SwePub
Sök i LIBRIS databas

  Utökad sökning

onr:"swepub:oai:DiVA.org:hh-48817"
 

Sökning: onr:"swepub:oai:DiVA.org:hh-48817" > Two monoclonal anti...

  • Xu, YuekangMonash University, Clayton, Australia (författare)

Two monoclonal antibodies to precisely the same epitope of type II collagen select non-crossreactive phage clones by phage display : Implications for autoimmunity and molecular mimicry

  • Artikel/kapitelEngelska2004

Förlag, utgivningsår, omfång ...

  • Oxford :Elsevier,2004
  • printrdacarrier

Nummerbeteckningar

  • LIBRIS-ID:oai:DiVA.org:hh-48817
  • https://urn.kb.se/resolve?urn=urn:nbn:se:hh:diva-48817URI
  • https://doi.org/10.1016/j.molimm.2004.03.025DOI
  • https://lup.lub.lu.se/record/274480URI

Kompletterande språkuppgifter

  • Språk:engelska
  • Sammanfattning på:engelska

Ingår i deldatabas

Klassifikation

  • Ämneskategori:ref swepub-contenttype
  • Ämneskategori:art swepub-publicationtype

Anmärkningar

  • Two monoclonal antibodies (mAb) CB268 and CII-C1 to type II collagen (CII) react with precisely the same conformational epitope constituted by the residues ARGLT on the three chains of the CII triple helix. The antibodies share structural similarity, with most differences in the complementarity determining region 3 of the heavy chain (HCDR3). The fine reactivity of these mAbs was investigated by screening two nonameric phage-displayed random peptide libraries. For each mAb, there were phage clones (phagotopes) that reacted strongly by ELISA only with the selecting mAb, and inhibited binding to CII only for that mAb, not the alternate mAb. Nonetheless, a synthetic peptide RRLPFGSQM corresponding to an insert from a highly reactive CII-C1-selected phagotope, which was unreactive (and non-inhibitory) with CB268, inhibited the reactivity of CB268 with CII. Most phage-displayed peptides contained a motif in the first part of the molecule that consisted of two basic residues adjacent to at least one hydrophobic residue (e.g. RRL or LRR), but the second portion of the peptides differed for the two mAbs. We predict that conserved CDR sequences interact with the basic-basic-hydrophobic motif, whereas non-conserved amino acids in the binding sites (especially HCDR3) interact with unique peptide sequences and limit cross-reactivity. The observation that two mAbs can react identically with a single epitope on one antigen (CII), but show no cross-reactivity when tested against a second (phagotope) indicates that microorganisms could exhibit mimics capable of initiating autoimmunity without this being evident from conventional assays. © 2004 Elsevier Ltd. All rights reserved.

Ämnesord och genrebeteckningar

Biuppslag (personer, institutioner, konferenser, titlar ...)

  • Ramsland, Paul A.Monash University, Parkville, Australia; Austin Research Institute, Heidelberg, Australia (författare)
  • Davies, Janet M.Monash University, Clayton, Australia (författare)
  • Scealy, MaritaMonash University, Clayton, Australia (författare)
  • Nandakumar, Kutty Selva,1965-Lund University, Lund, Sweden(Swepub:hh)kutnam (författare)
  • Holmdahl, RikardLund University,Lunds universitet,Immunologi,Forskargrupper vid Lunds universitet,Immunology,Lund University Research Groups,Lund University, Lund, Sweden(Swepub:lu)infl-rho (författare)
  • Rowley, Merrill J.Monash University, Clayton, Australia (författare)
  • Monash University, Clayton, AustraliaMonash University, Parkville, Australia; Austin Research Institute, Heidelberg, Australia (creator_code:org_t)

Sammanhörande titlar

  • Ingår i:Molecular ImmunologyOxford : Elsevier41:4, s. 411-4190161-58901872-9142

Internetlänk

Hitta via bibliotek

Till lärosätets databas

Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.

 
pil uppåt Stäng

Kopiera och spara länken för att återkomma till aktuell vy