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Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods
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VSIG4 interaction with heparan sulfates inhibits VSIG4-complement binding.

Sarah Y Ebstein1, Ashique Rafique1, Yi Zhou1

  • 1Regeneron Pharmaceuticals, 777 Old Saw Mill River Road, Tarrytown, NY 10591, United States.

Glycobiology
|June 21, 2023
PubMed
Summary
This summary is machine-generated.

V-set and immunoglobulin domain-containing 4 (VSIG4), a macrophage immune regulator, binds to heparan sulfates. This interaction competes with complement proteins, revealing a new mechanism for VSIG4

Keywords:
VSIG4complementglycosaminoglycanheparan sulfateheparin-binding-protein

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Area of Science:

  • Immunology
  • Molecular Biology
  • Glycobiology

Background:

  • V-set and immunoglobulin domain-containing 4 (VSIG4) is a complement receptor on tissue-resident macrophages with diverse immune functions.
  • The precise mechanisms underlying VSIG4's context-dependent immune regulation are not fully understood.

Purpose of the Study:

  • To identify novel binding partners of VSIG4.
  • To elucidate the role of these interactions in VSIG4-mediated immune modulation.

Main Methods:

  • Genetic deletion of heparan sulfate synthesis enzymes.
  • Enzymatic cleavage of cell-surface heparan sulfates.
  • Binding assays to assess VSIG4-heparan sulfate interactions.
  • Mutagenesis studies to identify binding epitopes.
  • Competition assays with complement proteins C3b and iC3b.

Main Results:

  • Heparan sulfates (HS) were identified as novel binding partners for VSIG4.
  • VSIG4 binding to cell surfaces was reduced by disrupting HS synthesis or presence.
  • VSIG4 directly binds to HS, showing a preference for highly sulfated and longer chains.
  • HS competes with C3b and iC3b for VSIG4 binding at overlapping epitopes.

Conclusions:

  • Heparan sulfates represent a novel class of VSIG4 binding partners.
  • HS binding modulates VSIG4 interaction with complement proteins.
  • This discovery suggests a new mechanism for heparan sulfate-mediated regulation of VSIG4 immune functions.