In isolated primary immunoglobulin M deficiency, there’s a decrease in the number of IgM antibodies in the blood, while the levels of other types of antibodies remain normal.
Let’s take a look at how B cells end up secreting different types of antibodies.
Each B cell is born in the bone marrow from a stem cell and develops its own B cell receptor, which sits on the cell surface.
The B cell receptor consists of two parts - a protein called CD79 that communicates with the rest of the cell and a membrane bound IgM or IgD antibody that can bind to an antigen.
An antigen is any substance recognized by that particular antibody.
Each antibody has two identical light chains and two identical heavy chains that combine into a Y shape.
So this Y-shaped antibody’s got two arms with identical tips, which is called the variable region.
This variable region contains an antigen binding domain that’s unique to that antibody.
Below the variable region, or toward the point where the arms meet, is the constant region where every member of an antibody class is identical – so all IgM antibodies have the same constant regions, but IgM and IgA constant regions are different.
And there are five classes of antibodies in total: IgM, IgG, IgA, IgE, and IgD class antibodies, and each one has a slightly different job.
For example, IgMs are part of B cell receptors, and are the first free-floating antibodies produced in an immune response.
They’re secreted as a pentamer, meaning there are five antibodies connected together, which provides many binding sites for grabbing antigens and taking them out of the blood.
Each antibody has complement protein binding sites on the heavy chains, so these IgM pentamers are also great at activating complement proteins, which help destroy and remove pathogens.