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. 2013 Dec;87(24):13520–13531. doi: 10.1128/JVI.02123-13

Table 2.

Comparison of HN-H interaction residues of PIV5 F and measles virus Fa

Serial no. Mutated PIV5 F residue Corresponding measles virus F residue Location in PIV5 F prefusion structure Possible PIV5 HN-interacting residue Corresponding measles virus H-interacting residue
1 A392 T402 Domain II (Ig-like) Y ND
2 V393 I403 Domain II (Ig-like) Y ND
3 I394 I404 Domain II (Ig-like) ND
4 L395 N405 Domain II (Ig-like) Y ND
5 Q396 Q406 Domain II (Ig-like) ND
6 S382 S392 Domain II (Ig-like) Y ND
7 L384 L394 Domain II (Ig-like) Y Y
8 N298 S308 Domain I (h.p.) Y ND
9 F295 N305 Domain I (h.p.) ND
10 R368 R378 Domain I (h.p.) ND
11 T312 Q322 Domain I (h.p.) N Y
12 S314 Y324 Domain I (h.p.) N ND
13 Q339 Y349 Domain I (h.p.) N Y
14 V340 P350 Domain I N ND
15 V362 S372 Domain I N ND
16 S364 S374 Domain I N ND
a

List of point mutants generated in PIV5 F and the corresponding residues of measles virus F as shown by sequence alignment. The residues in PIV5 F or measles virus F (49) that are implicated in interactions with HN or H are indicated. PIV5 F residues shown in gray do not reach the surfaces of cells. Y, yes (possible interaction); N, no (possibly not involved in direct interaction); h.p., hydrophobic pocket adjacent to the Ig-like domain (Ig-like); ND, not determined.