Two Early Vaccinia Virus Genes Encode Polypeptides Related to Protein Kinases

Abstract

SUMMARYVaccinia virus particles contain a protein kinase with an Mr of 62K calculated from sedimentation rate. We have sequenced the SalI G restriction fragment of the v accinia virus genome near to the right inverted terminal repeat and have identified two genes which share 36~ amino acid identity with each other and are related to the family of protein kinase genes. One gene, designated B1 R, encodes a 34.2K protein which shares 27~ identity with a protein kinase encoded by the herpes simplex virus type 1 US3 gene and contains conserved motifs characteristic of protein kinases of serine/ threonine specificity. The second gene, BI2R, encodes a protein of 33-3K which is poorly related to known protein kinases and lacks specific amino acids at several highly conserved key positions. The deduced partial amino acid sequence of a gene in the corresponding region of the cowpox virus genome is identical to B 12R except for one conservative amino acid substitution. Both of the vaccinia virus genes are transcribed towards the right-hand end of the genome early during infection. It is possible that the product of either or both of these genes associates to form a homo-or heterodimer that represents the 62K virion-associated protein kinase.

Phosphorylation of ribosomal proteins by the vaccinia virus B1R protein kinase

“…Although there is another vaccinia ORF designated Bl2R. that is related to BlR and to some other protein kinases, the gene product was considered unlikely to have protein kinase activity due to the poor conservation of several important motifs [24]. Moreover, the B13R protein expressed in E. coli does not have protein kinase activity under conditions in which the vaccinia Bl R protein kinase and a serine protein kinase from African swine fever virus are active [1,25] (A.H. Banham and G.L.…”

Nucleotide sequence of 42 kbp of vaccinia virus strain WR from near the right inverted terminal repeat

“…3. Genes known to be transcribed early during infection are DNA ligase (renamed SalF13R) (Smith et al, 1989b), TmpK (renamed SalF11R) (Smith et aL, 1989c), serpins B13R and B22R (renamed) (Smith et aL, 1989a), candidate protein kinases B1R and B12R (Howard & Smith, 1989;Traktman et al, 1989;Rempel et al, 1990), B2R (Rempel et al, 1990) and B18R (Ueda et al, 1990). The only late gene described from this region is the haemagglutinin (HA) (SalG1R) (Shida, 1986).…”

“…TmpK (SalFI1R), DNA ligase (SalF13R) and two potential serine-threonine protein kinases (B1R and B12R) have been described previously (Smith et al, 1989c, b;Kerr & Smith, 1989;Howard & Smith, 1989;Traktman et al, 1989;Rempel et al, 1990). Enzyme activity has been demonstrated for DNA ligase (Kerr & Smith, 1989;Colinas et al, 1990) and TmpK (S. Hughes, unpublished results).…”

“…Some of these gene families have already been described, e.g. the serpins (Kotwal & Moss, 1989;Smith et al, 1989a), protein kinases (Howard & Smith, 1989), D9R and D10R (Binns et al, 1990), and four families which have homologues encoded in the ITR of the SFV genome (Howard et al, 1991). One of these families includes host range proteins from cowpox and vaccinia virus, and several of the members have repeated sequences with homology to ankyrin or ankyrin-like repeats.…”

“…After the construction of restriction maps (Wittek et al, 1977;Mackett & Archard, 1979) and the cloning of individual restriction fragments (Wittek et al, 1980;Belle Isle et al, 1981), the 186kb genome of the laboratory strain of vaccinia virus (Western Reserve, WR) has been studied in detail. The structure of the terminal hairpins has been determined and the complete sequence of several of the viral HindIII restriction fragments and many individual genes have been reported from WR and other strains of virus (Ahn et al, 1990;Amegadzie et al, 1991;Baldick & Moss, 1987;Boursnell et al, 1988;Bertholet et al,, 1985;Broyles & Moss, 1986;Earl et al, 1986;Gillard et al, 1986;Gordon et al, 1988;Hirt et al, 1986;Howard & Smith, 1989;Howard et al, 1991 ;Jin et al, 1989;Kotwal & Moss, 1988aNiles et al, 1986;Plucienniczak et al, 1985;Rodriguez et al, 1986;Rodriguez & Esteban, 1987;Rosel et al, 1986;Rosel & Moss, 1985;Roseman & Hruby, 1987;Roseman & Slabaugh, 1990;Schmitt & Stunnenberg, 1989;Slabaugh & Roseman, 1989;Slabaugh et al, 1988;Shida, 1986;Smith et al, 1989a, b, c;Smith & Chan, 1991;Tamin et al, 1988;Tengelsen et al, 1988;Traktman et al, 1989;Tsoa et al, 1986;…”