Effects of Sialic Acid Modifications on Virus Binding and Infection. Issue 12 (December 2016)

• Record Type: Journal Article
• Authors: Wasik, Brian R.; Barnard, Karen N.; Parrish, Colin R.
• Is Part Of: Trends in microbiology. Volume 24:Issue 12(2016)
• Page Start: 991
• Page End: 1001
• Publication Date: 2016-12
• Subjects: virus -- sialic acids -- modification -- receptor -- inhibitor.; Microbiology -- Periodicals; Infection -- Periodicals; Virulence (Microbiology) -- Periodicals; Infection -- Periodicals; Microbiology -- Periodicals; Virulence -- Periodicals; Microbiologie -- Périodiques; Infection -- Périodiques; Virulence (Microbiologie) -- Périodiques; Infection; Microbiology; Virulence (Microbiology); 579
• DOI: 10.1016/j.tim.2016.07.005
• Languages: English
• ISSNs: 0966-842X

Abstract

Abstract : Sialic acids (Sias) are abundantly displayed on the surfaces of vertebrate cells, and particularly on all mucosal surfaces. Sias interact with microbes of many types, and are the targets of specific recognition by many different viruses. They may mediate virus binding and infection of cells, or alternatively can act as decoy receptors that bind virions and block virus infection. These nine-carbon backbone monosaccharides naturally occur in many different modified forms, and are attached to underlying glycans through varied linkages, creating significant diversity in the pathogen receptor forms. Here we review the current knowledge regarding the distribution of modified Sias in different vertebrate hosts, tissues, and cells, their effects on viral pathogens where those have been examined, and outline unresolved questions. Trends: Sialic acids (Sias) are components of cell-surface glycoproteins and glycolipids, as well as secreted glycoproteins and milk oligosaccharides. Sias play important roles in cell signaling, development, and host–pathogen interactions. Cellular enzymes can modify Sias, yet how modifications vary between tissues and hosts has not been fully elucidated. Many viruses use Sias as receptors, with different modifications aiding or inhibiting virus infection. How modified Sias influence viral protein evolution and determine host/tissue tropism are poorly understood, and are important areas of research. New advances in molecular glycobiology using pathogen proteins to detect varied forms allows for improved study of modified Sias that have otherwise proven difficult to isolate. This opens new avenues of inquiry for virology, as well as host interactions with bacterial and eukaryotic pathogens.