Molecular Inhibition of Phagocytosis: Systematic Review of Immune Response

Abstract

There are many viral variants that bind to sialic acid rather than cleave it on a human macrophage, which inhibits a macrophage’s phagocytosis; for example, the D151G mutant of the influenza virus. Sialic acid must be cleaved in order to initiate phagocytosis, so viral variants that cleave sialic acid can help hasten the cleansing process of the immune system. The process of researching began with the understanding of how sialic acid synthesis occurs and how it inhibits phagocytosis. Next is the understanding of how the enzyme Neuraminidase-1 works in a human macrophage. The function of Neuraminidase-1 is to cleave sialic acid allowing for phagocytosis to occur. Next is the analysis of the molecule 12-O-tetradecanoylphorbol-13-acetate which is able to cause more Neuraminidase-1 to be produced and sent to the surface of human macrophages to cleave sialic acid. It has the potential of being used as a drug to stimulate Neuraminidase-1 production and specific activity, so sialic acid can be cleaved therefore the macrophage is able to phagocytize the virus. In vitro results show us that it is able to happen; however, this has not been tested in vivo which shows that the results obtained do not account for the biological factors that occur in the human bodies. 12-O-tetradecanoylphorbol-13-acetate has the potential to be used as a drug to speed up the breakdown of viruses that bind to sialic acid, but more research needs to be made with much progress being made.