Host Defense Proteins and Peptides with Lipopolysaccharide-Binding Activity from Marine Invertebrates and their Therapeutic Potential in Gram-Negative Sepsis
Preprint
- 26 September 2023
- preprint
- Published by MDPI AG in Preprints.org
Abstract
Sepsis is a life-threatening complication of an infectious process that results from excessive and uncontrolled activation of the host's pro-inflammatory immune response to a pathogen. Lipopolysaccharide (LPS), also known as endotoxin, which is a major component of the Gram-negative bacteria outer membrane, plays a key role in the development of Gram-negative sepsis and septic shock in humans. To date, no specific and effective drug against sepsis has been developed. This review summarizes data on LPS-binding proteins from marine invertebrates (ILBPs), that inhibit LPS toxic effects, and are of interest as potential drugs for the sepsis treatment. The structure, physicochemical properties, antimicrobial and LPS-binding/neutralizing activity of these proteins and their synthetic analogues are considered in details. Problems that arise during clinical trials of potential anti-endotoxic drugs are discussed.Keywords
All Related Versions
This publication has 148 references indexed in Scilit:
- The Anti-lipopolysaccharide Factors in Crustaceans2020
- Cationic Antimicrobial Peptides in Penaeid ShrimpMarine Biotechnology, 2011
- NMR structure of rALF‐Pm3, an anti‐lipopolysaccharide factor from shrimp: Model of the possible lipid A‐binding siteBiopolymers, 2008
- Molecular insight into mechanism of antimicrobial action of the β‐hairpin peptide arenicin: Specific oligomerization in detergent micellesBiopolymers, 2007
- Molecular Cloning and Expression Profile of Putative Antilipopolysaccharide factor in Chinese Shrimp(Fenneropenaeus chinensis)Marine Biotechnology, 2005
- The 1.7 Å crystal structure of BPI: a study of how two dissimilar amino acid sequences can adopt the same fold 1 1Edited by D. ReesJournal of Molecular Biology, 2000
- The BPI/LBP family of proteins: A structural analysis of conserved regionsProtein Science, 1998
- Expression and Characterization of Cysteine-Modified Variants of an Amino-Terminal Fragment of Bactericidal/Permeability-Increasing ProteinProtein Expression and Purification, 1996
- Crystal structure of an endotoxin‐neutralizing protein from the horseshoe crab, Limulus anti‐LPS factor, at 1.5 A resolution.The EMBO Journal, 1993
- anti-LPS factor: An anticoagulant which inhibits the endotoxin-mediated activation of coagulation systemBiochemical and Biophysical Research Communications, 1982