Understanding the interaction of Hsp70 with NK cells

Abstract

AbstractHeat Shock Protein 70 (Hsp70) is a highly conserved and ubiquitous molecular chaperone that plays a central role in cellular protein machinery and stress response. Membrane-bound HSP70 has emerged as an important cancer biomarker and acts as a danger signal and elicits immune response. Hsp70 membrane expression is correlated to increased sensitivity to lysis carried out by NK cells. This study uses computational approaches to decode the interaction of Hsp70 with NK cells and determines the binding site for Hsp70 on the surface of NK cells. Our findings identified CD69 and NKP46 as the most probable binding sites for Hsp70. Additionally, we confirmed the strong binding affinity between Hsp70 and the CD94-NKG2A complex.