ABSTRACT
Scavenger receptors of macrophages represent a trimeric integral membrane glycoproteins implicated in the pathogenesis of atherosclerosis (1,2), apoptosis or programmed cell death, and host defense against microbial pathogens or their toxic products. The cloning and characterization of molecular structure of scavenger receptor type I and type II class A showed that it consists of six specific domains, which are well conserved among different species. However, only scavenger receptor class A was found to date to interact specifically with microbial components of both gram-positive and gram-negative bacteria. In contrast, the collagen-like domain V of scavenger receptor consists of a number of glycine-X-Y triplet repeats frequently containing prolines and lysines in positions X and Y, which may well be positively charged at physiological pH and be involved in specific interaction of scavenger receptor with polyanionic li gands.
