The Core-Trisaccharide Hemagglutinin as a Protein Vaccine against Influenza Virus Infection
Date Issued
2011
Date
2011
Author(s)
Wang, Ting-Yun
Abstract
Influenza pandemics occur when influenza hemagglutinins (HA) are little recognized by immunity and the viruses transmit efficiently from human to human. HA is the major viral surface glycoprotein that binds to specific sialylated glycan receptors in the respiratory tract and allows the virus to enter the cell. It has been recognized as the key antigen in the host immune response to influenza virus in both natural infection and vaccination. The glycans of HA have been shown to be important for protein folding and receptor binding. Glycans can also mask important epitopes of protein so that the host may not produce effective antibodies to defeat the viruses. Previous study has showed that the core trisaccharide of an N-linked glycoprotein intrinsically accelerates folding and enhances stability. It means that the core triose of N-linked glycans has a general structure stabilizing effect. Here, we demonstrate that the core-trisaccharide HA (HAtg) could be a better protein vaccine than other HA glycoforms. Our analysis showed that the N-glycan of HAtg proteins were mostly two N-acetylglucosamines (GlcNAc) and one mannose (Man), and the molecular weight of HAtg was as expected. Furthermore, the secondary structure of HAtg is similar to HA with different glycosylations although it is in an aggregated form. The immunogenicity of HAtg was lower than the monoglycosylated HA (HAmg), but superior than the fullyglycosylated HA (HAfg). This study provides new insight into the vaccine design of HA glycoproteins against influenza.
Subjects
Influenza virus
Hemagglutinin
Glycoprotein
Sialic acid
Endocytosis
SDGs
Type
thesis
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