Protein prenylation: A new mode of host–pathogen interaction

Post translational modifications are required for proteins to be fully functional. The three step process, prenylation, leads to farnesylation or geranylgeranylation, which increase the hydrophobicity of the prenylated protein for efficient anchoring into plasma membranes and/or organellar membranes. Prenylated proteins function in a number of signaling and regulatory pathways that are responsible for basic cell operations. Well characterized prenylated proteins include Ras, Rac and Rho. Recently, pathogenic prokaryotic proteins, such as SifA and AnkB, have been shown to be prenylated by eukaryotic host cell machinery, but their functions remain elusive. The identification of other bacterial proteins undergoing this type of host-directed post-translational modification shows promise in elucidating host–pathogen interactions to develop new therapeutics. This review incorporates new advances in the study of protein prenylation into a broader aspect of biology with a focus on host–pathogen interaction.

► Well characterized prenylated proteins are vital to signaling pathways.
► PrePS predicts prenylation states of protein sequences harboring CAAX motifs.
► Eukaryotic prenylated proteins are implicated in multiple diseases and cancers.
► Pathogenic bacterial effector proteins, AnkB and SifA have been shown to be prenylated.
► Prenylation inhibition therapeutics directed towards host and pathogen are under development.