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

Virology
Stefan KunzMichael B A Oldstone

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.

References

Sep 20, 1991·Cell·J M Ervasti, K P Campbell
Aug 1, 1983·The Journal of General Virology·F J Dutko, M B Oldstone
Aug 1, 1993·The Journal of Cell Biology·J M Ervasti, K P Campbell
Feb 16, 1996·The Journal of Biological Chemistry·E A PallJ M Ervasti
Dec 1, 1996·Journal of Virology·Y ChenR M Marks
Dec 29, 1998·Cell·M D Henry, K P Campbell
Apr 11, 2001·Advances in Immunology·P W Parren, D R Burton
Apr 23, 2002·Journal of Virology·Christina F SpiropoulouMichael B A Oldstone

❮ Previous
Next ❯

Related Concepts

Related Feeds