<i>N</i>-Glycan Profiles of Neuraminidase from Avian Influenza Viruses
Wentian Chen,
Tianran Ma,
Sinuo Liu,
Yaogang Zhong,
Hanjie Yu,
Jian Shu,
Xiurong Wang,
Zheng Li
Affiliations
Wentian Chen
Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi’an 710069, China
Tianran Ma
Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi’an 710069, China
Sinuo Liu
Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi’an 710069, China
Yaogang Zhong
Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi’an 710069, China
Hanjie Yu
Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi’an 710069, China
Jian Shu
Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi’an 710069, China
Xiurong Wang
National Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Science, Harbin 150001, China
Zheng Li
Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi’an 710069, China
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 p-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 N-glycans of isolated NAs. We found that more than 20 N-glycans were identified, and 16 glycan peaks were identical in the strains derived from chicken embryo cultivation. Multi-antennae, bisected, or core-fucosylated N-glycans are common in all the NAs. The terminal residues of N-glycans are predominantly composed of galactose and N-acetylglucosamine residues. Meanwhile, sialic acid residue was uncommon in these N-glycans. Further computational docking analysis predicted the interaction mechanism between NA and p-aminophenyloxamic acid.
