The vaccinia virus A40R gene product is a nonstructural, type II membrane glycoprotein that is expressed at the cell surface
| Autor: | Wei-Hong Zhang, Paula Traktman, Stephen A. Duncan, Geoffrey L. Smith, Diane Wilcock |
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| Rok vydání: | 1999 |
| Předmět: | |
| Zdroj: | Journal of General Virology. 80:2137-2148 |
| ISSN: | 1465-2099 0022-1317 |
| Popis: | Gene A40R from vaccinia virus (VV) strain Western Reserve has been characterized. The open reading frame (ORF) was predicted to encode a 159 amino acid, 18152 Da protein with amino acid similarity to C-type animal lectins and to the VV A34R protein, a component of extracellular enveloped virus (EEV). Northern blotting and S1 nuclease mapping showed that gene A40R is transcribed early during infection from a position 12 nucleotides upstream of the ORF, producing a transcript of approximately 600 nucleotides. Rabbit anti-sera were raised against bacterial fusion proteins containing parts of the A40R protein. These were used to identify an 18 kDa primary translation product andN- andO-glycosylated forms of 28, 35 and 38 kDa. The A40R proteins were detected early during infection, formed higher molecular mass complexes under non-reducing conditions and were present on the cell surface but absent from virions. The proteins partitioned with integral membrane proteins in Triton X-114. Canine pancreatic microsomal membranes protectedin vitro-translated A40R from proteinase K digestion, suggesting the A40R protein has type II membrane topology. A mutant virus with the A40R gene disrupted after amino acid 50, so as to remove the entire lectin-like domain, and a revertant virus were constructed. Disruption of the A40R gene did not affect virus plaque size,in vitrogrowth rate and titre, EEV formation, or virus virulence in a murine intranasal model. |
| Databáze: | OpenAIRE |
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