Interaction of a human blood group Sd (a-) Tamm- Horsfall glycoprotein with applied lectins

Journal/Book: FEBS Letters 384, 231-234. 1996;

Abstract: Unlike the human blood group Sd(a+) Tamm-Horsfall glycoprotein (THGP),the Sd(a-) one lacks terminal GalNAcbeta1--> residues at the nonreducingends. The binding properties of this glycoprotein and its asialo productwith lectins were characterized by quantitative precipitin (QPA) andprecipitin inhibition assays. Among 20 lectins tested by QPA, bothnative and asialo Sd(a-) THGP reacted best with Abrus precatorius andRicinus communis and completely precipitated the lectin added. They alsoprecipitated well Wistaria floribunda (WFA), Glycine max (SBA), Bauhiniapurpurea alba, abrin-a and ricin, all of which recognize the Galbeta1--> 4GlcNAcbeta1--> sequence, although at different strength. Thelectin-glycan interactions were inhibited by Galbeta1--> 4GlcNAc andGalbeta1--> 4Glc. When the precipitability of Sd(a-) THGP was comparedwith that of the Sd(a+) phenotype, the native Sd(a-) THGP exhibited a40% lesser affinity for WFA, SBA, WGA and mistletoe lectin-I (ML-I).Mapping the precipitation and inhibition profiles of the present studyand the results of THGP Sd(a+), it is concluded that Sd(a-) THGP showeda strongly diminished affinity for GalNAcbeta1--> active lectins (SBAand WFA) than the Sd(a+) phenotype. Author.

Keyword(s): ADJUVANTS-IMMUNOLOGIC/ME (metabolism)

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