page_title: Myristoylation
section_title: Viral infectivity
hierarchical_section_title: Myristoylation / Impact on human health / Viral infectivity
caption_attribution_description: English: HIV utilizes myristoylation on the Matrix protein in order to target the viral proteins and viral genome to the membrane for budding and viral maturation.
context_page_description: Myristoylation is a lipidation modification where a myristoyl group, derived from myristic acid, is covalently attached by an amide bond to the alpha-amino group of an N-terminal glycine residue. Myristic acid is a 14-carbon saturated fatty acid with the systematic name of n-Tetradecanoic acid. This modification can be added either co-translationally or post-translationally. N-myristoyltransferase catalyzes the myristic acid addition reaction in the cytoplasm of cells. This lipidation event is the most found type of fatty acylation and is common among many organisms including animals, plants, fungi, protozoans and viruses. Myristoylation allows for weak protein–protein and protein–lipid interactions and plays an essential role in membrane targeting, protein–protein interactions and functions widely in a variety of signal transduction pathways.
context_section_description: HIV-1 is a retrovirus that relies on myristoylation of one of its structural proteins in order to successfully package its genome, assemble and mature into a new infectious particle. Viral matrix protein, the N-terminal most domain of the gag polyprotein is myristoylated. This myristoylation modification targets gag to the membrane of the host cell. Utilizing the myristoyl-electrostatic switch, including a basic patch on the matrix protein, gag can assemble at lipid rafts at the plasma membrane for viral assembly, budding and further maturation.  In order to prevent viral infectivity, myristoylation of the matrix protein could become a good drug target.
caption: HIV-1 utilizes myristoylation on the Matrix protein to target the viral proteins and viral genome to the membrane for budding and viral maturation.
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