prikaz prve stranice dokumenta Human cytomegalovirus glycoprotein complex gH/gL/gO uses PDGFR-α as a key for entry
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Scientific paper - Original scientific paper
Human cytomegalovirus glycoprotein complex gH/gL/gO uses PDGFR-α as a key for entry
PLoS Pathogens, 13 (2017), 4; e1006281. https://doi.org/10.1371/journal.ppat.1006281
Wu, Yiquan; ...; ...; Brizić, Ilija; ...; ...

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Wu, Y. & Brizić, I. (2017). Human cytomegalovirus glycoprotein complex gH/gL/gO uses PDGFR-α as a key for entry. PLoS Pathogens, 13. (4). doi: 10.1371/journal.ppat.1006281

Wu, Yiquan and Ilija Brizić. "Human cytomegalovirus glycoprotein complex gH/gL/gO uses PDGFR-α as a key for entry." PLoS Pathogens, vol. 13, no. 4, 2017. https://doi.org/10.1371/journal.ppat.1006281

Wu, Yiquan and Ilija Brizić. "Human cytomegalovirus glycoprotein complex gH/gL/gO uses PDGFR-α as a key for entry." PLoS Pathogens 13, no. 4 (2017). https://doi.org/10.1371/journal.ppat.1006281

Wu, Y. and Brizić, I. (2017) 'Human cytomegalovirus glycoprotein complex gH/gL/gO uses PDGFR-α as a key for entry', PLoS Pathogens, 13(4). doi: 10.1371/journal.ppat.1006281

Wu Y, Brizić I. Human cytomegalovirus glycoprotein complex gH/gL/gO uses PDGFR-α as a key for entry. PLoS Pathogens [Internet]. 2017 [cited 2024 December 27];13(4). doi: 10.1371/journal.ppat.1006281

Y. Wu and I. Brizić, "Human cytomegalovirus glycoprotein complex gH/gL/gO uses PDGFR-α as a key for entry", PLoS Pathogens, vol. 13, no. 4, 2017. [Online]. Available at: https://urn.nsk.hr/urn:nbn:hr:184:966328. [Accessed: 27 December 2024]

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Metadata
Title (english)Human cytomegalovirus glycoprotein complex gH/gL/gO uses PDGFR-α as a key for entry
AuthorYiquan Wu
Author
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Author
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AuthorIlija Brizić
Author
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Author
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Author's institutionUniversity of Rijeka
Faculty of Medicine
(Center for Proteomics)
Scientific / art field,
discipline and subdiscipline		BIOMEDICINE AND HEALTHCARE
Basic Medical Sciences
Abstract (english)
Herpesvirus gH/gL envelope glycoprotein complexes are key players in virus entry as ligands for host cell receptors and by promoting fusion of viral envelopes with cellular membranes. Human cytomegalovirus ( HCMV) has two alternative gH/gL complexes, gH/gL/gO and gH/gL/UL128,130,131A which both shape the HCMV tropism. By studying binding of HCMV particles to fibroblasts, we could for the first time show that virion gH/gL/gO binds to platelet-derived growth factor-alpha (PDGFR-alpha) on the surface of fibroblasts and that gH/gL/gO either directly or indirectly recruits gB to this complex. PDGFR-alpha functions as an entry receptor for HCMV expressing gH/gL/gO, but not for HCMV mutants lacking the gH/gL/gO complex. PDGFR-alpha-dependent entry is not dependent on activation of PDGFR-alpha. We could also show that the gH/gL/gO-PDGFR-alpha interaction starts the predominant entry pathway for infection of fibroblasts with free virus. Cell-associated virus spread is either driven by gH/gL/gO interacting with PDGFR-alpha or by the gH/gL/UL128,130,131A complex. PDGFR-alpha-positive cells may thus be preferred first target cells for infections with free virus which might have implications for the design of future HCMV vaccines or anti-HCMV drugs.
Keywords (english)
Languageenglish
Publication typeScientific paper - Original scientific paper
Publication statusPublished
Peer reviewPeer review - international
Publication versionPublished version
Journal titlePLoS Pathogens
Numberingvol. 13, no. 4, e1006281
p-ISSN1553-7366
e-ISSN1553-7374
DOIhttps://doi.org/10.1371/journal.ppat.1006281
URN:NBNurn:nbn:hr:184:966328
Publication2017
Document URLhttp://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1006281
Type of resourceText
Access conditionsOpen access
Terms of useLicence Attribution 4.0 International (CC BY 4.0) icon
Created on2017-12-27 09:36:06