Abstract
Soluble forms of decay-accelerating factor (DAF) (CD55), the receptor for echovirus 7, were synthesized in the yeast Pichia pastoris. Purified recombinant protein containing SCR domains 2, 3, and 4, but lacking the serine/threonine rich region, was shown to block infection of susceptible cells by echovirus 7. In contrast to the situation with poliovirus and its receptor, the neutralization of echovirus 7 by soluble DAF was completely reversible and did not lead to the formation of 135S A-particles, Binding of virus to susceptible cells, by contrast, did lead to the formation of A particles, mainly from virus that had been internalized, The data suggest that a secondary factor(s) may contribute to A-particle formation and uncoating of echovirus 7.
Original language | English |
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Pages (from-to) | 9306-9312 |
Number of pages | 7 |
Journal | Journal of Virology |
Volume | 71 |
Issue number | 12 |
Publication status | Published - Dec 1997 |
Keywords
- COMPLEMENT REGULATORY PROTEIN
- HELA-CELLS
- HUMAN RHINOVIRUS
- MEASLES-VIRUS
- POLIOVIRUS
- MEMBRANE
- COFACTOR
- NEUTRALIZATION
- DOMAINS
- BINDING