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SLC35A2 gene product modulates paramyxovirus fusion events during infection.

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  • Additional Information
    • Source:
      Publisher: Public Library of Science Country of Publication: United States NLM ID: 101238921 Publication Model: eCollection Cited Medium: Internet ISSN: 1553-7374 (Electronic) Linking ISSN: 15537366 NLM ISO Abbreviation: PLoS Pathog Subsets: MEDLINE
    • Publication Information:
      Original Publication: San Francisco, CA : Public Library of Science, c2005-
    • Subject Terms:
      Virus Internalization*; Humans ; Animals ; Paramyxoviridae Infections/virology ; Paramyxoviridae Infections/metabolism ; Newcastle disease virus/genetics ; Newcastle disease virus/physiology ; Nucleotide Transport Proteins/metabolism ; Nucleotide Transport Proteins/genetics ; Monosaccharide Transport Proteins/metabolism ; Monosaccharide Transport Proteins/genetics ; Paramyxoviridae/genetics ; A549 Cells ; Sendai virus/genetics
    • Abstract:
      Paramyxoviruses are significant human and animal pathogens that include mumps virus (MuV), Newcastle disease virus (NDV) and the murine parainfluenza virus Sendai (SeV). Despite their importance, few host factors implicated in paramyxovirus infection are known. Using a recombinant SeV expressing destabilized eGFP (rSeVCdseGFP) in a loss-of-function CRISPR screen, we identified the CMP-sialic acid transporter (CST) gene SLC35A1 and the UDP-galactose transporter (UGT) gene SLC35A2 as essential for paramyxovirus infection. As expected, SLC35A1 knockout (KO) cells showed drastic reduction in infections with SeV, NDV and MuV due to the lack of cell surface sialic acids receptors. However, SLC35A2 KO cells revealed unknown critical roles for this factor in virus-cell and cell-to-cell fusion events for the different paramyxoviruses. While UGT was essential for virus-cell fusion during SeV entry to the cell, it was not required for NDV or MuV entry. Importantly, UGT promoted the formation of syncytia during MuV infection, suggesting a role in cell-to-cell virus spread. Our findings demonstrate that paramyxoviruses can bind to or enter A549 cells in the absence of canonical galactose-bound sialic-acid decorations and show that UGT facilitates paramyxovirus fusion processes involved in entry and spread.
      Competing Interests: The authors have declared that no competing interests exist.
      (Copyright: © 2025 Yang et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.)
    • Comments:
      Update of: bioRxiv. 2024 Aug 27:2024.08.27.609835. doi: 10.1101/2024.08.27.609835. (PMID: 39253522)
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    • Grant Information:
      R01 AI137062 United States AI NIAID NIH HHS; T32 DK077653 United States DK NIDDK NIH HHS
    • Accession Number:
      0 (Nucleotide Transport Proteins)
      0 (Monosaccharide Transport Proteins)
      0 (SLC35A1 protein, human)
    • Publication Date:
      Date Created: 20250110 Date Completed: 20250123 Latest Revision: 20250129
    • Publication Date:
      20250129
    • Accession Number:
      PMC11756793
    • Accession Number:
      10.1371/journal.ppat.1012531
    • Accession Number:
      39792924