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| Fältnamn | Indikatorer | Metadata |
|---|---|---|
| 000 | 03269naa a2200349 4500 | |
| 001 | oai:lup.lub.lu.se:e3a2cdc2-22e8-4cd1-8dd2-65fbde1f7bc0 | |
| 003 | SwePub | |
| 008 | 160401s2005 | |||||||||||000 ||eng| | |
| 024 | 7 | a https://lup.lub.lu.se/record/2248702 URI |
| 024 | 7 | a https://doi.org/10.1128/JVI.79.18.12016-12024.20052 DOI |
| 040 | a (SwePub)lu | |
| 041 | a engb eng | |
| 042 | 9 SwePub | |
| 072 | 7 | a art2 swepub-publicationtype |
| 072 | 7 | a ref2 swepub-contenttype |
| 100 | 1 | a Goodfellow, IG4 aut |
| 245 | 1 0 | a Inhibition of coxsackie B virus infection by soluble forms of its receptors: Binding affinities, altered particle formation, and competition with cellular receptors |
| 264 | 1 | c 2005 |
| 520 | a We previously reported that soluble decay-accelerating factor (DAF) and coxsackievirus-adenovirus receptor (CAR) blocked coxsackievirus 133 (CVB3) myocarditis in mice, but only soluble CAR blocked CVB3-mediated pancreatitis. Here, we report that the in vitro mechanisms of viral inhibition by these soluble receptors also differ. Soluble DAF inhibited virus infection through the formation of reversible complexes with CVB3, while binding of soluble CAR to CVB induced the formation of altered (A) particles with a resultant irreversible loss of infectivity. A-particle formation was characterized by loss of VP4 from the virions and required incubation of CVB3-CAR complexes at 37 degrees C. Dimeric soluble DAF (DAF-Fc) was found to be 125-fold-more effective at inhibiting CVB3 than monomeric DAF, which corresponded to a 100-fold increase in binding affinity as determined by surface plasmon resonance analysis. Soluble CAR and soluble dimeric CAR (CAR-Fc) bound to CVB3 with 5,000- and 10,000-fold-higher affinities than the equivalent forms of DAF. While DAF-Fc was 125-fold-more effective at inhibiting virus than monomeric DAF, complement regulation by DAF-Fc was decreased 4 fold. Therefore, while the virus binding was a cooperative event, complement regulation was hindered by the molecular orientation of DAF-Fc, indicating that the regions responsible for complement regulation and virus binding do not completely overlap. Relative contributions of CVB binding affinity, receptor binding footprint on the virus capsid, and induction of capsid conformation alterations for the ability of cellular DAF and CAR to act as receptors are discussed. | |
| 650 | 7 | a MEDICIN OCH HÄLSOVETENSKAPx Klinisk medicin0 (SwePub)3022 hsv//swe |
| 650 | 7 | a MEDICAL AND HEALTH SCIENCESx Clinical Medicine0 (SwePub)3022 hsv//eng |
| 700 | 1 | a Evans, DJ4 aut |
| 700 | 1 | a Blom, Annau Lund University,Lunds universitet,Proteinkemi, Malmö,Forskargrupper vid Lunds universitet,Protein Chemistry, Malmö,Lund University Research Groups4 aut0 (Swepub:lu)klke-abl |
| 700 | 1 | a Kerrigan, D4 aut |
| 700 | 1 | a Miners, JS4 aut |
| 700 | 1 | a Morgan, BP4 aut |
| 700 | 1 | a Spiller, OB4 aut |
| 710 | 2 | a Proteinkemi, Malmöb Forskargrupper vid Lunds universitet4 org |
| 773 | 0 | t Journal of Virologyg 79:18, s. 12016-12024q 79:18<12016-12024x 1098-5514 |
| 856 | 4 | u http://dx.doi.org/10.1128/JVI.79.18.12016-12024.2005x freey FULLTEXT |
| 856 | 4 8 | u https://lup.lub.lu.se/record/224870 |
| 856 | 4 8 | u https://doi.org/10.1128/JVI.79.18.12016-12024.2005 |
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