Marine-Derived Sulfated Glycans Inhibit the Interaction of Heparin with Adhesion Proteins of IMycoplasma pneumoniae/I

Mycoplasma pneumoniae , a notable pathogen behind respiratory infections, employs specialized proteins to adhere to the respiratory epithelium, an essential process for initiating infection. The role of glycosaminoglycans, especially heparan sulfate, is critical in facilitating pathogen–host interac...

Full description

Saved in:
Bibliographic Details
Published in:Marine drugs 2024-05, Vol.22 (5)
Main Authors: Yang, Jiyuan, Song, Yuefan, Xia, Ke, Pomin, Vitor H, Wang, Chunyu, Qiao, Mingqiang, Linhardt, Robert J, Dordick, Jonathan S, Zhang, Fuming
Format: Article
Language:English
Subjects:
Bacterial infections
Composition
Control
Genetic aspects
Health aspects
Heparin
Identification and classification
Mycoplasma pneumoniae
Polysaccharides
Prevention
Production processes
Risk factors
Sulfates
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Mycoplasma pneumoniae , a notable pathogen behind respiratory infections, employs specialized proteins to adhere to the respiratory epithelium, an essential process for initiating infection. The role of glycosaminoglycans, especially heparan sulfate, is critical in facilitating pathogen–host interactions, presenting a strategic target for therapeutic intervention. In this study, we assembled a glycan library comprising heparin, its oligosaccharide derivatives, and a variety of marine-derived sulfated glycans to screen the potential inhibitors for the pathogen–host interactions. By using Surface Plasmon Resonance spectroscopy, we evaluated the library’s efficacy in inhibiting the interaction between M. pneumoniae adhesion proteins and heparin. Our findings offer a promising avenue for developing novel therapeutic strategies against M. pneumoniae infections.
ISSN:1660-3397
1660-3397
DOI:10.3390/md22050232