NDLI: Characterization of the echovirus 7 receptor: domains of CD55 critical for virus binding.

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Mapping of mutations contributing to the temperature sensitivity of the Sabin 1 vaccine strain of poliovirus.

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Characterization of the echovirus 7 receptor: domains of CD55 critical for virus binding.

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Infectious cDNA clones of echovirus 12 and a variant resistant against the uncoating inhibitor rhodanine differ in seven amino acids.

Immune responses to plasmid DNA encoding the hepatitis C virus core protein.

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Isolation of novel human endogenous retrovirus-like elements with foamy virus-related pol sequence.

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Sequences in the human immunodeficiency virus type 1 U3 region required for in vivo and in vitro integration.

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Full-length proviruses of baboon endogenous virus (BaEV) and dispersed BaEV reverse transcriptase retroelements in the genome of baboon species.

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Characterization of the echovirus 7 receptor: domains of CD55 critical for virus binding.

Content Provider	PubMed Central
Author	Clarkson, N. A. Kaufman, R. Lublin, D. M. Ward, T. Pipkin, P. A. Minor, P. D. Evans, D. J. Almond, J. W.
Abstract	CD55, or decay-accelerating factor (DAF), is a cell surface glycoprotein which regulates complement activity by accelerating the decay of C3/C5 convertases. Recently, we and others have established that this molecule acts as a cellular receptor for echovirus 7 and related viruses. DAF consists of five domains: four short consensus repeats (SCRs) and a serine/threonine-rich region, attached to the cell surface by a glycosylphosphatidyl inositol anchor. Chinese hamster ovary cells stably transfected with deletion mutants of DAF or DAF-membrane cofactor protein recombinants were analyzed for virus binding. The results indicate that the binding of echovirus 7 to DAF specifically requires SCR2, SCR3, and SCR4. There is also a nonspecific requirement for the S/T-rich region which probably functions to project the binding region away from the cell membrane. The three nonpeptide modifications of DAF, N-linked glycosylation, O-linked glycosylation, and the glycosylphosphatidyl inositol anchor, are not required for virus binding. The SCRs of membrane cofactor protein, the closest known relative of DAF, cannot substitute for those of DAF with retention of virus binding activity. The monoclonal antibody used to identify DAF as an echovirus receptor, and which inhibits binding of the virus (monoclonal antibody 854), binds to SCR3.
Starting Page	5497
File Format	PDF
ISSN	10985514
e-ISSN	10985514
Journal	Journal of Virology
Issue Number	9
Volume Number	69
Language	English
Publisher Date	1995-09-01
Access Restriction	Open
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Virology Immunology Microbiology Insect Science

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