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Infectious Entry and Neutralization of Pathogenic JC Polyomaviruses

  1. Author:
    Geoghegan, Eileen M
    Pastrana, Diana V
    Schowalter, Rachel M
    Ray, Upasana
    Gao, Wei
    Ho, Mitchell
    Pauly, Gary
    Sigano, Dina
    Kaynor, Campbell
    Cahir-McFarland, Ellen
    Combaluzier, Benoit
    Grimm, Jan
    Buck, Christopher B

  2. Author Address

    Laboratory of Cellular Oncology, Center for Cancer Research, National Cancer Institute, Bethesda, MD 20892-4263, USA., Antibody Therapy Section, Laboratory of Molecular Biology, Center for Cancer Research, National Cancer Institute, Bethesda, MD 20892, USA., Chemical Biology Laboratory, Center for Cancer Research, National Cancer Institute, Frederick, MD, 21702, USA., Biogen, Cambridge, MA 02142, USA., Neurimmune Holding AG, Schlieren-Zurich, Switzerland., Laboratory of Cellular Oncology, Center for Cancer Research, National Cancer Institute, Bethesda, MD 20892-4263, USA. Electronic address: buckc@mail.nih.gov.,
    1. Year: 2017
    2. Date: Oct 31
  2. Journal: Cell Reports
    1. 21
    2. 5
    3. Pages: 1169-1179
  4. Type of Article: Article
  5. ISSN: 2211-1247
  1. Abstract:

    Progressive multifocal leukoencephalopathy (PML) is a lethal brain disease caused by uncontrolled replication of JC polyomavirus (JCV). JCV strains recovered from the brains of PML patients carry mutations that prevent the engagement of sialylated glycans, which are thought to serve as receptors for the infectious entry of wild-type JCV. In this report, we show that non-sialylated glycosaminoglycans (GAGs) can serve as alternative attachment receptors for the infectious entry of both wild-type and PML mutant JCV strains. After GAG-mediated attachment, PML mutant strains engage non-sialylated non-GAG co-receptor glycans, such as asialo-GM1. JCV-neutralizing monoclonal antibodies isolated from patients who recovered from PML appear to block infection by preventing the docking of post-attachment co-receptor glycans in an apical pocket of the JCV major capsid protein. Identification of the GAG-dependent/sialylated glycan-independent alternative entry pathway should facilitate the development of infection inhibitors, including recombinant neutralizing antibodies. Published by Elsevier Inc.

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External Sources

  1. View Full Text
  2. DOI: 10.1016/j.celrep.2017.10.027
  3. PMID: 29091757
  4. View record in Web of Science®
  5. WOS: 000414057600006
  6. PII : S2211-1247(17)31459-6

Library Notes

  1. Fiscal Year: FY2017-2018
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