Lectin interactions with alpha-galactosylated xenoantigens

Svend Kirkeby; Dennis Moe

Lectin interactions with alpha-galactosylated xenoantigens

Svend Kirkeby, Dennis Moe

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

15 Citationer (Scopus)

Abstract

Udgivelsesdato: 2002-Jul

Originalsprog	Engelsk
Tidsskrift	Xenotransplantation
Vol/bind	9
Udgave nummer	4
Sider (fra-til)	260-7
Antal sider	7
ISSN	0908-665X
Status	Udgivet - 2002

Bibliografisk note

Keywords: Animals; Antigens, Heterophile; Carbohydrate Sequence; Disaccharides; Enzyme-Linked Immunosorbent Assay; Epitopes; Galactosides; Glycoproteins; Lectins; Molecular Sequence Data; Oligosaccharides; Primates; Swine

Citationsformater

@article{d0e66030eed011ddbf70000ea68e967b,

title = "Lectin interactions with alpha-galactosylated xenoantigens",

abstract = "alpha-Galactosylated xenoantigens (Galalpha1-3Galbeta1-4GlcNAcbeta1 and Galalpha1-3Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc) are often detected with the alpha-Gal specific lectin Griffonia simplicifolia 1 isolectin B4 (GS1 B4). However, this lectin exhibits a broad and variable specificity for carbohydrates terminating in alpha-Gal. Thus, both false positive and false negative results may occur when GS1 B4 is used to determine natural antigens in xeno (pig-to-primate) transplantation research. To refine the tools for detecting alpha-galactosylated antigens we have studied the binding of various alpha-galactophilic lectins to alpha-galactosylated neoglycoproteins. The lectins were: Euonymus europaeus agglutinin (EEA), Griffonia simplicifolia 1 isolectin B4 (GS1 B4), Maclura pomifera agglutinin (MPA) and Pseudomonas aeruginosa agglutinin (PA-IL). Although both GS1 B4 and MPA strongly bound glycoconjugates terminating in Gal there seems to be some differentiation in their sugar binding preferences. MPA was the only lectin that showed high affinity for the pentasaccharide Galalpha1-3Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc and for the Galalpha-glycans on non-primate thyroglobulin. The length of the xenoantigenic carbohydrate chain may influence the nature of the inhibition when a simple sugar is used to inhibit GS1 B4 binding to the xenoantigen. Inhibition studies of MPA GS1 B4 interaction further suggest that both lectins attach to the same site of the carbohydrate antigen and that GS1 B4 in addition binds to at least one other site that has no affinity for MPA. When lectins are used for recognition and investigation of natural Galalpha-antigens, we propose that GS1 B4 and MPA should accompany each other.",

author = "Svend Kirkeby and Dennis Moe",

note = "Keywords: Animals; Antigens, Heterophile; Carbohydrate Sequence; Disaccharides; Enzyme-Linked Immunosorbent Assay; Epitopes; Galactosides; Glycoproteins; Lectins; Molecular Sequence Data; Oligosaccharides; Primates; Swine",

year = "2002",

language = "English",

volume = "9",

pages = "260--7",

journal = "Xenotransplantation",

issn = "0908-665X",

publisher = "Wiley-Blackwell",

number = "4",

}

TY - JOUR

T1 - Lectin interactions with alpha-galactosylated xenoantigens

AU - Kirkeby, Svend

AU - Moe, Dennis

N1 - Keywords: Animals; Antigens, Heterophile; Carbohydrate Sequence; Disaccharides; Enzyme-Linked Immunosorbent Assay; Epitopes; Galactosides; Glycoproteins; Lectins; Molecular Sequence Data; Oligosaccharides; Primates; Swine

PY - 2002

Y1 - 2002

N2 - alpha-Galactosylated xenoantigens (Galalpha1-3Galbeta1-4GlcNAcbeta1 and Galalpha1-3Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc) are often detected with the alpha-Gal specific lectin Griffonia simplicifolia 1 isolectin B4 (GS1 B4). However, this lectin exhibits a broad and variable specificity for carbohydrates terminating in alpha-Gal. Thus, both false positive and false negative results may occur when GS1 B4 is used to determine natural antigens in xeno (pig-to-primate) transplantation research. To refine the tools for detecting alpha-galactosylated antigens we have studied the binding of various alpha-galactophilic lectins to alpha-galactosylated neoglycoproteins. The lectins were: Euonymus europaeus agglutinin (EEA), Griffonia simplicifolia 1 isolectin B4 (GS1 B4), Maclura pomifera agglutinin (MPA) and Pseudomonas aeruginosa agglutinin (PA-IL). Although both GS1 B4 and MPA strongly bound glycoconjugates terminating in Gal there seems to be some differentiation in their sugar binding preferences. MPA was the only lectin that showed high affinity for the pentasaccharide Galalpha1-3Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc and for the Galalpha-glycans on non-primate thyroglobulin. The length of the xenoantigenic carbohydrate chain may influence the nature of the inhibition when a simple sugar is used to inhibit GS1 B4 binding to the xenoantigen. Inhibition studies of MPA GS1 B4 interaction further suggest that both lectins attach to the same site of the carbohydrate antigen and that GS1 B4 in addition binds to at least one other site that has no affinity for MPA. When lectins are used for recognition and investigation of natural Galalpha-antigens, we propose that GS1 B4 and MPA should accompany each other.

AB - alpha-Galactosylated xenoantigens (Galalpha1-3Galbeta1-4GlcNAcbeta1 and Galalpha1-3Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc) are often detected with the alpha-Gal specific lectin Griffonia simplicifolia 1 isolectin B4 (GS1 B4). However, this lectin exhibits a broad and variable specificity for carbohydrates terminating in alpha-Gal. Thus, both false positive and false negative results may occur when GS1 B4 is used to determine natural antigens in xeno (pig-to-primate) transplantation research. To refine the tools for detecting alpha-galactosylated antigens we have studied the binding of various alpha-galactophilic lectins to alpha-galactosylated neoglycoproteins. The lectins were: Euonymus europaeus agglutinin (EEA), Griffonia simplicifolia 1 isolectin B4 (GS1 B4), Maclura pomifera agglutinin (MPA) and Pseudomonas aeruginosa agglutinin (PA-IL). Although both GS1 B4 and MPA strongly bound glycoconjugates terminating in Gal there seems to be some differentiation in their sugar binding preferences. MPA was the only lectin that showed high affinity for the pentasaccharide Galalpha1-3Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc and for the Galalpha-glycans on non-primate thyroglobulin. The length of the xenoantigenic carbohydrate chain may influence the nature of the inhibition when a simple sugar is used to inhibit GS1 B4 binding to the xenoantigen. Inhibition studies of MPA GS1 B4 interaction further suggest that both lectins attach to the same site of the carbohydrate antigen and that GS1 B4 in addition binds to at least one other site that has no affinity for MPA. When lectins are used for recognition and investigation of natural Galalpha-antigens, we propose that GS1 B4 and MPA should accompany each other.

M3 - Journal article

C2 - 12060462

SN - 0908-665X

VL - 9

SP - 260

EP - 267

JO - Xenotransplantation

JF - Xenotransplantation

IS - 4

ER -