Antibody recognition of cancer-related gangliosides and their mimics investigated using in silico site mapping.

Modified gangliosides may be overexpressed in certain types of cancer, thus, they are considered a valuable target in cancer immunotherapy. Structural knowledge of their interaction with antibodies is currently limited, due to the large size and high flexibility of these ligands. In this study, we a...

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Main Authors:	Mark Agostino, Elizabeth Yuriev, Paul A Ramsland
Format:	article
Language:	EN
Published:	Public Library of Science (PLoS) 2012
Subjects:	Medicine R Science Q
Online Access:	https://doaj.org/article/af14ca8bcbe0451596994dc406ff1a81
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spelling	oai:doaj.org-article:af14ca8bcbe0451596994dc406ff1a812021-11-18T07:21:25ZAntibody recognition of cancer-related gangliosides and their mimics investigated using in silico site mapping.1932-620310.1371/journal.pone.0035457https://doaj.org/article/af14ca8bcbe0451596994dc406ff1a812012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22536387/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Modified gangliosides may be overexpressed in certain types of cancer, thus, they are considered a valuable target in cancer immunotherapy. Structural knowledge of their interaction with antibodies is currently limited, due to the large size and high flexibility of these ligands. In this study, we apply our previously developed site mapping technique to investigate the recognition of cancer-related gangliosides by anti-ganglioside antibodies. The results reveal a potential ganglioside-binding motif in the four antibodies studied, suggesting the possibility of structural convergence in the anti-ganglioside immune response. The structural basis of the recognition of ganglioside-mimetic peptides is also investigated using site mapping and compared to ganglioside recognition. The peptides are shown to act as structural mimics of gangliosides by interacting with many of the same binding site residues as the cognate carbohydrate epitopes. These studies provide important clues as to the structural basis of immunological mimicry of carbohydrates.Mark AgostinoElizabeth YurievPaul A RamslandPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 4, p e35457 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Mark Agostino Elizabeth Yuriev Paul A Ramsland Antibody recognition of cancer-related gangliosides and their mimics investigated using in silico site mapping.
description	Modified gangliosides may be overexpressed in certain types of cancer, thus, they are considered a valuable target in cancer immunotherapy. Structural knowledge of their interaction with antibodies is currently limited, due to the large size and high flexibility of these ligands. In this study, we apply our previously developed site mapping technique to investigate the recognition of cancer-related gangliosides by anti-ganglioside antibodies. The results reveal a potential ganglioside-binding motif in the four antibodies studied, suggesting the possibility of structural convergence in the anti-ganglioside immune response. The structural basis of the recognition of ganglioside-mimetic peptides is also investigated using site mapping and compared to ganglioside recognition. The peptides are shown to act as structural mimics of gangliosides by interacting with many of the same binding site residues as the cognate carbohydrate epitopes. These studies provide important clues as to the structural basis of immunological mimicry of carbohydrates.
format	article
author	Mark Agostino Elizabeth Yuriev Paul A Ramsland
author_facet	Mark Agostino Elizabeth Yuriev Paul A Ramsland
author_sort	Mark Agostino
title	Antibody recognition of cancer-related gangliosides and their mimics investigated using in silico site mapping.
title_short	Antibody recognition of cancer-related gangliosides and their mimics investigated using in silico site mapping.
title_full	Antibody recognition of cancer-related gangliosides and their mimics investigated using in silico site mapping.
title_fullStr	Antibody recognition of cancer-related gangliosides and their mimics investigated using in silico site mapping.
title_full_unstemmed	Antibody recognition of cancer-related gangliosides and their mimics investigated using in silico site mapping.
title_sort	antibody recognition of cancer-related gangliosides and their mimics investigated using in silico site mapping.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/af14ca8bcbe0451596994dc406ff1a81
work_keys_str_mv	AT markagostino antibodyrecognitionofcancerrelatedgangliosidesandtheirmimicsinvestigatedusinginsilicositemapping AT elizabethyuriev antibodyrecognitionofcancerrelatedgangliosidesandtheirmimicsinvestigatedusinginsilicositemapping AT paularamsland antibodyrecognitionofcancerrelatedgangliosidesandtheirmimicsinvestigatedusinginsilicositemapping
_version_	1718423618479718400

Antibody recognition of cancer-related gangliosides and their mimics investigated using in silico site mapping.

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