Deciphering the complex three-way interaction between the non-integrin laminin receptor, galectin-3 and Neisseria meningitidis

Basit Öğe Kaydı
dc.contributor.authorAlqahtani, Fulwah
dc.contributor.authorMahdavi, Jafar
dc.contributor.authorWheldon, Lee M.
dc.contributor.authorVassey, Matthew
dc.contributor.authorPirinccioglu, Necmettin
dc.contributor.authorRoyer, Pierre-Joseph
dc.contributor.authorQarani, Suzan M.
dc.date.accessioned2024-04-24T17:08:37Z
dc.date.available2024-04-24T17:08:37Z
dc.date.issued2014
dc.departmentDicle Üniversitesien_US
dc.description.abstractThe non-integrin laminin receptor (LAMR1/RPSA) and galectin-3 (Gal-3) are multi-functional host molecules with roles in diverse pathological processes, particularly of infectious or oncogenic origins. Using bimolecular fluorescence complementation and confocal imaging, we demonstrate that the two proteins homo-and heterodimerize, and that each isotype forms a distinct cell surface population. We present evidence that the 37 kDa form of LAMR1 (37LRP) is the precursor of the previously described 67 kDa laminin receptor (67LR), whereas the heterodimer represents an entity that is distinct from this molecule. Site-directed mutagenesis confirmed that the single cysteine (C-173) of Gal-3 or lysine (K-166) of LAMR1 are critical for heterodimerization. Recombinant Gal-3, expressed in normally Gal-3-deficient N2a cells, dimerized with endogenous LAMR1 and led to a significantly increased number of internalized bacteria (Neisseria meningitidis), confirming the role of Gal-3 in bacterial invasion. Contact- dependent cross-linking determined that, in common with LAMR1, Gal-3 binds the meningococcal secretin PilQ, in addition to the major pilin PilE. This study adds significant new mechanistic insights into the bacterial-host cell interaction by clarifying the nature, role and bacterial ligands of LAMR1 and Gal-3 isotypes during colonization.en_US
dc.description.sponsorshipMedical Research Council, UK [G0801173]; Medical Research Council [G0801173] Funding Source: researchfish; MRC [G0801173] Funding Source: UKRIen_US
dc.description.sponsorshipThis project was part supported by a grant (G0801173) from the Medical Research Council, UK.en_US
dc.identifier.doi10.1098/rsob.140053
dc.identifier.issn2046-2441
dc.identifier.issue10en_US
dc.identifier.pmid25274119
dc.identifier.scopus2-s2.0-84923677317
dc.identifier.scopusqualityQ1
dc.identifier.urihttps://doi.org/10.1098/rsob.140053
dc.identifier.urihttps://hdl.handle.net/11468/17401
dc.identifier.volume4en_US
dc.identifier.wosWOS:000347899600002
dc.identifier.wosqualityQ1
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.language.isoenen_US
dc.publisherRoyal Socen_US
dc.relation.ispartofOpen Biology
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectLamr1en_US
dc.subjectRpsaen_US
dc.subjectGalectin-3en_US
dc.subject37lrpen_US
dc.subject67lren_US
dc.subjectNeisseria Meningitidisen_US
dc.titleDeciphering the complex three-way interaction between the non-integrin laminin receptor, galectin-3 and Neisseria meningitidisen_US
dc.titleDeciphering the complex three-way interaction between the non-integrin laminin receptor, galectin-3 and Neisseria meningitidis
dc.typeArticleen_US

Dosyalar

Koleksiyon

WoS İndeksli Yayınlar Koleksiyonu
PubMed İndeksli Yayın Koleksiyonu
Scopus İndeksli Yayınlar Koleksiyonu