作者: P Pieroni , E A Worobec , W Paranchych , G D Armstrong
DOI: 10.1128/IAI.56.5.1334-1340.1988
关键词:
摘要: We have identified a receptor for colonization factor antigen I (CFA/I) pili in human erythrocyte membranes. Erythrocyte binding assays, using whole organisms, suggested that the CFA/I was glycoprotein containing important sialic acid moieties. Subsequently, membranes were extracted with lithium diiodosalicylate to obtain soluble fraction from which isolate receptors. The material caused agglutination of CFA/I+ but not CFA/I- organisms at protein concentration 0.5 mg/ml. iodinated extract by an affinity isolation procedure, bacterial cells. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography washed, extract-coated H10407 revealed band apparent molecular weight 26,000 present original observed on bacteria. addition purified reduced 26,000-molecular-weight CFA/I-specific species also bound wheat germ agglutinin-agarose. This observation supported suggestion this report is sialoglycoprotein.