Abstract:
:During inflammatory response, blood leukocytes adhere to the endothelium. This process involves numerous adhesion molecules, including a transmembrane chemokine, CX3CL1, which behaves as a molecular cluster. How this cluster assembles and whether this association has a functional role remain unknown. The analysis of CX3CL1 clusters using native electrophoresis and single molecule fluorescence kinetics shows that CX3CL1 is a homo-oligomer of 3 to 7 monomers. Fluorescence recovery after photobleaching assays reveal that the CX3CL1-transmembrane domain peptide self-associates in both cellular and acellular lipid environments, while its random counterpart (i.e. peptide with the same residues in a different order) does not. This strongly indicates that CX3CL1 oligomerization is driven by its intrinsic properties. According to the molecular modeling, CX3CL1 does not associate in compact bundles but rather with monomers linearly assembled side by side. Finally, the CX3CL1 transmembrane peptide inhibits both the CX3CL1 oligomerization and the adhesive function, while its random counterpart does not. This demonstrates that CX3CL1 oligomerization is mandatory for its adhesive potency. Our results provide a new direction to control CX3CL1-dependent cellular adherence in key immune processes.
journal_name
Sci Repjournal_title
Scientific reportsauthors
Ostuni MA,Hermand P,Saindoy E,Guillou N,Guellec J,Coens A,Hattab C,Desuzinges-Mandon E,Jawhari A,Iatmanen-Harbi S,Lequin O,Fuchs P,Lacapere JJ,Combadière C,Pincet F,Deterre Pdoi
10.1038/s41598-020-65988-wsubject
Has Abstractpub_date
2020-06-03 00:00:00pages
9069issue
1issn
2045-2322pii
10.1038/s41598-020-65988-wjournal_volume
10pub_type
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