The BDLF3 gene product of Epstein-Barr virus, gp150, mediates non-productive binding to heparan sulfate on epithelial cells and only the binding domain of CD21 is required for infection
| Autor: | Liudmila S. Chesnokova, Sarah M. Valencia, Lindsey M. Hutt-Fletcher |
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| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Herpesvirus 4 Human B-cell receptor Virus Attachment Plasma protein binding CHO Cells Biology medicine.disease_cause Virus Article Cell Line 03 medical and health sciences chemistry.chemical_compound Viral Proteins Cricetulus Virology hemic and lymphatic diseases medicine Animals Humans Protein Interaction Domains and Motifs Cells Cultured chemistry.chemical_classification Membrane Glycoproteins Chinese hamster ovary cell Epithelial Cells Heparan sulfate Epstein–Barr virus Molecular biology 030104 developmental biology chemistry Receptors Complement 3d Heparitin Sulfate Glycoprotein Binding domain Protein Binding |
| Popis: | The cell surface molecules used by Epstein-Barr virus (EBV) to attach to epithelial cells are not well-defined, although when CD21, the B cell receptor for EBV is expressed epithelial cell infection increases disproportionately to the increase in virus bound. Many herpesviruses use low affinity charge interactions with molecules such as heparan sulfate to attach to cells. We report here that the EBV glycoprotein gp150 binds to heparan sulfate proteoglycans, but that attachment via this glycoprotein is not productive of infection. We also report that only the aminoterminal two short consensus repeats of CD21 are required for efficient infection, This supports the hypothesis that, when expressed on an epithelial cell CD21 serves primarily to cluster the major attachment protein gp350 in the virus membrane and enhance access of other important glycoproteins to the epithelial cell surface. |
| Databáze: | OpenAIRE |
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