| Title: |
A transcriptionally controlled trans-processing assay: putative identification of a vaccinia virus-encoded proteinase which cleaves precursor protein P25K |
| Authors: |
Whitehead, S S; Hruby, D E |
| Source: |
Journal of Virology ; volume 68, issue 11, page 7603-7608 ; ISSN 0022-538X 1098-5514 |
| Publisher Information: |
American Society for Microbiology |
| Publication Year: |
1994 |
| Description: |
Vaccinia virus maturation into infectious particles appears to be dependent on the proteolytic processing of at least five viral proteins, each containing a conserved AG*X cleavage motif and each requiring proper association with the previrion particle. To identify the responsible proteinase, a transcriptionally controlled trans-processing assay was developed to monitor cleavage at the permissive AG*S site of the P25K core protein precursor. This assay led to the putative identification of a VV proteinase encoded by open reading frame G1L. The predicted protein contains an HXXEH sequence which is a direct inversion of the active site consensus sequence present in thermolysin and other metalloendopeptidases. Site-directed mutation of this consensus sequence suggests that the G1L protein may be a novel, virus-encoded metalloendoproteinase, although confirmation of this activity must await the development of a suitable cell-free processing assay. |
| Document Type: |
article in journal/newspaper |
| Language: |
English |
| DOI: |
10.1128/jvi.68.11.7603-7608.1994 |
| Availability: |
https://doi.org/10.1128/jvi.68.11.7603-7608.1994; https://journals.asm.org/doi/pdf/10.1128/jvi.68.11.7603-7608.1994 |
| Rights: |
https://journals.asm.org/non-commercial-tdm-license |
| Accession Number: |
edsbas.D3AD27EB |
| Database: |
BASE |