Glycan Profiles of Neuraminidase from Avian Influenza Viruses |
| title_full_unstemmed | <i>N</i>-Glycan Profiles of Neuraminidase from Avian Influenza Viruses |
| title_short | <i>N</i>-Glycan Profiles of Neuraminidase from Avian Influenza Viruses |
| title_sort | i n i glycan profiles of neuraminidase from avian influenza viruses |
| topic | avian influenza virus neuraminidase <i>N</i>-glycan profiles lecin microarrays MALDI-TOF/TOF-MS |
| url | https://www.mdpi.com/1999-4915/16/2/190 |
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