Репозиторий Университета

© 2018 Russian Academy of Sciences. All rights reserved. The current theoretical and experimental data about the impact of the lipid A structure on interactions of lipopolysaccharide (LPS) with serum lipid-binding protein (LBP) are presented. LBP interacts more efficiently with the LPS lipid A from Rhizobium, Escherichia, and Neisseria spp. than with the LPS lipid from Francisella, Porphyromonas, Helicobacter, Chlamydophila, as well as with the lipid A synthetic analogue-compound E5564. It is shown that the lipid A hydrocarbon chain of 14 carbon atoms is most favorable, while that of 16 carbon atoms is ultimate for interaction of LBP with lipid A. A high content of unusually long chains and branched-chain acyl residues in lipid A will further complicate the interaction of LBP with LPS. The reviewed data provide a deeper insight into the mechanisms of the LPS delivery and cell activation accomplished by serum cationic proteins such as LBP. A direct relation between the efficiency of the LBP interaction with a particular lipid A of LPS and the development of the fulminant acute inflammation is proposed.