Disease relevance of 6K1

• A possible regulatory effect on the function of the potyvirus P3 + 6K1 protein by processing at the P3-6K1 junction is discussed in light of our present results with PPV [1].
• In this study, 6K1-specific polyclonal antiserum was raised against PPV 6K1 expressed in Escherichia coli as a translational fusion with the N terminus of avian troponin C and an unusual metal-binding cluster of troponin T-1 [2].
• Amino acid sequence comparison with poty- and rymoviruses reveals eight domains corresponding to the potyviral P3, 6K1, Cl, 6K2, Nla-VPg, Nla-Pro, Nlb and capsid proteins, respectively [3].
• To evaluate molecular variability in the 5' region of the Plum pox virus (PPV) genome, a fragment spanning the C-terminal part of P3, the complete 6K1 and start of the CI gene in 12 Slovak and French PPV isolates was amplified in IC-RT-PCR and sequenced [4].

High impact information on 6K1

• For detection of 6K1 in vivo, a pPPV-H6K1-NAT infectious clone was constructed, enabling concentration of histidine-tagged 6K1 by affinity chromatography [2].
• However, deletion of either the 6K1 or 6K2 protein-encoding regions rendered PVA non-infectious [5].
• The sites at the P3/6K1, CI-6K2 and VPg/NIaPro junctions were processed slowly, in contrast to other proteolytic cleavage sites which were processed at a high rate [5].
• However, disease symptoms were not detected and virus accumulation occurred after a second site mutation was introduced into the 6K1 cistron during replication [1].
• The 6K1 protein between P3 and C1 is also highly similar to those of other potyviruses [6].

Biological context of 6K1

• Although sequence identities over most of the genome were well above 90% at both the nt and aa levels, reaching 99.6% (aa) in the CP and 100% (aa) in the 6K1 and 6K2, thereby suggesting that WMV-Pk and WMV-Fr are identical strains, but the sequence identities in the P1 region were only 80.6% (aa) and 82.8% (nt), while that in the 5' UTR was 82% [7].

Other interactions of 6K1

• In particular, the most considerable divergence has been found in part of 5' non coding region, in regions encoding P1, P3 + 6K1, 6K2 and NIa-VPg proteins as well as in the N-terminal domain of the coat protein [8].

References