Chemokine binding to PSGL-1 is controlled by O-glycosylation and tyrosine sulfation

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Standard

Chemokine binding to PSGL-1 is controlled by O-glycosylation and tyrosine sulfation. / Goth, Christoffer K.; Mehta, Akul Y.; McQuillan, Alyssa M.; Baker, Kelly J.; Hanes, Melinda S.; Park, Simon S.; Stavenhagen, Kathrin; Hjortø, Gertrud M.; Heimburg-Molinaro, Jamie; Chaikof, Elliot L.; Rosenkilde, Mette M.; Cummings, Richard D.

I: Cell Chemical Biology, Bind 30, Nr. 8, 2023, s. 893-905.e7.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Goth, CK, Mehta, AY, McQuillan, AM, Baker, KJ, Hanes, MS, Park, SS, Stavenhagen, K, Hjortø, GM, Heimburg-Molinaro, J, Chaikof, EL, Rosenkilde, MM & Cummings, RD 2023, 'Chemokine binding to PSGL-1 is controlled by O-glycosylation and tyrosine sulfation', Cell Chemical Biology, bind 30, nr. 8, s. 893-905.e7. https://doi.org/10.1016/j.chembiol.2023.06.013

APA

Goth, C. K., Mehta, A. Y., McQuillan, A. M., Baker, K. J., Hanes, M. S., Park, S. S., Stavenhagen, K., Hjortø, G. M., Heimburg-Molinaro, J., Chaikof, E. L., Rosenkilde, M. M., & Cummings, R. D. (2023). Chemokine binding to PSGL-1 is controlled by O-glycosylation and tyrosine sulfation. Cell Chemical Biology, 30(8), 893-905.e7. https://doi.org/10.1016/j.chembiol.2023.06.013

Vancouver

Goth CK, Mehta AY, McQuillan AM, Baker KJ, Hanes MS, Park SS o.a. Chemokine binding to PSGL-1 is controlled by O-glycosylation and tyrosine sulfation. Cell Chemical Biology. 2023;30(8):893-905.e7. https://doi.org/10.1016/j.chembiol.2023.06.013

Author

Goth, Christoffer K. ; Mehta, Akul Y. ; McQuillan, Alyssa M. ; Baker, Kelly J. ; Hanes, Melinda S. ; Park, Simon S. ; Stavenhagen, Kathrin ; Hjortø, Gertrud M. ; Heimburg-Molinaro, Jamie ; Chaikof, Elliot L. ; Rosenkilde, Mette M. ; Cummings, Richard D. / Chemokine binding to PSGL-1 is controlled by O-glycosylation and tyrosine sulfation. I: Cell Chemical Biology. 2023 ; Bind 30, Nr. 8. s. 893-905.e7.

Bibtex

@article{64e75497d4f740cf89415ddad624b361,

title = "Chemokine binding to PSGL-1 is controlled by O-glycosylation and tyrosine sulfation",

abstract = "Protein glycosylation influences cellular recognition and regulates protein interactions, but how glycosylation functions alongside other common posttranslational modifications (PTMs), like tyrosine sulfation (sTyr), is unclear. We produced a library of 53 chemoenzymatically synthesized glycosulfopeptides representing N-terminal domains of human and murine P-selectin glycoprotein ligand-1 (PSGL-1), varying in sTyr and O-glycosylation (structure and site). Using these, we identified key roles of PSGL-1 O-glycosylation and sTyr in controlling interactions with specific chemokines. Results demonstrate that sTyr positively affects CCL19 and CCL21 binding to PSGL-1 N terminus, whereas O-glycan branching and sialylation reduced binding. For murine PSGL-1, interference between PTMs is greater, attributed to proximity between the two PTMs. Using fluorescence polarization, we found sTyr is a positive determinant for some chemokines. We showed that synthetic sulfopeptides are potent in decreasing chemotaxis of human dendritic cells toward CCL19 and CCL21. Our results provide new research avenues into the interplay of PTMs regulating leukocyte/chemokine interactions.",

keywords = "CCL19, CCL21, CCL5, chemokine, glycosulfopeptides, O-glycan, P-selectin, PSGL-1, tyrosine sulfation",

author = "Goth, {Christoffer K.} and Mehta, {Akul Y.} and McQuillan, {Alyssa M.} and Baker, {Kelly J.} and Hanes, {Melinda S.} and Park, {Simon S.} and Kathrin Stavenhagen and Hjort{\o}, {Gertrud M.} and Jamie Heimburg-Molinaro and Chaikof, {Elliot L.} and Rosenkilde, {Mette M.} and Cummings, {Richard D.}",

note = "Publisher Copyright: {\textcopyright} 2023 Elsevier Ltd",

year = "2023",

doi = "10.1016/j.chembiol.2023.06.013",

language = "English",

volume = "30",

pages = "893--905.e7",

journal = "Chemistry and Biology",

issn = "2451-9448",

publisher = "Elsevier",

number = "8",

}

RIS

TY - JOUR

T1 - Chemokine binding to PSGL-1 is controlled by O-glycosylation and tyrosine sulfation

AU - Goth, Christoffer K.

AU - Mehta, Akul Y.

AU - McQuillan, Alyssa M.

AU - Baker, Kelly J.

AU - Hanes, Melinda S.

AU - Park, Simon S.

AU - Stavenhagen, Kathrin

AU - Hjortø, Gertrud M.

AU - Heimburg-Molinaro, Jamie

AU - Chaikof, Elliot L.

AU - Rosenkilde, Mette M.

AU - Cummings, Richard D.

PY - 2023

Y1 - 2023

N2 - Protein glycosylation influences cellular recognition and regulates protein interactions, but how glycosylation functions alongside other common posttranslational modifications (PTMs), like tyrosine sulfation (sTyr), is unclear. We produced a library of 53 chemoenzymatically synthesized glycosulfopeptides representing N-terminal domains of human and murine P-selectin glycoprotein ligand-1 (PSGL-1), varying in sTyr and O-glycosylation (structure and site). Using these, we identified key roles of PSGL-1 O-glycosylation and sTyr in controlling interactions with specific chemokines. Results demonstrate that sTyr positively affects CCL19 and CCL21 binding to PSGL-1 N terminus, whereas O-glycan branching and sialylation reduced binding. For murine PSGL-1, interference between PTMs is greater, attributed to proximity between the two PTMs. Using fluorescence polarization, we found sTyr is a positive determinant for some chemokines. We showed that synthetic sulfopeptides are potent in decreasing chemotaxis of human dendritic cells toward CCL19 and CCL21. Our results provide new research avenues into the interplay of PTMs regulating leukocyte/chemokine interactions.

AB - Protein glycosylation influences cellular recognition and regulates protein interactions, but how glycosylation functions alongside other common posttranslational modifications (PTMs), like tyrosine sulfation (sTyr), is unclear. We produced a library of 53 chemoenzymatically synthesized glycosulfopeptides representing N-terminal domains of human and murine P-selectin glycoprotein ligand-1 (PSGL-1), varying in sTyr and O-glycosylation (structure and site). Using these, we identified key roles of PSGL-1 O-glycosylation and sTyr in controlling interactions with specific chemokines. Results demonstrate that sTyr positively affects CCL19 and CCL21 binding to PSGL-1 N terminus, whereas O-glycan branching and sialylation reduced binding. For murine PSGL-1, interference between PTMs is greater, attributed to proximity between the two PTMs. Using fluorescence polarization, we found sTyr is a positive determinant for some chemokines. We showed that synthetic sulfopeptides are potent in decreasing chemotaxis of human dendritic cells toward CCL19 and CCL21. Our results provide new research avenues into the interplay of PTMs regulating leukocyte/chemokine interactions.

KW - CCL19

KW - CCL21

KW - CCL5

KW - chemokine

KW - glycosulfopeptides

KW - O-glycan

KW - P-selectin

KW - PSGL-1

KW - tyrosine sulfation

UR - http://www.scopus.com/inward/record.url?scp=85166244577&partnerID=8YFLogxK

U2 - 10.1016/j.chembiol.2023.06.013

DO - 10.1016/j.chembiol.2023.06.013

M3 - Journal article

C2 - 37463583

AN - SCOPUS:85166244577

VL - 30

SP - 893-905.e7

JO - Chemistry and Biology

JF - Chemistry and Biology

SN - 2451-9448

IS - 8

ER -

ID: 365961389

Biomedicinsk Institut