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. 2014 Aug 4;173(3):177–188. doi: 10.1016/j.vetmic.2014.07.020

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Copyright © 2014 Elsevier B.V. All rights reserved.

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Fig. 2 — Sequence alignment of the putative fusion peptide and adjacent heptad repeat 1 (HR1) domain (A) and a part of the linker region and adjacent heptad repeat 2 (HR2) (B) of the spike protein. Residues diverging from the consensus are highlighted by grey boxes; aa at positions 1045 and 1108 are highlighted by translucent boxes. The putative fusion peptide and HR 1 and HR 2 domains are indicated by brackets. The leucine zipper domain in HR 2 is highlighted by black dots. A stretch of 14 aa comprising exactly two heptad repeats which is only found in alphacoronaviruses is indicated by a black bar. Numbers refer to amino acid position in spike protein of strain Black. Accession numbers of reference strains: Black: EU186072, C1Je: dq848678. Amino acids EY at position 1217/1218 of FECV were replaced with DH or QY in most FIPV spike proteins. Further noticeable changes were D1210N, E1267D/Q, Y1268H, N1275G, F1295L, T1299A/S, T1308A, YTT/I to FV/SN/R/M (1310–1312), E1315D/N, Y1334H, T/AP to I/TS/T (1341/1342), N/H/DL to HF/L (1345/1346), H1444N and S1454R/N (B).

Fig. 2 — Sequence alignment of the putative fusion peptide and adjacent heptad repeat 1 (HR1) domain (A) and a part of the linker region and adjacent heptad repeat 2 (HR2) (B) of the spike protein. Residues diverging from the consensus are highlighted by grey boxes; aa at positions 1045 and 1108 are highlighted by translucent boxes. The putative fusion peptide and HR 1 and HR 2 domains are indicated by brackets. The leucine zipper domain in HR 2 is highlighted by black dots. A stretch of 14 aa comprising exactly two heptad repeats which is only found in alphacoronaviruses is indicated by a black bar. Numbers refer to amino acid position in spike protein of strain Black. Accession numbers of reference strains: Black: EU186072, C1Je: dq848678. Amino acids EY at position 1217/1218 of FECV were replaced with DH or QY in most FIPV spike proteins. Further noticeable changes were D1210N, E1267D/Q, Y1268H, N1275G, F1295L, T1299A/S, T1308A, YTT/I to FV/SN/R/M (1310–1312), E1315D/N, Y1334H, T/AP to I/TS/T (1341/1342), N/H/DL to HF/L (1345/1346), H1444N and S1454R/N (B).