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Herpes Simplex Virus Type 2 Mucin-Like Glycoprotein mgG Promotes Virus Release from the Surface of Infected Cells.
Trybala, Edward; Peerboom, Nadia; Adamiak, Beata; Krzyzowska, Malgorzata; Liljeqvist, Jan-Åke; Bally, Marta; Bergström, Tomas.
Afiliação
  • Trybala E; Department of Infectious Diseases, Section for Clinical Virology, Institute of Biomedicine, University of Gothenburg, SE-413 46 Göteborg, Sweden.
  • Peerboom N; Department of Physics, Chalmers University of Technology, SE-412 96 Göteborg, Sweden.
  • Adamiak B; Department of Infectious Diseases, Section for Clinical Virology, Institute of Biomedicine, University of Gothenburg, SE-413 46 Göteborg, Sweden.
  • Krzyzowska M; Department of Infectious Diseases, Section for Clinical Virology, Institute of Biomedicine, University of Gothenburg, SE-413 46 Göteborg, Sweden.
  • Liljeqvist JÅ; Department of Infectious Diseases, Section for Clinical Virology, Institute of Biomedicine, University of Gothenburg, SE-413 46 Göteborg, Sweden.
  • Bally M; Department of Clinical Microbiology, Umeå University, SE-901 85 Umeå, Sweden.
  • Bergström T; Wallenberg Centre for Molecular Medicine, Umeå University, SE-901 85 Umeå, Sweden.
Viruses ; 13(5)2021 05 12.
Article em En | MEDLINE | ID: mdl-34065826
ABSTRACT
The contribution of virus components to liberation of herpes simplex virus type 2 (HSV-2) progeny virions from the surface of infected cells is poorly understood. We report that the HSV-2 mutant deficient in the expression of a mucin-like membrane-associated glycoprotein G (mgG) exhibited defect in the release of progeny virions from infected cells manifested by ~2 orders of magnitude decreased amount of infectious virus in a culture medium as compared to native HSV-2. Electron microscopy revealed that the mgG deficient virions were produced in infected cells and present at the cell surface. These virions could be forcibly liberated to a nearly native HSV-2 level by the treatment of cells with glycosaminoglycan (GAG)-mimicking oligosaccharides. Comparative assessment of the interaction of mutant and native virions with surface-immobilized chondroitin sulfate GAG chains revealed that while the mutant virions associated with GAGs ~fourfold more extensively, the lateral mobility of bound virions was much poorer than that of native virions. These data indicate that the mgG of HSV-2 balances the virus interaction with GAG chains, a feature critical to prevent trapping of the progeny virions at the surface of infected cells.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Glicoproteínas / Proteínas do Envelope Viral / Herpesvirus Humano 2 / Liberação de Vírus / Herpes Simples Limite: Humans Idioma: En Revista: Viruses Ano de publicação: 2021 Tipo de documento: Article País de afiliação: Suécia

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Glicoproteínas / Proteínas do Envelope Viral / Herpesvirus Humano 2 / Liberação de Vírus / Herpes Simples Limite: Humans Idioma: En Revista: Viruses Ano de publicação: 2021 Tipo de documento: Article País de afiliação: Suécia