The JI PBL Intereron Source
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 King, T. P.
Right arrow Articles by Lu, G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by King, T. P.
Right arrow Articles by Lu, G.

The Journal of Immunology, Vol 154, Issue 2 577-584, Copyright © 1995 by American Association of Immunologists

ARTICLES

Murine T and B cell responses to natural and recombinant hornet venom allergen Dol m 5.02 and its recombinant fragments

TP King, L Kochoumian and G Lu
Rockefeller University, New York, NY 10021.

White-face hornet venom allergen, Dol m 5.02, is a protein of 204 amino acid residues. This protein and its overlapping fragments, of 53-114 residues in size, containing the N-terminal, middle, and C-terminal regions of the molecule, can be expressed in high yield in bacteria by using the plasmid vector pQE12. Natural (n) and recombinant (r) Dol m 5.02s and the r-fragments are about equally immunogenic for IgG Ab response in BALB/c mice. n-Dol m 5.02 induces mainly murine IgG Abs specific for its discontinuous B cell epitopes and, to a lesser extent, Abs specific for its continuous epitopes. r-Dol m 5.02 and the r- fragments induce only Abs specific for continuous B cell epitopes that are common with those of the n-protein. Abs specific for the discontinuous epitopes show higher affinity than those specific for the continuous epitopes. r-Dol m 5.02 and the r-fragments are as efficient as n-Dol m 5.02 in inducing murine T cell responses specific for the n- protein. The differences in the immunogenicity of n- and r-proteins or r-peptide fragments for B and T cell responses are related to their conformations, inasmuch as only the n-protein is cross-linked by four disulfide bonds. These findings are relevant to the potential use of r- fragments as immunotherapeutic reagents in humans.


This article has been cited by other articles:


Home page
 J. Immunol.Home page
T. P. King, S. Y. Jim, R. I. Monsalve, A. Kagey-Sobotka, L. M. Lichtenstein, and M. D. Spangfort
Recombinant Allergens with Reduced Allergenicity but Retaining Immunogenicity of the Natural Allergens: Hybrids of Yellow Jacket and Paper Wasp Venom Allergen Antigen 5s
J. Immunol., May 15, 2001; 166(10): 6057 - 6065.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
G. Lu, L. Kochoumian, and T. P. King
Sequence Identity and Antigenic Cross-reactivity of White Face Hornet Venom Allergen, Also a Hyaluronidase, with Other Proteins
J. Biol. Chem., March 3, 1995; 270(9): 4457 - 4465.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Website Copyright © 1995 by The American Association of Immunologists, Inc. All rights reserved.
All Contents Copyright © 1995 by The American Association of Immunologists, Inc. All rights reserved.