The human IgG anti-carbohydrate repertoire exhibits a universal architecture and contains specificity for microbial attachment sites-Reference-Cited by-同舟云学术

The human IgG anti-carbohydrate repertoire exhibits a universal architecture and contains specificity for microbial attachment sites

Published:2015-01-07 Issue:269 Volume:7 Page:
ISSN:1946-6234
Container-title:Science Translational Medicine
language:en
Short-container-title:Sci. Transl. Med.

Author:

Schneider Christoph¹,Smith David F.²,Cummings Richard D.²,Boligan Kayluz Frias¹,Hamilton Robert G.³,Bochner Bruce S.³,Miescher Sylvia⁴,Simon Hans-Uwe¹,Pashov Anastas⁵,Vassilev Tchavdar⁵,von Gunten Stephan¹

Affiliation:

1. Institute of Pharmacology, University of Bern, CH-3010 Bern, Switzerland.

2. Protein-Carbohydrate Interaction Core H, Consortium for Functional Glycomics, Department of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA.

3. Division of Allergy and Clinical Immunology, Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, MD 21224, USA.

4. Research and Development, CSL Behring AG, CH-3014 Bern, Switzerland.

5. Department of Immunology, Stefan Angelov Institute of Microbiology, Bulgarian Academy of Sciences, 1113 Sofia, Bulgaria.

Abstract

The IgG anti-carbohydrate repertoire reveals potential glycan antigen determinants relevant to vaccine design.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

General Medicine

Reference64 articles.

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5. Intravenous immunoglobulin contains a broad repertoire of anticarbohydrate antibodies that is not restricted to the IgG2 subclass

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