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Review
. 2019 Jul 1;11(7):596.
doi: 10.3390/v11070596.

Heparan Sulfate Proteoglycans and Viral Attachment: True Receptors or Adaptation Bias?

Valeria Cagno  1 , Eirini D Tseligka  2 , Samuel T Jones  3 , Caroline Tapparel  2
Affiliations
Review

Heparan Sulfate Proteoglycans and Viral Attachment: True Receptors or Adaptation Bias?

Valeria Cagno et al. Viruses. .

Abstract

Heparan sulfate proteoglycans (HSPG) are composed of unbranched, negatively charged heparan sulfate (HS) polysaccharides attached to a variety of cell surface or extracellular matrix proteins. Widely expressed, they mediate many biological activities, including angiogenesis, blood coagulation, developmental processes, and cell homeostasis. HSPG are highly sulfated and broadly used by a range of pathogens, especially viruses, to attach to the cell surface.

Keywords: viral attachment receptor, heparan sulfate proteoglycans, HSPG, syndecans, glypicans, viral adaptation, intra-host adaptation, tropism, broad-spectrum antivirals, viral binding.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Schematic structure of syndecans and glypicans, the two HSPG chiefly involved in virus infection. HSPG typically consist of a core protein and GAG chains. The core protein of syndecans is composed of an extracellular domain, a single transmembrane domain, and a short cytoplasmic domain that interacts with the cytoskeleton. Glypicans are GPI-anchored HSPG. The GAG chain is composed of unbranched anionic polysaccharides composed of repeating disaccharide units formed by sulfated uronic acid and hexosamine residues.
Figure 2
Figure 2
HS synthesis pathway. The glycans are attached to the protein core through a serine linker. After the addition of different sugars, O- and N-sulfotransferases further modify the side chain conferring the negative charges.
Figure 3
Figure 3
Functions of HSPG. HSPG in the ECM contribute to basement membrane organization. HSPG expressed on the cells mediate interactions with extracellular factors, play a role in endocytosis and lysosomal degradation and transcellular transport, and can be shed in response to stress after proteolytic cleavage. Adapted with permission from [7].
See this image and copyright information in PMC

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