Regulatory Mechanisms of the Mucin-Like Region on Herpes Simplex Virus during Cellular Attachment
| Autor: | Marta Bally, Tomas Bergström, Grégoire Le Brun, Edward Trybala, Martin Delguste, Nadia Peerboom, David Alsteens, Sigvard Olofsson |
|---|---|
| Přispěvatelé: | UCL - SST/LIBST - Louvain Institute of Biomolecular Science and Technology |
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
Cell Membrane Permeability Glycosylation Viral protein viruses Plasma protein binding Herpesvirus 1 Human medicine.disease_cause 01 natural sciences Biochemistry Virus Sulfate binding Cell Line Glycosaminoglycan 03 medical and health sciences Viral envelope Viral Envelope Proteins medicine Humans Glycoproteins Glycosaminoglycans chemistry.chemical_classification 010405 organic chemistry Chemistry Cell Membrane Mucins Virion Herpes Simplex General Medicine 0104 chemical sciences Cell biology 030104 developmental biology Herpes simplex virus Mutation Molecular Medicine Mutant Proteins Glycoprotein Protein Binding Signal Transduction |
| Zdroj: | ACS Chemical Biology, Vol. 14, no.3, p. 534-542 (2019) |
| Popis: | Mucin-like regions, characterized by a local high density of O-linked glycosylation, are found on the viral envelope glycoproteins of many viruses. Herpes simplex virus type 1 (HSV-1), for example, exhibits a mucin-like region on its glycoprotein gC, a viral protein involved in initial recruitment of the virus to the cell surface via interaction with sulfated glycosaminoglycans. So far, this mucin-like region has been proposed to play a key role in modulating the interactions with cellular glycosaminoglycans, and in particular to promote release of HSV-1 virions from infected cells. However, the molecular mechanisms and the role as a pathogenicity factor remains unclear. Using single virus particle tracking, we show that the mobility of chondroitin sulfate-bound HSV-1 virions is decreased in absence of the mucin-like region. This decrease in mobility correlates with an increase in HSV-1-chondroitin sulfate binding forces as observed using atomic force microscopy-based force spectroscopy. Our data suggest that the mucin-like region modulates virus-glycosaminoglycan interactions by regulating the affinity, type, and number of glycoproteins involved in the virus-glycosaminoglycan interaction. This study therefore presents new evidence for a role of the mucin-like region in balancing the interaction of HSV-1 with glycosaminoglycans and provides further insights into the molecular mechanisms used by the virus to ensure both successful cell entry and release from the infected cell. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|