Immunoglobulin (Ig)A is one of the dominant antibody classes in our bodies. You would think that we know all about it by now, since antibodies have been studied for more than a century.
Well, that is not true. Amber Rolland, postdoc in the lab, mapped the structure of IgA molecules in the blood in high detail. Separation of the different molecular forms of IgA followed by antibody repertoire analysis showed that many of the clones are present in different forms: both as monomer and as J-chain coupled dimer. Until now, it was widely assumed that these different forms were produced in separate locations by distinct cells. The data Amber generated makes it quite likely that these cells can actually make one IgA clone both with and without J-chain.
Also intrigued? Read the full story here, and a feature on the Utrecht University website here.
