author(s)
Mangalam P, Balasubramaniyan R and Vasuki V

abstract
Enolase is one of the most abundantly expressed cytosolic proteins in many organisms. It is a key glycolytic metalloenzyme found from archaebacteria to mammals and its sequence is highly conserved. Enolase, a multifunctional protein, exhibits diversity in its location as well as in function. Besides its function in glycolysis and gluconeogenesis, it also serves as a surface protein and surface receptor for the binding of plasminogen on the surface of the variety of haematopoetic, epithelial and endothelial cells for the invasion of pathogens. Enolase is transported to the cell surface through an unknown mechanism. It efficiently binds with plasminogen and converts it to a serine protease, plasmin that helps to degrade the fibrin matrix together with other extracellular matrix surrounding the targeted host cell for the invasion of pathogen. Presence of enolase and its key role in the metabolism and in the pathogen invasion process in many of the vector-borne pathogens from arboviral to nematode pathogens are being recognised recently. The location and possible function of enolase and its importance as therapeutic target in vector-borne pathogens are discussed.