Publication

Profiling of Glycan Receptors for Minute Virus of Mice in Permissive Cell Lines Towards Understanding the Mechanism of Cell Recognition

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Last modified
  • 03/05/2025
Type of Material
Authors
    Sujata Halder, University of FloridaSusan Cotmore, Yale UniversityJamie Heimburg-Molinaro, Emory UniversityDavid Smith, Emory UniversityRichard Cummings, Emory UniversityXi Chen, University of California DavisAlana J. Trollope, Imperial College LondonSimon J. North, Imperial College LondonStuart M. Haslam, Imperial College LondonAnne Dell, Imperial College LondonPeter Tattersall, Yale UniversityRobert McKenna, University of FloridaMavis Agbandje-McKenna, University of Florida
Language
  • English
Date
  • 2014-01-27
Publisher
  • Public Library of Science
Publication Version
Copyright Statement
  • © 2014 Halder et al.
License
Final Published Version (URL)
Title of Journal or Parent Work
ISSN
  • 1932-6203
Volume
  • 9
Issue
  • 1
Start Page
  • e86909
End Page
  • e86909
Grant/Funding Information
  • This work was supported by National Science Foundation [MCB-0718948 to R.M. and M.A-M.], University of Florida College of Medicine Research Funds to [M.A-M.], National Institute of Health [CA029303 to S.C. and P.T., GM085448 to D.F.S., and GM076360 to X.C.].
Supplemental Material (URL)
Abstract
  • The recognition of sialic acids by two strains of minute virus of mice (MVM), MVMp (prototype) and MVMi (immunosuppressive), is an essential requirement for successful infection. To understand the potential for recognition of different modifications of sialic acid by MVM, three types of capsids, virus-like particles, wild type empty (no DNA) capsids, and DNA packaged virions, were screened on a sialylated glycan microarray (SGM). Both viruses demonstrated a preference for binding to 9-O-methylated sialic acid derivatives, while MVMp showed additional binding to 9-O-acetylated and 9-O-lactoylated sialic acid derivatives, indicating recognition differences. The glycans recognized contained a type-2 Galβ1-4GlcNAc motif (Neu5Acα2-3Galβ1-4GlcNAc or 3′SIA-LN) and were biantennary complex-type N-glycans with the exception of one. To correlate the recognition of the 3′SIA-LN glycan motif as well as the biantennary structures to their natural expression in cell lines permissive for MVMp, MVMi, or both strains, the N- and O-glycans, and polar glycolipids present in three cell lines used for in vitro studies, A9 fibroblasts, EL4 T lymphocytes, and the SV40 transformed NB324K cells, were analyzed by MALDI-TOF/TOF mass spectrometry. The cells showed an abundance of the sialylated glycan motifs recognized by the viruses in the SGM and previous glycan microarrays supporting their role in cellular recognition by MVM. Significantly, the NB324K showed fucosylation at the non-reducing end of their biantennary glycans, suggesting that recognition of these cells is possibly mediated by the Lewis X motif as in 3′SIA-Le X identified in a previous glycan microarray screen.
Author Notes
Keywords
Research Categories
  • Biology, Molecular
  • Chemistry, Biochemistry

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