Table 2.
Peptides used for probing CyPA bindinga
| Peptide | Sequence |
|---|---|
| P1 | THSNTYDVDMVDANLLME |
| P2 | ANLLMEGGVAQTEPESRV |
| P3 | EPESRVPVLDFLEPMAEE |
| P4 | EPMAEEESDLEPSIPSEC |
| P5 | SIPSECMLPRSGFPRALP |
| P6 | FPRALPAWARPDYNPPLV |
| P7 | NPPLVESWRRPDYQPPTV* |
| P8 | DYQPPTVAGCALPPPKKA |
| P9 | PPPKKAPTPPPRRRRTVG |
| P10 | RRRTVGLSESTISEALQQ |
| P11 | SEALQQLAIKTFGQPPSS |
| P12 | GQPPSSGDAGSSTGAGAA |
| P13 | TGAGAAESGGPTSPGEPA |
| P14 | SPGEPAPSETGSASSMPP |
| P15 | ASSMPPLEGEPGDPDLES |
| P16 | DPDLESDQVELQPPPQGG |
| P17 | PPPQGGGVAPGSGSGSWS |
| P18 | GSGSWSTCSEEDDTTVCC |
a
Sequences of 18 peptides (P1 through P18) that span the distance from low-complexity sequence I (LCS-I) to the C terminus of domain III of JFH-1 NS5A (residues 245 through 466) are shown. Each is 18 residues in length and includes a six-amino-acid overlap with the preceding peptide.
*
, the P7 peptide was shifted one residue to avoid an N-terminal tyrosine, which interfered with the HRP-based spot assay used in this study.