Skip to main content
. Author manuscript; available in PMC: 2022 Jan 1.
Published in final edited form as: J Proteome Res. 2020 Oct 19;20(1):485–497. doi: 10.1021/acs.jproteome.0c00521

Table 1.

Glycosylation of the secreted form of PD-L1 (Phe19-Thr239) produced by human HEK293, mouse NS0, and human MDA-MB-231 cells.

Origin Site SO GP# Glycan Type %
HEK293 (human) N35 >99% 44 HexNAc(6)Hex(4)SA(1) CL 13
HexNAc(6)Hex(5) CL 8
HexNAc(6)Hex(4)Fuc(1) CL 6
N192 >99% 75 HexNAc(4)Hex(4) CL 15
HexNAc(4)Hex(4)Fuc(1) CL 13
HexNAc(4)Hex(5) CL 12
N200 >81% 61 HexNAc(5)Hex(4)Fuc(1)SA(2) CL 19
HexNAc(5)Hex(4)SA(2) C 18
HexNAc(5)Hex(4)Fuc(2) C 5
N219 <0.1% 0 NQ n/a n/a
NS0 (mouse) N35 98% 7 HexNAc(5)Hex(9)Fuc(1) GG 43
HexNAc(5)Hex(8)Fuc(1) GG 30
HexNAc(9)Hex(4) CL 14
N192 >99% 19 HexNAc(2)Hex(5) HM 47
HexNAc(2)Hex(7) HM 32
HexNAc(2)Hex(6) HM 17
N200 97% 17 HexNAc(5)Hex(9)Fuc(1) GG 67
HexNAc(4)Hex(7)Fuc(1) GG 5
HexNAc(5)Hex(8)Fuc(1) GG 5
N219 >99% 34 HexNAc(8)Hex(8) CP 59
HexNAc(8)Hex(7) CP 22
HexNAc(8)Hex(6) CP 12
MDA-MB-231 (human) N35 91% 24 HexNAc(4)Hex(6)Fuc(1) H 26
HexNAc(4)Hex(6)Fuc(2) H 23
HexNAc(2)Hex(5) HM 10
N192 >99% 34 HexNAc(2)Hex(9) HM 25
HexNAc(3)Hex(5)SA(1) H 16
HexNAc(2)Hex(6) HM 12
N200 >99% 30 HexNAc(4)Hex(5)Fuc(1) C 43
HexNAc(4)Hex(4)Fuc(1) C 12
HexNAc(4)Hex(3)Fuc(1) PM 8
N219 <1% 9 HexNAc(5)Hex(5) C 33
HexNAc(4)Hex(5)Fuc(3) C 18
HexNAc(2)Hex(5) HM 17

Glycoforms were analyzed on four glycopeptides: DLYVVEYGSNMTIECK (N35), LFNVTSTLR (N192), INTTTNEIFYCTFR (N200), and LDPEENHTAELVIPELPLAHPPNER (N219). Abbreviations: HexNAc, N-acetylhexosamine; Hex, Hexose; Fuc, Fucose; SA, sialic acid; SO, site occupancy; GP#, number of identified glycopeptides; NQ, not quantifiable. Three most abundant glycoforms for each site are listed. Types of glycan structure: HM, high mannose; H, hybrid; C, complex; CL, complex glycan containing LacdiNAc; CP, complex glycan containing polyLacNAc; GG, complex glycan containing Gal-Gal (Galili); PM, paucimannose.