IL2

The major histocompatibility complex (MHC) is responsible for binding peptide fragments arising from pathogens in order to display them on the cell surface for recognition from immune cells.  Once recognized, the foreign pathogen is typically evaded. The MHC complex is broken into two categories, MHC Class I proteins and MHC Class II proteins.  MHC complex I and II proteins are all very different and contain specific molecules to bind different peptides – in fact, they have been described as the most polymorphic genes there are.

Integrins are transmembrane receptors composed of alpha and beta chains, where beta-integrins are mainly expressed in leukocytes. Leukocytes are white blood cells that act in the immune system to defend our body against foreign pathogens.

Transferrin, an iron binding protein that facilitates iron uptake in cells, is an integral part of a mechanism that may introduce antibody therapies to the central nervous system. Currently, the brain’s ability to take in antibody therapies is limited by the presence of the blood brain barrier.

MHC molecules (also known as major histocompatibility complex molecules) assist in the presentation of antigens to T cells in order to eradicate foreign pathogens.  These molecules are highly polymorphic, meaning that they exist in multiple variants in order to avoid pathogens evading their activation of the immune response.  MHC Class I molecules in particular deliver cytosolic peptides to the cell surface so that they can continue on through the cytosol and ultimately the endoplasmic reticulum (ER).

Our immune system is a powerful defense mechanism against infection, however different variables can cause our immune response to work for or against us.  CD3 (cluster of differentiation 3) is one component of our immune signal response that is composed of four distinct chains (CD3-g, CD3-e, CD3-s and the zeta chain). These chains associate with a molecule known as the T-cell receptor (TCR) to comprise the TCR complex.