Close Association of the First and Fourth Extracellular Domains of the Duffy Antigen/Receptor for Chemokines by a Disulfide Bond Is Required for Ligand Binding

Tournamille, Christophe; Kim, Caroline Le Van; Gane, Pierre; Blanchard, Dominique; Proudfoot, Amanda E. I.; Cartron, Jean Pierre; Colin, Yves

doi:10.1074/jbc.272.26.16274

Cited by 67 publications

(57 citation statements)

References 36 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…In addition, the epitopes for inhibitory mAbs 2D10, 2H2, and 2C6 in SD3 suggest that a secondary receptor-binding event may occur between DARC and DBP-II outside of previously identified primary DARC-binding sites in SD2 (18,19). The tail end of SD3 may contact extracellular loops linking the seven transmembrane regions of DARC that may play a role in DBP binding (51).…”

Section: Discussionmentioning

confidence: 99%

Broadly neutralizing epitopes in the Plasmodium vivax vaccine candidate Duffy Binding Protein

Chen

Salinas

Huang

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

129

View full text Add to dashboard Cite

Plasmodium vivax Duffy Binding Protein (PvDBP) is the most promising vaccine candidate for P. vivax malaria. The polymorphic nature of PvDBP induces strain-specific immune responses, however, and the epitopes of broadly neutralizing antibodies are unknown. These features hamper the rational design of potent DBP-based vaccines and necessitate the identification of globally conserved epitopes. Using X-ray crystallography, small-angle X-ray scattering, hydrogen-deuterium exchange mass spectrometry, and mutational mapping, we have defined epitopes for three inhibitory mAbs (mAbs 2D10, 2H2, and 2C6) and one noninhibitory mAb (3D10) that engage DBP. These studies expand the currently known inhibitory epitope repertoire by establishing protective motifs in subdomain three outside the receptor-binding and dimerization residues of DBP, and introduce globally conserved protective targets. All of the epitopes are highly conserved among DBP alleles. The identification of broadly conserved epitopes of inhibitory antibodies provides critical motifs that should be retained in the next generation of potent vaccines for P. vivax malaria.

show abstract

Section: Discussionmentioning

confidence: 99%

Broadly neutralizing epitopes in the Plasmodium vivax vaccine candidate Duffy Binding Protein

Chen

Salinas

Huang

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

129

View full text Add to dashboard Cite

show abstract

“…Our preliminary studies show that CXCL4 displaces histones from the DNA within neutrophil extravascular traps, which may injure the pulmonary vasculature and the adjacent epithelial barrier (53,54). Alternatively, binding of CXCL4 to cell-surface glycosaminoglycans (55) might compete with CXCL7, CXCL5, and other CXC chemokines for binding to Duffy antigen/receptor for chemokines (56), thereby impairing their removal from sites of inflammation (22). This model would be consistent with the reported role of CXCL5 in ALI (34) and would help explain how overexpression of CXCL4 can substitute for the absence of CXCL7, notwithstanding the differences in their effects on attracting and activating neutrophils to the injured lung.…”

Section: /Cxcl7mentioning

confidence: 99%

Platelet-Specific Chemokines Contribute to the Pathogenesis of Acute Lung Injury

Bdeir¹,

Gollomp²,

Stasiak

et al. 2017

Am J Respir Cell Mol Biol

View full text Add to dashboard Cite

Platelets and neutrophils contribute to the development of acute lung injury (ALI). However, the mechanism by which platelets make this contribution is incompletely understood. We investigated whether the two most abundant platelet chemokines, CXCL7, which induces neutrophil chemotaxis and activation, and CXCL4, which does neither, mediate ALI through complementary pathogenic pathways. To examine the role of platelet-derived chemokines in the pathogenesis of ALI using Cxcl7 2/2 and Cxcl4 2/2 knockout mice and mice that express human CXCL7 or CXCL4, we measured levels of chemokines in these mice. ALI was then induced by acid aspiration, and the severity of injury was evaluated by histology and by the presence of neutrophils and protein in the bronchoalveolar lavage fluid. Pulmonary vascular permeability was studied in vivo by measuring extravasation of fluorescently labeled dextran. Murine CXCL7, both recombinant and native protein released from platelets, can be N-terminally processed by cathepsin G to yield a biologically active CXCL7 fragment. Although Cxcl7 2/2 mice are protected from lung injury through the preservation of endothelial/epithelial barrier function combined with impaired neutrophils transmigration, Cxcl4 2/2 mice are protected through improved barrier function without affecting neutrophils transmigration to the airways. Sensitivity to ALI is restored by transgenic expression of CXCL7 or CXCL4. Platelet-derived CXCL7 and CXCL4 contribute to the pathogenesis of ALI through complementary effects on neutrophil chemotaxis and through activation and vascular permeability.

show abstract

“…Affinities with DARC natural ligand, CXCL8, and different antibodies [33,[51][52][53][54][55][56][57][58] confirmed predictions made about DARC topology [59]. This transmembrane protein as bona fide GPCR has 7 transmembrane segments with four extracellular loops (named Extra Cellular Domains or ECDs) and four intracellular loops (named Intra Cellular Domains or ICDs).…”

Section: The Different Aspects Of the Researchmentioning

confidence: 80%

Multiple interests in structural models of DARC transmembrane protein

Smolarek

Bertrand

Czerwiński

et al. 2010

Transfusion Clinique et Biologique

View full text Add to dashboard Cite

Close Association of the First and Fourth Extracellular Domains of the Duffy Antigen/Receptor for Chemokines by a Disulfide Bond Is Required for Ligand Binding

Cited by 67 publications

References 36 publications

Broadly neutralizing epitopes in the Plasmodium vivax vaccine candidate Duffy Binding Protein

Broadly neutralizing epitopes in the Plasmodium vivax vaccine candidate Duffy Binding Protein

Platelet-Specific Chemokines Contribute to the Pathogenesis of Acute Lung Injury

Multiple interests in structural models of DARC transmembrane protein

Contact Info

Product

Resources

About