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. Author manuscript; available in PMC: 2009 Apr 13.
Published in final edited form as: Cytokine Growth Factor Rev. 2005 Jul 5;16(6):637–658. doi: 10.1016/j.cytogfr.2005.05.008

Table 6.

N- linked and O-linked glycosylation of chemokine receptors

Receptor Residuesa Cell type Ligand Effect Referenceb
CCR2B N14c HEK293d None = Surface expression [153]
CCR5 S6e (S7e) HEK293d; HeLad; MFd; Cf2Th-CD4d None = Surface expression [132,133]
Cf2Th-CD4d CCL3-4 + Binding [133]
HIV-1; SIV = HIVco [133]
CXCR2 N17c; N186c; N197c Neutrophils None + Proteolytic protection [152]
CXCL7 = Granulation, endocytosis, recycling [152]
CXCR4 Nc HEK293Td; HuTKd [141,188]
N11; (N176) CCCd; Mv-1-lud None + Surface expression [145]
HIV-2 3 HIVco [145]
BSC-1d None = Surface expression [144]
U373-MG-CD4+d R5 HIV-1 3 HIVco [144]
X4 HIV-1 = HIVco [144]
Cf2-Thd + sCD4 None = Surface expression [146]
X4 HIV-1 3 Binding; HIVco [146]
R5 HIV-1 3 Binding; HIVco [146]
CXCL12 + Binding; [Ca] [146]
D6 N17 L1.2d Murine CCL3 = Binding [156]
DARC N16 K562d = Surface expression [155]
CXCL8 = Binding [155]

HIVco: HIV co-receptor activity; MF: primary rhesus macrophages; sCD4: in the presence of soluble CD4; Ca: calcium mobilization. The term inside the paranthesis indicates glycosylation site effectively used, but to lesser extent or with less biological consequences. [Ca] indicates calcium mobilization likely indirect effect, namely due to enhanced ligand binding.

a

Residues are O-linked or N-linked glycosylated on a specific Ser (S) or Asn (N) residue, respectively. Glycosylation can promote (+), inhibit (−) or not affect the specific effect mentioned.

b

References include only those in which glycosylation was really demonstrated.

c

Still unclear whether that particular potential glycosylation site was effectively glycosylated.

d

Cells were transfected with the corresponding chemokine receptor.

e

Glycans were sialylated.