Table 2.
N-glycosylation in the IBV M41-CK S glycoprotein and relative glycoform abundance (%) at each site
|
N-glycan site |
|||||||||
|---|---|---|---|---|---|---|---|---|---|
|
|
Predicted |
Observed |
|
|
|
|
|||
|
Subunit |
Domain |
Position |
HCDpdEThcd |
D2O labelled |
Enzyme |
Peptide sequence |
Glycan composition |
Relative glycan composition (%) |
Glycan type |
|
S1 |
S1-NTD |
144 |
144 |
144 |
Chymotrypsin |
Y.NLTVSVAKYPTF.K |
HexNAc(2)Hex(7); HexNAc(2)Hex(8) |
74;26 |
N-linked oligomannose |
|
S1 |
S1-NTD |
212 |
212 |
212 |
Trypsin |
K.ALAYFVNGTAQDVILCDGSPR.G |
HexNAc(2)Hex(8); HexNAc(2)Hex(9) |
26;74 |
N-linked oligomannose |
|
S1 |
|
425 |
425 |
Trypsin |
R.HNYNNITLNTCVDYNIYGR.T |
HexNAc(2)Hex(5); HexNAc(2)Hex(6); HexNAc(2)Hex(7); HexNAc(2)Hex(8) |
23;17;27;33 |
N-linked oligomannose |
|
|
S1 |
|
447 |
447 |
447 |
Chymotrypsin |
Y.GRTGQGFITNVTDSAVSY.N |
HexNAc(2)Hex(8) |
100 |
N-linked oligomannose |
|
S1 |
|
513 |
513 |
513 |
Trypsin |
R.NETGSQLLENQFYIK.I |
HexNAc(2)Hex(5); HexNAc(2)Hex(7); HexNAc(2)Hex(8) |
37;37;26 |
N-linked oligomannose |
|
S2 |
|
947 |
947 |
947 |
Chymotrypsin |
F.SYTPDSFVNVTAIVGF.C |
HexNAc(2)Hex(5); HexNAc(2)Hex(7); HexNAc(3)Hex(6) |
46;24;30 |
N-linked oligomannose |
|
S2 |
|
979 |
979 |
979 |
Chymotrypsin |
F.IQVNGSYY.I |
HexNAc(2)Hex(5) |
100 |
N-linked oligomannose |
|
S2 |
|
1014 |
1014 |
1014 |
Chymotrypsin; Trypsin |
Y.VSVNKTVITTF.V; R.AITAGDIVTLTSCQANYVSVNK.T |
HexNAc(2)Hex(5) |
100 |
N-linked oligomannose |
Position refers to asparagine residue position in the amino acid sequence of IBV M41-CK S protein. Blank cells indicate that the glycan was not confirmed by this method.