000133511 001__ 133511
000133511 005__ 20181203021433.0
000133511 0247_ $$2doi$$a10.1016/S0014-5793(02)02274-3
000133511 037__ $$aARTICLE
000133511 245__ $$aThe glycan core of GPI-anchored proteins modulates aerolysin binidng but is not sufficient: the polypeptide moiety is required for the toxin-receptor interaction
000133511 269__ $$a2002
000133511 260__ $$c2002
000133511 336__ $$aJournal Articles
000133511 520__ $$aSensitivity of mammalian cells to the bacterial toxin aerolysin is due to the presence at their surface of glycosylphosphatidyl inositol (GPI)-anchored proteins which act as receptors. Using a panel of mutants that are affected in the GPI biosynthetic pathway and Trypanosoma brucei variant surface glycoproteins, we show that addition of an ethanolamine phosphate residue on the first mannose of the glycan core does not affect binding. In contrast, the addition of a side chain of up to four galactose residues at position 3 of this same mannose leads to an increase in binding. However, protein free GPIs, which accumulate in mutant cells deficient in the transamidase that transfers the protein to the pre-formed GPI-anchor, were unable to bind the toxin indicating a requirement for the polypeptide moiety, the nature and size of which seem of little importance although two exceptions have been identified.
000133511 700__ $$aAbrami, L.
000133511 700__ $$aVelluz, M.-C.
000133511 700__ $$aHong, H.
000133511 700__ $$aOhishi, K.
000133511 700__ $$aMehlert, A.
000133511 700__ $$aFerguson, M.
000133511 700__ $$aKinoshita, T.
000133511 700__ $$g171549$$avan der Goot, F.G.$$0240085
000133511 773__ $$j512$$tFEBS Lett$$k1-3$$q249-254
000133511 909C0 $$xU11271$$0252037$$pVDG
000133511 909CO $$pSV$$particle$$ooai:infoscience.tind.io:133511
000133511 917Z8 $$x148230
000133511 937__ $$aVDG-ARTICLE-2002-007
000133511 973__ $$rREVIEWED$$sPUBLISHED$$aOTHER
000133511 980__ $$aARTICLE