Helmerhorst E J, Maaskant J J, Appelmelk B J
Department of Oral Biochemistry, Vrije Universiteit, Amsterdam, The Netherlands.
Infect Immun. 1998 Feb;66(2):870-3. doi: 10.1128/IAI.66.2.870-873.1998.
This note describes the binding specificities of four lipid A monoclonal antibodies (MAbs) including Centoxin (HA-1A); these MAbs display similar binding properties. MAbs reacted with lipid A and heat-killed smooth bacteria, whereas no reactivity was observed with smooth lipopolysaccharide (LPS). Immunoblotting of bacterial extracts separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed that the MAbs bound to many polypeptide bands including the molecular weight markers. Denaturation of bovine serum albumin (BSA) by boiling or dithiothreitol treatment unmasked antibody epitopes. In addition, binding both to a hydrophobic aliphatic C12 chain covalently coupled to BSA and to single-stranded DNA was observed. The polyreactivity of these clones is most likely mediated by a preferential reactivity with hydrophobic molecular patches.
本笔记描述了四种脂多糖A单克隆抗体(MAb)的结合特异性,包括Centoxin(HA-1A);这些单克隆抗体表现出相似的结合特性。单克隆抗体与脂多糖A和热灭活的光滑型细菌发生反应,而与光滑型脂多糖(LPS)未观察到反应性。通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳分离的细菌提取物的免疫印迹显示,单克隆抗体与包括分子量标记物在内的许多多肽条带结合。通过煮沸或二硫苏糖醇处理使牛血清白蛋白(BSA)变性可暴露抗体表位。此外,还观察到与共价偶联到BSA的疏水性脂肪族C12链以及单链DNA的结合。这些克隆的多反应性很可能是由与疏水分子斑块的优先反应性介导的。