An important initial event in the life cycle of a virus is its attachment to a specific receptor at the surface of a cell. The presence of specific virus receptors on cells and in tissues contribute to the tropism of the virus as well as to tissue specific pathology associated with virus infection. Despite the importance of this initial event in virus infection very few virus receptors have been identified. Data presented in this dissertation strongly imply that major histocompatibility encoded class I proteins are receptors for the simian papovavirus, SV40. Adsorption of SV40 to rhesus monkey kidney cells inhibits the binding of anti-class I antibody to cells by 62%. This same pretreatment inhibits the binding of antibodies directed at two other cell surface proteins, anti-LFA-3 and anti-vitronectin receptor, by 22%. Pretreatment of rhesus monkey kidney cells with anti-class I antibody inhibits SV40 infection by 85%. The amount of inhibition decreases with increasing dilutions of antibody. Anti-LFA-3 and anti-vitronectin receptor antibodies do not inhibit infection by SV40. SV40 infection of class I negative Daudi cells were compared with infection of class I positive Raji cells. Raji cells were three fold more infectable than Daudi cells at multiplicities of infection (MOI) of both 10 and 100 plaque forming units per milliliter (PFU/ml). To demonstrate a direct interaction between SV40 and class I proteins, cell surface extracts were prepared from rhesus monkey kidney cells. When SV40 is incubated with these extracts and immunoprecipitated with anti-SV40 antibody class I proteins are specifically coimmunoprecipitated. Finally, purified class I proteins were found to inhibit SV40 infection by 68%.
| Identifer | oai:union.ndltd.org:UMASS/oai:scholarworks.umass.edu:dissertations-8149 |
| Date | 01 January 1991 |
| Creators | Atwood, Walter Joseph |
| Publisher | ScholarWorks@UMass Amherst |
| Source Sets | University of Massachusetts, Amherst |
| Language | English |
| Detected Language | English |
| Type | text |
| Source | Doctoral Dissertations Available from Proquest |
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