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Publications (3 of 3) Show all publications
Zemła, J., Abidine, Y. & Verdier, C. (2023). Microrheology. In: Malgorzata Lekka; Daniel Navajas; Manfred Radmacher; Alessandro Podestà (Ed.), Mechanics of cells and tissues in diseases: Biomedical methods. Volume 1 (pp. 199-216). Walter de Gruyter
Open this publication in new window or tab >>Microrheology
2023 (English)In: Mechanics of cells and tissues in diseases: Biomedical methods. Volume 1 / [ed] Malgorzata Lekka; Daniel Navajas; Manfred Radmacher; Alessandro Podestà, Walter de Gruyter, 2023, p. 199-216Chapter in book (Refereed)
Place, publisher, year, edition, pages
Walter de Gruyter, 2023
National Category
Microbiology in the medical area
Identifiers
urn:nbn:se:umu:diva-206962 (URN)10.1515/9783110640632-012 (DOI)2-s2.0-85152348865 (Scopus ID)9783110640632 (ISBN)9783110640595 (ISBN)9783110640687 (ISBN)
Available from: 2023-04-26 Created: 2023-04-26 Last updated: 2023-08-29Bibliographically approved
Abidine, Y., Liu, L., Wallén, O., Trybala, E., Olofsson, S., Bergström, T. & Bally, M. (2022). Cellular Chondroitin Sulfate and the Mucin-like Domain of Viral Glycoprotein C Promote Diffusion of Herpes Simplex Virus 1 While Heparan Sulfate Restricts Mobility. Viruses, 14(8), Article ID 1836.
Open this publication in new window or tab >>Cellular Chondroitin Sulfate and the Mucin-like Domain of Viral Glycoprotein C Promote Diffusion of Herpes Simplex Virus 1 While Heparan Sulfate Restricts Mobility
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2022 (English)In: Viruses, E-ISSN 1999-4915, Vol. 14, no 8, article id 1836Article in journal (Refereed) Published
Abstract [en]

The diffusion of viruses at the cell membrane is essential to reach a suitable entry site and initiate subsequent internalization. Although many viruses take advantage of glycosaminoglycans (GAG) to bind to the cell surface, little is known about the dynamics of the virus–GAG interactions. Here, single-particle tracking of the initial interaction of individual herpes simplex virus 1 (HSV-1) virions reveals a heterogeneous diffusive behavior, regulated by cell-surface GAGs with two main diffusion types: confined and normal free. This study reports that different GAGs can have competing influences in mediating diffusion on the cells used here: chondroitin sulfate (CS) enhances free diffusion but hinders virus attachment to cell surfaces, while heparan sulfate (HS) promotes virus confinement and increases entry efficiency. In addition, the role that the viral mucin-like domains (MLD) of the HSV-1 glycoprotein C plays in facilitating the diffusion of the virus and accelerating virus penetration into cells is demonstrated. Together, our results shed new light on the mechanisms of GAG-regulated virus diffusion at the cell surface for optimal internalization. These findings may be extendable to other GAG-binding viruses.

Place, publisher, year, edition, pages
MDPI, 2022
Keywords
glycocalyx, glycocalyx, glycosaminoglycan, herpesvirus, mucin-like domain, single particle tracking, viral O-glycans, virus diffusion
National Category
Cell and Molecular Biology Biophysics
Identifiers
urn:nbn:se:umu:diva-199466 (URN)10.3390/v14081836 (DOI)000845137500001 ()36016458 (PubMedID)2-s2.0-85137388191 (Scopus ID)
Funder
Wenner-Gren Foundations, UPD2018-0193Knut and Alice Wallenberg FoundationSwedish Research Council, 2017-04029
Available from: 2022-09-26 Created: 2022-09-26 Last updated: 2024-01-17Bibliographically approved
Kirui, J., Abidine, Y., Lenman, A., Islam, M. K. K., Yong-Dae, G., Lasswitz, L., . . . Gerold, G. (2021). The Phosphatidylserine Receptor TIM-1 Enhances Authentic Chikungunya Virus Cell Entry. Cells, 10(7), Article ID 1828.
Open this publication in new window or tab >>The Phosphatidylserine Receptor TIM-1 Enhances Authentic Chikungunya Virus Cell Entry
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2021 (English)In: Cells, E-ISSN 2073-4409, Vol. 10, no 7, article id 1828Article in journal (Refereed) Published
Abstract [en]

Chikungunya virus (CHIKV) is a re-emerging, mosquito-transmitted, enveloped positive stranded RNA virus. Chikungunya fever is characterized by acute and chronic debilitating arthritis. Although multiple host factors have been shown to enhance CHIKV infection, the molecular mechanisms of cell entry and entry factors remain poorly understood. The phosphatidylserine-dependent receptors, T-cell immunoglobulin and mucin domain 1 (TIM-1) and Axl receptor tyrosine kinase (Axl), are transmembrane proteins that can serve as entry factors for enveloped viruses. Previous studies used pseudoviruses to delineate the role of TIM-1 and Axl in CHIKV entry. Conversely, here, we use the authentic CHIKV and cells ectopically expressing TIM-1 or Axl and demonstrate a role for TIM-1 in CHIKV infection. To further characterize TIM-1-dependent CHIKV infection, we generated cells expressing domain mutants of TIM-1. We show that point mutations in the phosphatidylserine binding site of TIM-1 lead to reduced cell binding, entry, and infection of CHIKV. Ectopic expression of TIM-1 renders immortalized keratinocytes permissive to CHIKV, whereas silencing of endogenously expressed TIM-1 in human hepatoma cells reduces CHIKV infection. Altogether, our findings indicate that, unlike Axl, TIM-1 readily promotes the productive entry of authentic CHIKV into target cells.

Place, publisher, year, edition, pages
MDPI, 2021
Keywords
Chikungunya virus, CHIKV, alphavirus, enveloped virus, phosphatidylserine, T-cell immunoglobulin and mucin domain 1, TIM-1, Axl receptor tyrosine kinase, Axl, entry
National Category
Microbiology in the medical area
Identifiers
urn:nbn:se:umu:diva-187299 (URN)10.3390/cells10071828 (DOI)000676394100001 ()34359995 (PubMedID)2-s2.0-85114081934 (Scopus ID)
Funder
Knut and Alice Wallenberg FoundationSwedish Research Council, 2017-05607
Available from: 2021-09-09 Created: 2021-09-09 Last updated: 2021-09-09Bibliographically approved
Organisations
Identifiers
ORCID iD: ORCID iD iconorcid.org/0000-0002-1612-7247

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