دورية أكاديمية
VT68.2: An Antibody to Chondroitin Sulfate Proteoglycan 4 (CSPG4) Displays Reactivity against a Tumor-Associated Carbohydrate Antigen
العنوان: | VT68.2: An Antibody to Chondroitin Sulfate Proteoglycan 4 (CSPG4) Displays Reactivity against a Tumor-Associated Carbohydrate Antigen |
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المؤلفون: | Bernice Nounamo, Fariba Jousheghany, Eric Robb Siegel, Steven R. Post, Thomas Kelly, Soldano Ferrone, Thomas Kieber-Emmons, Behjatolah Monzavi-Karbassi |
المصدر: | International Journal of Molecular Sciences, Vol 24, Iss 3, p 2506 (2023) |
بيانات النشر: | MDPI AG, 2023. |
سنة النشر: | 2023 |
المجموعة: | LCC:Biology (General) LCC:Chemistry |
مصطلحات موضوعية: | CSPG4, TACAs, breast cancer, carbohydrate-mimicking peptide, Biology (General), QH301-705.5, Chemistry, QD1-999 |
الوصف: | The anti-CSPG4 monoclonal antibodies (mAbs) have shown anti-tumor activity and therapeutic potential for treating breast cancer. In addition, CSPG4 is a dominant tumor-associated antigen that is also involved in normal-tissue development in humans. Therefore, the potential for off-tumor activity remains a serious concern when targeting CSPG4 therapeutically. Previous work suggested that glycans contribute to the binding of specific anti-CSPG4 antibodies to tumor cells, but the specificity and importance of this contribution are unknown. In this study, the reactivity of anti-CSPG4 mAbs was characterized with a peptide mimetic of carbohydrate antigens expressed in breast cancer. ELISA, flow cytometry, and microarray assays were used to screen mAbs for their ability to bind to carbohydrate-mimicking peptides (CMPs), cancer cells, and glycans. The mAb VT68.2 displayed a distinctly strong binding to a CMP (P10s) and bound to triple-negative breast cancer cells. In addition, VT68.2 showed a higher affinity for N-linked glycans that contain terminal fucose and fucosylated lactosamines. The functional assays demonstrated that VT68.2 inhibited cancer cell migration. These results define the glycoform reactivity of an anti-CSPG4 antibody and may lead to the development of less toxic therapeutic approaches that target tumor-specific glyco-peptides. |
نوع الوثيقة: | article |
وصف الملف: | electronic resource |
اللغة: | English |
تدمد: | 24032506 1422-0067 1661-6596 |
Relation: | https://www.mdpi.com/1422-0067/24/3/2506; https://doaj.org/toc/1661-6596; https://doaj.org/toc/1422-0067 |
DOI: | 10.3390/ijms24032506 |
URL الوصول: | https://doaj.org/article/c18a9b4548914dad8796d2fc841c5fd0 |
رقم الأكسشن: | edsdoj.18a9b4548914dad8796d2fc841c5fd0 |
قاعدة البيانات: | Directory of Open Access Journals |
تدمد: | 24032506 14220067 16616596 |
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DOI: | 10.3390/ijms24032506 |