Glycosaminoglycans and infection

被引:111
作者
Aquino, Rafael S. [1 ]
Park, Pyong Woo [1 ,2 ]
机构
[1] Harvard Univ, Childrens Hosp, Sch Med, Div Resp Dis, Boston, MA 02115 USA
[2] Harvard Univ, Childrens Hosp, Sch Med, Div Newborn Med, Boston, MA 02115 USA
来源
FRONTIERS IN BIOSCIENCE-LANDMARK | 2016年 / 21卷
关键词
Heparan Sulfate; Heparin; Chondroitin Sulfate; Dermatan Sulfate; Hyaluronan; Keratan Sulfate; Proteoglycan; Syndecan; Microbial Pathogenesis; Host Defense; Virulence Factor; Antimicrobial Peptide; Review; HEPARAN-SULFATE PROTEOGLYCANS; HEPATITIS-C VIRUS; HIV-1 TAT PROTEIN; COLI POLYSACCHARIDE DERIVATIVES; CELL-SURFACE PROTEOGLYCANS; OUTER-MEMBRANE PROTEIN; PLASMODIUM-FALCIPARUM; CHONDROITIN SULFATE; LISTERIA-MONOCYTOGENES; NEISSERIA-GONORRHOEAE;
D O I
10.2741/4455
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Glycosaminoglycans (GAGs) are complex linear polysaccharides expressed in intracellular compartments, at the cell surface, and in the extracellular environment where they interact with various molecules to regulate many cellular processes implicated in health and disease. Subversion of GAGs is a pathogenic strategy shared by a wide variety of microbial pathogens, including viruses, bacteria, parasites, and fungi. Pathogens use GAGs at virtually every major portals of entry to promote their attachment and invasion of host cells, movement from one cell to another, and to protect themselves from immune attack. Pathogens co-opt fundamental activities of GAGs to accomplish these tasks. This ingenious strategy to subvert essential activities of GAGs likely prevented host organisms from deleting or inactivating these mechanisms during their evolution. The goal of this review is to provide a mechanistic overview of our current understanding of how microbes subvert GAGs at major steps of pathogenesis, using select GAG-pathogen interactions as representative examples.
引用
收藏
页码:1260 / 1277
页数:18
相关论文
共 128 条
[41]   Effects of toxin production in a murine model of Staphylococcus aureus keratitis [J].
Girgis, DO ;
Sloop, GD ;
Reed, JM ;
O'Callaghan, RJ .
INVESTIGATIVE OPHTHALMOLOGY & VISUAL SCIENCE, 2005, 46 (06) :2064-2070
[42]   Acidic sphingomyelinase mediates entry of N-gonorrhoeae into nonphagocytic cells [J].
Grassme, H ;
Gulbins, E ;
Brenner, B ;
Ferlinz, K ;
Sandhoff, K ;
Harzer, K ;
Lang, F ;
Meyer, TF .
CELL, 1997, 91 (05) :605-615
[43]   Heparin-Binding Motifs and Biofilm Formation by Candida albicans [J].
Green, Julianne V. ;
Orsborn, Kris I. ;
Zhang, Minlu ;
Tan, Queenie K. G. ;
Greis, Kenneth D. ;
Porollo, Alexey ;
Andes, David R. ;
Lu, Jason Long ;
Hostetter, Margaret K. .
JOURNAL OF INFECTIOUS DISEASES, 2013, 208 (10) :1695-1704
[44]   Risk factors and causative organisms in microbial keratitis [J].
Green, Matthew ;
Apel, Andrew ;
Stapleton, Fiona .
CORNEA, 2008, 27 (01) :22-27
[45]   Decorin-binding adhesins from Borrelia burgdorferi [J].
Guo, BP ;
Brown, EL ;
Dorward, DW ;
Rosenberg, LC ;
Höök, M .
MOLECULAR MICROBIOLOGY, 1998, 30 (04) :711-723
[46]   Heparanase is a host enzyme required for herpes simplex virus-1 release from cells [J].
Hadigal, Satvik R. ;
Agelidis, Alex M. ;
Karasneh, Ghadah A. ;
Antoine, Thessicar E. ;
Yakoub, Abraam M. ;
Ramani, Vishnu C. ;
Djalilian, Ali R. ;
Sanderson, Ralph D. ;
Shukla, Deepak .
NATURE COMMUNICATIONS, 2015, 6
[47]   2-O-Sulfated Domains in Syndecan-1 Heparan Sulfate Inhibit Neutrophil Cathelicidin and Promote Staphylococcus aureus Corneal Infection [J].
Hayashida, Atsuko ;
Amano, Shiro ;
Gallo, Richard L. ;
Linhardt, Robert J. ;
Liu, Jian ;
Park, Pyong Woo .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2015, 290 (26) :16157-16167
[48]   Syndecan-1 Promotes Staphylococcus aureus Corneal Infection by Counteracting Neutrophil-mediated Host Defense [J].
Hayashida, Atsuko ;
Amano, Shiro ;
Park, Pyong Woo .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2011, 286 (05) :3288-3297
[49]   Syndecan-1 is an in vivo suppressor of Gram-positive toxic shock [J].
Hayashida, Kazutaka ;
Chen, Ye ;
Bartlett, Allison H. ;
Park, Pyong Woo .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2008, 283 (29) :19895-19903
[50]   Syndecan-1 shedding facilitates the resolution of neutrophilic inflammation by removing sequestered CXC chemokines [J].
Hayashida, Kazutaka ;
Parks, William C. ;
Park, Pyong Woo .
BLOOD, 2009, 114 (14) :3033-3043