A lectin recognizes differential arrangements of O-glycans on mucin repeats

TY - JOUR

T1 - A lectin recognizes differential arrangements of O-glycans on mucin repeats

AU - Kato, Kentaro

AU - Takeuchi, Hideyuki

AU - Ohki, Takao

AU - Waki, Michihiko

AU - Usami, Katsuaki

AU - Hassan, Helle

AU - Clausen, Henrik

AU - Irimura, Tatsuro

N1 - Keywords: Acetylgalactosamine; Amino Acid Sequence; Glycopeptides; Humans; Molecular Sequence Data; Mucin-2; Mucins; Plant Lectins; Polysaccharides; Repetitive Sequences, Amino Acid; Surface Plasmon Resonance

PY - 2008

Y1 - 2008

N2 - Interaction of Vicia villosa agglutinin-B4 (VVA-B4) to glycopeptides with O-linked GalNAc residues was investigated by surface plasmon resonance. The affinity was shown to be influenced by the arrangement of O-glycosylation sites on a peptide, PTTTPITTTTK, representing the tandem repeat of MUC2. The association rate constant was relatively high with a particular category of GalNAc-peptides in which more than three amino acid residues were placed between GalNAc-Thr residues. PTT( *)T( *)PITT( *)T( *)TK (T( *) indicates GalNAc-Thr) had the highest association rate constant among the glycopeptides tested. The dissociation rate constant was low in the peptides containing consecutive GalNAc residues and PT( *)TTPIT( *)T( *)T( *)TK was the lowest of the glycopeptides tested. Dissociation constant (K(D)), calculated as k(d)/k(a) was the lowest with PTT( *)T( *)PITT( *)T( *)TK. Therefore, the arrangement but not the quantity of GalNAc residues apparently determines the affinity between VVA-B4 and peptides with attached GalNAc residues.

AB - Interaction of Vicia villosa agglutinin-B4 (VVA-B4) to glycopeptides with O-linked GalNAc residues was investigated by surface plasmon resonance. The affinity was shown to be influenced by the arrangement of O-glycosylation sites on a peptide, PTTTPITTTTK, representing the tandem repeat of MUC2. The association rate constant was relatively high with a particular category of GalNAc-peptides in which more than three amino acid residues were placed between GalNAc-Thr residues. PTT( *)T( *)PITT( *)T( *)TK (T( *) indicates GalNAc-Thr) had the highest association rate constant among the glycopeptides tested. The dissociation rate constant was low in the peptides containing consecutive GalNAc residues and PT( *)TTPIT( *)T( *)T( *)TK was the lowest of the glycopeptides tested. Dissociation constant (K(D)), calculated as k(d)/k(a) was the lowest with PTT( *)T( *)PITT( *)T( *)TK. Therefore, the arrangement but not the quantity of GalNAc residues apparently determines the affinity between VVA-B4 and peptides with attached GalNAc residues.

U2 - 10.1016/j.bbrc.2008.04.120

DO - 10.1016/j.bbrc.2008.04.120

M3 - Journal article

C2 - 18455506

SN - 0006-291X

VL - 371

SP - 698

EP - 701

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 4

ER -