Vaccinia virus L1 binds to cell surfaces and blocks virus entry independently of glycosaminoglycans
| Autor: | Chwan Hong Foo, Huan Lou, Roselyn J. Eisenberg, Doina Atanasiu, Manuel Ponce-de-Leon, J. Charles Whitbeck, Gary H. Cohen |
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| Rok vydání: | 2009 |
| Předmět: |
viruses
Entry Virus Attachment Attachment Vaccinia virus Biology Antibodies Viral DNA-binding protein Article Virus Cell Line Cell membrane Mice 03 medical and health sciences chemistry.chemical_compound Viral Envelope Proteins Viral entry Virology Chlorocebus aethiops medicine Vaccinia Animals Humans Receptor Vero Cells Glycosaminoglycans 030304 developmental biology 0303 health sciences Cell Membrane 030302 biochemistry & molecular biology Membrane Proteins virus diseases Fibroblasts Virus Internalization L1 3. Good health medicine.anatomical_structure chemistry Cell culture Poxvirus Vero cell Receptors Virus A28 Carrier Proteins Viral Fusion Proteins Receptor-binding HeLa Cells |
| Zdroj: | Virology. 385(2):368-382 |
| ISSN: | 0042-6822 |
| DOI: | 10.1016/j.virol.2008.12.019 |
| Popis: | L1 and A28 are vaccinia virus (VACV) envelope proteins which are essential for cellular entry. However, their specific roles during entry are unknown. We tested whether one or both of these proteins might serve as receptor binding proteins (RBP). We found that a soluble, truncated form of L1, but not A28, bound to cell surfaces independently of glycosaminoglycans (GAGs). Hence, VACV A28 is not likely to be a RBP and functions after attachment during entry. Importantly, soluble L1 inhibited both binding and entry of VACV in GAG-deficient cells, suggesting that soluble L1 blocks entry at the binding step by competing with the virions for non-GAG receptors on cells. In contrast, soluble A27, a VACV protein which attaches to GAGs but is non-essential for virus entry, inhibited binding and entry of VACV in a GAG-dependent manner. To our knowledge, this is the first report of a VACV envelope protein that blocks virus binding and entry independently of GAGs. |
| Databáze: | OpenAIRE |
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