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


     
 


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 Similar articles in PubMed
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 Rogers, B. L.
Right arrow Articles by Kuo, M. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Rogers, B. L.
Right arrow Articles by Kuo, M. C.

The Journal of Immunology, Vol 147, Issue 8 2547-2552, Copyright © 1991 by American Association of Immunologists


ARTICLES

Complete sequence of the allergen Amb alpha II. Recombinant expression and reactivity with T cells from ragweed allergic patients

BL Rogers, JP Morgenstern, IJ Griffith, XB Yu, CM Counsell, AW Brauer, TP King, RD Garman and MC Kuo
ImmuLogic Pharmaceutical Corporation, Cambridge, MA 02139.

This study defines the complete primary structure of Amb alpha II, an important allergen produced by short ragweed (Ambrosia artemisiifolia). The deduced amino acid sequence derived from the cDNA indicates that Amb alpha II shares approximately 65% sequence identity with the Amb alpha I multigene family of allergens. Full-length cDNA encoding Amb alpha I.1 and Amb alpha II have been expressed in E. coli and purified. An in-frame linker encoding polyhistidine has been added to the 5' end of the cDNA to facilitate purification using Ni2+ ion affinity chromatography, yielding greater than 90% pure recombinant protein in a single step. T cells from patients allergic to ragweed proliferate in response to pollen extract as well as purified recombinant Amb alpha I.1 and Amb alpha II. T cell lines established using either Amb alpha I.1 or II as the stimulating Ag exhibit a high level of cross- reactivity to both proteins. This result is entirely consistent with the extensive primary sequence identity shared by these two proteins. These data suggest that allergic humans recognize shared T cell epitopes on these two related molecules.


This article has been cited by other articles:


Home page
J. Immunol.Home page
S. P. Chapoval, T. Neeno, C. J. Krco, E. V. Marietta, J. Harders, and C. S. David
HLA-DQ6 and HLA-DQ8 Transgenic Mice Respond to Ragweed Allergens and Recognize a Distinct Set of Epitopes on Short and Giant Ragweed Group 5 Antigens
J. Immunol., August 15, 1998; 161(4): 2032 - 2037.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
D. A. Bagarozzi Jr., R. Pike, J. Potempa, and J. Travis
Purification and Characterization of a Novel Endopeptidase in Ragweed (Ambrosia artemisiifolia) Pollen
J. Biol. Chem., October 18, 1996; 271(42): 26227 - 26232.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Website Copyright © 1991 by The American Association of Immunologists, Inc. All rights reserved.
All Contents Copyright © 1991 by The American Association of Immunologists, Inc. All rights reserved.