Protein A is a 40-60
kD surface
protein originally found in the cell wall of the
bacteria Staphylococcus aureus. It is encoded by the spa gene and its regulation is controlled by DNA topology, cellular osmolarity, and a two-component system called ArlS-ArlR. It has found use in biochemical research because of its ability to bind
immunoglobulins. It binds proteins from many of mammalian species, most notably IgG’s. It binds with the
Fc region of immunoglobulins through interaction with the heavy chain. The result of this type of interaction is that, in serum, the bacteria will bind IgG molecules in the wrong orientation (in relation to normal
antibody function) on their surface which disrupts
opsonization and
phagocytosis.
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A 42-kDa monomeric protein from Staphylococcus aureus bacteria, protein A lacks cysteine residues and binds to the Fc portion of immunoglobulins. It is used extensively in affinity chromatography; ELISAs; and immunoblotting, -precipitation, and -histochemistry.