Methods for studying endocytotic pathways of herpesvirus encoded G protein-coupled receptors

Mavri, Maša (author), Spiess, Katja (author), Rosenkilde, Mette Marie (author), Rutland, Catrin S. (author), Vrecl, Milka (author), Kubale, Valentina (author)

Endocytosis is a fundamental process involved in trafficking of various extracellular and transmembrane molecules from the cell surface to its interior. This enables cells to communicate and respond to external environments, maintain cellular homeostasis, and transduce signals. G protein-coupled receptors (GPCRs) constitute a family of receptors with seven transmembrane alpha-helical domains (7TM receptors) expressed at the cell surface, where they regulate physiological and pathological cellular processes. Several herpesviruses encode receptors (vGPCRs) which benefits the virus by avoiding host immune surveillance, supporting viral dissemination, and thereby establishing widespread and lifelong infection, processes where receptor signaling and/or endocytosis seem central. vGPCRs are rising as potential drug targets as exemplified by the cytomegalovirus-encoded receptor US28, where its constitutive internalization has been exploited for selective drug delivery in virus infected cells. Therefore, studying GPCR trafficking is of great importance. This review provides an overview of the current knowledge of endocytic and cell localization properties of vGPCRs and methodological approaches used for studying receptor internalization. Using such novel approaches, we show constitutive internalization of the BILF1 receptor from human and porcine γ-1 herpesviruses and present motifs from the eukaryotic linear motif (ELM) resources with importance for vGPCR endocytosis.

• Language: English
• Keywords: endocytosis, G-protein coupled receptors, herpesvirus, methods, Herpesviridae
• Work type: Article
• Typology: 1.02 - Review Article
• Organization: VF - Veterinary Faculty
• Publication status: Published
• Publication version: Version of Record
• Year: 2020
• Number of pages: 23 str.
• Numbering: Vol. 25, iss. 23, art. 5710
• PID: 20.500.12556/RUL-128831
• UDC: 636.09:616
• ISSN on article: 1420-3049
• DOI: 10.3390/molecules25235710
• COBISS.SI-ID: 40808963
• Publication date in RUL: 04.08.2021

Record is a part of a journal

• Title: Molecules
• Shortened title: Molecules
• Publisher: MDPI
• ISSN: 1420-3049
• COBISS.SI-ID: 18462981

Licences

• License: CC BY 4.0, Creative Commons Attribution 4.0 International
• Link: http://creativecommons.org/licenses/by/4.0/
• Description: This is the standard Creative Commons license that gives others maximum freedom to do what they want with the work as long as they credit the author.
• Licensing start date: 03.12.2020