The Quest for Anticancer Vaccines: Deciphering the Fine-Epitope Specificity of Cancer-Related Monoclonal Antibodies by Combining Microarray Screening and Saturation Transfer Difference NMR

Helena Coelho; Takahiko Matsushita; Gerard Artigas; Hiroshi Hinou; F. Javier Canada; Richard Lo-Man; Claude Leclerc; Eurico J. Cabrita; Jesus Jimenez-Barbero; Shin-Ichiro Nishimura; Fayna Garcia-Martin; Filipa Marcelo

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The Quest for Anticancer Vaccines: Deciphering the Fine-Epitope Specificity of Cancer-Related Monoclonal Antibodies by Combining Microarray Screening and Saturation Transfer Difference NMR

机译：寻求抗癌疫苗：通过结合微阵列筛选和饱和转移差异NMR破译与癌症相关的单克隆抗体的精细表位特异性

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The identification of MUC1 tumor-associated Tn antigen (αGalpNAc1-O-Ser/Thr) has boosted the development of anticancer vaccines. Combining micro-arrays and saturation transfer difference NMR, we have characterized the fine-epitope mapping of a MUC1 chemical library (naked and Tn-glycosylated) toward two families of cancer-related monoclonal antibodies (anti-MUC1 and anti-Tn mAbs). Anti-MUC1 mAbs clone VU-3C6 and VU-11E2 recognize naked MUC1-derived peptides and bind GalNAc in a peptide-sequence-depend-ent manner. In contrast, anti-Tn mAbs done 8D4 and 14D6 mostly recognize the GalNAc and do not bind naked MUC1-derived peptides. These anti-Tn mAbs show a clear preference for glycopeptides containing the Tn-Ser antigen rather than the Tn-Thr analogue, stressing the role of the underlying amino acid (serine or threonine) in the binding process. The reported strategy can be employed, in general, to unveil the key minimal structural features that modulate antigen-antibody recognition, with particular relevance for the development of Tn-MUC1-based anticancer vaccines.

机译：MUC1肿瘤相关Tn抗原（αGalpNAc1-O-Ser/ Thr）的鉴定促进了抗癌疫苗的开发。结合微阵列和饱和转移差异NMR，我们已经表征了MUC1化学文库（裸和Tn-糖基化）向两个与癌症相关的单克隆抗体（抗MUC1和抗Tn mAb）的精细表位作图。抗MUC1 mAb克隆VU-3C6和VU-11E2识别裸MUC1衍生的肽并以肽序列依赖性方式结合GalNAc。相反，在8D4和14D6中完成的抗Tn单抗大多识别GalNAc，并且不结合裸MUC1衍生的肽。这些抗Tn mAb表现出对包含Tn-Ser抗原而不是Tn-Thr类似物的糖肽的明显偏好，从而强调了潜在氨基酸（丝氨酸或苏氨酸）在结合过程中的作用。一般而言，可以使用已报道的策略揭示调节抗原-抗体识别的关键最小结构特征，特别是与开发基于Tn-MUC1的抗癌疫苗有关。

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来源
《Journal of the American Chemical Society》 |2015年第39期|12438-12441|共4页
作者
Helena Coelho; Takahiko Matsushita; Gerard Artigas; Hiroshi Hinou; F. Javier Canada; Richard Lo-Man; Claude Leclerc; Eurico J. Cabrita; Jesus Jimenez-Barbero; Shin-Ichiro Nishimura; Fayna Garcia-Martin; Filipa Marcelo;
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作者单位

UCIBIO, REQUIMTE, Departamento de Quimica, Faculdade de Ciencias e Tecnologia, Universidade Nova de Lisboa, 2829-516 Caparica, Portugal;

Faculty of Advanced Life Science and Graduate School of Life Science, Hokkaido University, Kita-ku, Sapporo 001-0021, Japan;

Faculty of Advanced Life Science and Graduate School of Life Science, Hokkaido University, Kita-ku, Sapporo 001-0021, Japan;

Faculty of Advanced Life Science and Graduate School of Life Science, Hokkaido University, Kita-ku, Sapporo 001-0021, Japan;

Centro de Investigaciones Biologicas, CIB-CSIC, 28040 Madrid, Spain;

Unite de Regulation Immunitaire et Vaccinologie, Equipe Labellisee Ligue Contre le Cancer, Paris, Institut Pasteur, 75724 Paris Cedex 15, France,INSERM U1041, 75724 Paris Cedex 15, France;

Unite de Regulation Immunitaire et Vaccinologie, Equipe Labellisee Ligue Contre le Cancer, Paris, Institut Pasteur, 75724 Paris Cedex 15, France,INSERM U1041, 75724 Paris Cedex 15, France;

UCIBIO, REQUIMTE, Departamento de Quimica, Faculdade de Ciencias e Tecnologia, Universidade Nova de Lisboa, 2829-516 Caparica, Portugal;

CIC bioGUNE Bizkaia, 48160 Derio, Spain,Ikerbasque, Basque Foundation for Science, 48005 Bilbao, Spain;

Faculty of Advanced Life Science and Graduate School of Life Science, Hokkaido University, Kita-ku, Sapporo 001-0021, Japan;

Faculty of Advanced Life Science and Graduate School of Life Science, Hokkaido University, Kita-ku, Sapporo 001-0021, Japan;

UCIBIO, REQUIMTE, Departamento de Quimica, Faculdade de Ciencias e Tecnologia, Universidade Nova de Lisboa, 2829-516 Caparica, Portugal;

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收录信息美国《科学引文索引》(SCI);美国《工程索引》(EI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
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The Quest for Anticancer Vaccines: Deciphering the Fine-Epitope Specificity of Cancer-Related Monoclonal Antibodies by Combining Microarray Screening and Saturation Transfer Difference NMR

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