Hybridoma antibodies to the lipid-binding site(s) in the amino-terminal region of fibronectin inhibits binding of streptococcal lipoteichoic acid.
Hybridoma antibodies to the lipid-binding site(s) in the amino-terminal region of fibronectin inhibits binding of streptococcal lipoteichoic acid.
复制标题
针对纤连蛋白氨基末端区域中的脂质结合位点的杂交瘤抗体抑制链球菌脂磷壁酸的结合。
DOI：
10.1093/infdis/156.2.344
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发表时间：
1987
期刊：
影响因子：
--
通讯作者：
Ofek,I
中科院分区：
文献类型：
--
作者：
Stanislawski,L;Courtney,HS;Simpson,WA;Hasty,DL;Beachey,EH;Robert,L;Ofek,I
在本报告中，我们提出证据表明，链球菌和脂质胆酸（LTA）与位于纤维连接蛋白nh2端附近的脂肪酸结合位点相互作用。证据是基于以下观察。(1)针对合成肽（纤连蛋白氨基端残基1 - 30）的抗体与被链球菌吸附和洗脱的两个热溶菌素生成的肽（24和28千道尔顿[kDa]）反应。(2) LTA抑制了24-和28-kDa肽对链球菌的吸附。(3)抑制LTA与纤维连接蛋白结合的两种单克隆抗体仅与纤维连接蛋白的24- kda和28-kDA片段反应。(4)相反，LTA以及月桂酸和油酸可以阻断同一种单克隆抗体与纤维连接蛋白的结合。(5) LTA对针对胶原或细胞结合域的杂交瘤抗体结合无影响。
In this report, we present evidence to suggest that streptococci and lipoteichoic acid (LTA) interact with a fatty acid binding site located near the NH2-terminus of fibronectin. The evidence is based on the following observations. (1) Antibodies directed against a synthetic peptide (residues 1–30 of the amino-terminus of fibronectin) reacted with the two thermolysin-generated peptides (24 and 28 kilodaltons [kDa)) that were adsorbed by and eluted from streptococci. (2) The adsorption of the 24- and 28-kDa peptides to streptococci was inhibited by LTA. (3) The two monoclonal antibodies that inhibited the binding of LTA to fibronectin reacted only with the 24- and 28-kDA fragments of fibronectin. (4) Conversely, LTA, as well as lauric acid and oleic acid, blocked the binding of the same monoclonal antibodies to fibronectin. (5) LTA had no effect on the binding of hybridoma antibodies directed against the collagen or cell-binding domain.