March 2012

Deciphering the role of antibody glycosylation in vaccine effectiveness


Immunoglobulin G, or IgG, is a type of an antibody critical to fighting off bacteria and viruses. People get vaccinated to stimulate their bodies to produce IgGs against known pathogens and confer immunity. IgGs are heavily glycosylated, but “we only know very little about how [the glycosylation] is regulated,” says Manfred Wuhrer at Leiden University Medical Center in the Netherlands. In a paper recently published in Molecular & Cellular Proteomics, Wuhrer and colleagues looked at the changes in glycosylation patterns of a subtype of IgG when 10 white European adults and 10 black African children were vaccinated with tetanus and several kinds of influenza. They studied the sugars in the IgG1 subtype by mass spectrometry, which was technically challenging to do, because the method had to be sensitive enough to detect the changes in glycosylation reproducibly and robustly. As Wuhrer explains, the glycosylation changes were observed to be the same in both Africans and Europeans irrespective of age and vaccine type, with an increase in galactose and sialic acid within weeks after vaccination. These data suggested that depending on when the person was vaccinated, the invading pathogen faced IgGs with different glycosylation profiles. This in turn could influence the effectiveness of the IgGs in combating infection. Wuhrer says, “We hope that our paper, together with the body of literature on the functional consequences of IgG glycosylation changes, will stimulate vaccine developers to consider antibody glycosylation as a factor that has to be taken into account in vaccine development.”


Maurice H. J. Selman, et al.; Mol. Cell Proteomics (2011) doi: mcp.M111.014563  

Rajendrani Mukhopadhyay ( is the senior science writer for ASBMB Today and the technical editor for the Journal of Biological Chemistry.

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