ABSTRACT
Neutrophils play as major phagocytes that participate in the various effector phase of immunity. Mannosebinding lectin (MBL) assisted priming of neutrophils could trigger various processes including modulationof endocytosis rate, reactive oxygen production, chemotaxis, etc., through interactions with cell surfacereceptors. The physiological receptor for MBL on neutrophil's surface is still unreported. Macromoleculardocking could be attempted to determine the protein-protein interactions which are important forunderstanding cellular function and organization. The study was performed to identify the interacting partnerof MBL present on neutrophils surface which leads to the activation of various cell processes. Protein networkanalysis, homology modeling, and Rigid docking were performed to explore structural features and bindingmechanism of MBL with its cellular receptors. The results indicates that CR1 interact with the MBL and mayact as MBL receptor.