Abstract 609: Overcoming host histocompatibility barrier to create a renewable source of off-the-shelf effector lymphocytes for adoptive immunotherapy
Abstract 609: Overcoming host histocompatibility barrier to create a renewable source of off-the-shelf effector lymphocytes for adoptive immunotherapy
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DOI：
10.1158/1538-7445.am2017-609
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发表时间：
2017-07
期刊：
影响因子：
11.2
通讯作者：
Raedun Clarke;Matthieu Bauer;R. Bjordahl;Jeffrey Sasaki;Brian C. Groff;S. Gaidarova;Tom Tong Lee;Weijie Lan;M. Burrascano;Ramzey Abujarour;G. Bonello;Megan Robinson;Stewart Abbot;Scott Wolchko;Daniel Shoemaker;Bob Valamehr
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文献类型：
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作者：
Raedun Clarke;Matthieu Bauer;R. Bjordahl;Jeffrey Sasaki;Brian C. Groff;S. Gaidarova;Tom Tong Lee;Weijie Lan;M. Burrascano;Ramzey Abujarour;G. Bonello;Megan Robinson;Stewart Abbot;Scott Wolchko;Daniel Shoemaker;Bob Valamehr
使用代表II型胶原的CB-11肽的氨基酸序列的272个短的合成肽的表位扫描，我们已经表明，用II型胶原免疫的五种大鼠产生针对CB-11肽的氨基末端的37 - 45个氨基酸的区域的抗体。该区域的抗体总是给出最高的结合值，表明它是免疫显性区域。用代表该区域的合成肽与钥孔血蓝蛋白偶联免疫的Wistar大鼠产生了针对该肽的抗体，该抗体在1：4000至1：8000稀释度下仍可检测到，但均未发生临床关节炎。所有血清也显示结合变性牛II型胶原蛋白的抗体，但不自然的II型胶原蛋白，匙孔血蓝蛋白或牛血清白蛋白的ELISA。检测了来自肽免疫大鼠的血清中与CB-11肽的272个短肽和代表免疫显性区的缩短形式及其具有取代氨基酸的形式的合成肽的抗体结合。这些结果表明，肽免疫大鼠中的抗体与用II型胶原免疫的大鼠产生的抗体不同，但可能代表它们的亚群。这些发现表明，在解释关节炎诱导中单个肽的抗体的作用时要谨慎，而不知道它们的精细特异性。
Using epitope scanning of 272 short, synthetic peptides representing the amino acid sequence of the CB-11 peptide of type II collagen, we have shown that five strains of rat, immunized with type II collagen, produce antibodies to a region 37-45 amino acids from the amino end of CB-11 peptide. Antibodies to this region always gave the highest binding values suggesting that it is an immunodominant region. Wistar rats immunized with a synthetic peptide representing this region, coupled to keyhole limpet haemocyanin, produced antibodies to this peptide which could still be detected at 1:4000 to 1:8000 dilution but none developed clinical arthritis. All sera also showed binding of antibodies to denatured bovine type II collagen but not to native type II collagen, keyhole limpet haemocyanin or to bovine serum albumin by ELISA. Sera from peptide-immunized rats were examined for antibody binding to the 272 short peptides of the CB-11 peptide and to the synthetic peptides representing shortened forms of the immunodominant region and forms of it with substituted amino acids. These results showed that the antibodies in the peptide-immunized rats were not identical to those produced to that peptide by rats immunized with type II collagen but may represent subpopulations of them. These findings suggest caution in interpreting the role of antibodies to individual peptides in arthritis induction without knowledge of their fine specificity.