Recognition of an octapeptide sequence by multiple Gal alpha(1,3)Gal-binding proteins

被引：38

作者：

Vaughan, HA ^{[1
]}

Oldenburg, KR ^{[1
]}

Gallop, MA ^{[1
]}

Atkin, JD ^{[1
]}

McKenzie, IFC ^{[1
]}

Sandrin, MS ^{[1
]}

机构：

[1] AFFYMAX RES INST,PALO ALTO,CA

来源：

XENOTRANSPLANTATION | 1996年 / 3卷 / 01期

关键词：

Gal alpha(1,3)Gal; natural antibodies; peptide library; peptide surrogates;

D O I：

10.1111/j.1399-3089.1996.tb00114.x

中图分类号：

R-3 [医学研究方法]; R3 [基础医学];

学科分类号：

1001 ;

摘要：

Strategies are now being designed to overcome the hyperacute rejection of vascularized pig xenografts by human natural anti-Ga1 alpha(1,3)Gal antibodies. We now demonstrate that a synthetic octapeptide, Gal pep 1 (DAHWESWL), isolated from a peptide epitope library using the alpha-galactosyl specific lectin IB4, ''mimics'' the carbohydrate epitope Gal alpha(1,3)Gal. In vitro studies demonstrated that the binding of the IB4 lectin or human natural antibodies to pig cells could be specifically blocked by Gal pep 1, in several different serological assays: a) the hemagglutnation of pig erythrocytes; b) cytofluorographic analysis of pig lymphocytes and endothelial cells c) cytotoxicity of human serum against pig endoethelial cells; d) an ELISA assay. The relative affinity of the peptide for the IB4 lectin was similar to that of alpha-galactosyl sugars, although it was bound at a lower affinity by human antibodies. The implications of these observations to xenotransplantation are that peptides could theoretically be used to block hyperacute rejection,

引用

页码：18 / 23

页数：6

共 17 条

[1] INTERACTION BETWEEN HUMAN NATURAL ANTI-ALPHA-GALACTOSYL IMMUNOGLOBULIN-G AND BACTERIA OF THE HUMAN FLORA [J].