The JI
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     
 


The Journal of Immunology, 1977, 118: 6-11.
Copyright © 1977 by The American Association of Immunologists, Inc.

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Coligan, J. E.
Right arrow Articles by Kindt, T. J.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Coligan, J. E.
Right arrow Articles by Kindt, T. J.

A Disaccharide Hapten from Streptococcal Group C Carbohydrate that Cross-Reacts with the Forssman Glycolipid1

John E. Coligan, Blair A. Fraser2 and Thomas J. Kindt

From The Rockefeller University, 1230 York Avenue, New York, New York 10021

Abstract

A disaccharide hapten was isolated in approximately 20% yield from an acid hydrolysate of the streptococcal Group C carbohydrate. This disaccharide was assigned the structure 3-0-{alpha}-N-acetylgalactosaminosyl-N-acetylgalactosamine on the basis of chemical and immunochemical data. The ability of the hapten to inhibit completely the binding between Group C carbohydrate and most Group C antibodies indicated that this disaccharide is the immunodominant feature of the Group C carbohydrate. Fractionation of antisera on an {alpha}-N-acetylgalactosamine immunoadsorbent column yielded several populations of anti-Group C antibodies. The reaction between labeled Group C carbohydrate and antibodies which strongly bound the immunoadsorbent column was 50% inhibitable by the disaccharide hapten when the hapten was added in approximately 15-fold excess (w/w) of the labeled antigen. On the other hand, the binding of those antibodies which did not bind to the immunoadsorbent column was poorly inhibited under these conditions. The Forssman glycosphingolipid, which has a common terminal digalactosamine unit, was shown to likewise inhibit Group C carbohydrate binding reactions.

Footnotes

1 This work was supported by Grant PCM75-2131) from the National Science Foundation, Washington, D. C. and by Grant AI08429 from the National Institute of Allergy and Infectious Diseases, National Institutes of Health.

2 Recipient of a Postdoctoral Research Fellowship from the National Institutes of Health, National Institute of Allergy and Infectious Diseases AI05181




This article has been cited by other articles:


Home page
Arch Otolaryngol Head Neck SurgHome page
J. M. Bernstein and K. Kano
Heterophile Antibodies in Middle Ear Effusions
Arch Otolaryngol Head Neck Surg, May 1, 1982; 108(5): 267 - 269.
[Abstract] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Website Copyright © 1977 by The American Association of Immunologists, Inc. All rights reserved.
All Contents Copyright © 1977 by The American Association of Immunologists, Inc. All rights reserved.