Electron microscopy of an alpha-dystroglycan fragment containing receptor sites for lymphocytic choriomeningitis virus and laminin, and use of the receptoid body as a reagent to neutralize virus.

Abstract	We report the electron microscopic structure of an alpha-dystroglycan (alpha-DG) fragment (DGEKFc4) that contains binding sites for lymphocytic choriomeningitis virus (LCMV) and the extracellular matrix (ECM) molecule laminin. In electron microscopic images, DGEKFc4 appears as dumbbell-shaped rods with a length of 7.5 +/- 0.5 nM and width of 3 +/- 0.3 nM. The C-terminal human Fc allows binding of anti-human Fc antibody resulting in formation of immune complexes that preserve alpha-DG binding to virus. Electron microscopy shows the antibody binding to near one end of the dumbbell-shaped rods. Because arenaviruses like LCMV or Lassa fever virus (LFV) generate poor neutralizing antibodies during natural infection or vaccination, we assayed whether the alpha-DG receptoid bodies generated could be used as an efficient antibody mimic. However, the receptor body formed by either alpha-DG fragment alone or complexed to antibody to human Fc failed to efficiently neutralize virus.
Authors	Stefan Kunz, Lesley Calder, Michael B A Oldstone
Journal	Virology (Virology) Vol. 325 Issue 2 Pg. 207-15 (Aug 01 2004) ISSN: 0042-6822 [Print] United States
PMID	15246261 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)
Chemical References	Cytoskeletal Proteins DAG1 protein, human DNA Primers Membrane Glycoproteins Peptide Fragments Receptors, Laminin Receptors, Virus Dystroglycans
Topics	Animals Base Sequence Binding Sites Cell Line Cytoskeletal Proteins (chemistry, genetics, physiology, ultrastructure) DNA Primers (genetics) Dystroglycans Humans In Vitro Techniques Lymphocytic choriomeningitis virus (physiology) Membrane Glycoproteins (chemistry, genetics, physiology, ultrastructure) Microscopy, Electron Neutralization Tests Peptide Fragments (chemistry, genetics, physiology, ultrastructure) Rabbits Receptors, Laminin (physiology) Receptors, Virus (physiology)

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