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


     
 


This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
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
Right arrow Request Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Paddock, C. D.
Right arrow Articles by Marshall, N.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Paddock, C. D.
Right arrow Articles by Marshall, N.
The Journal of Immunology, 2001, 167: 2694-2699.
Copyright © 2001 by The American Association of Immunologists

Identification, Cloning, and Recombinant Expression of Procalin, a Major Triatomine Allergen1

Christopher D. Paddock*, James H. McKerrow2,{dagger},§, Elizabeth Hansell{dagger}, K. W. Foreman{ddagger}, Ivy Hsieh{dagger} and Neal Marshall

* Viral and Rickettsial Zoonoses Branch, Centers for Disease Control and Prevention, Atlanta, GA 30333; Departments of {dagger} Pathology and {ddagger} Pharmaceutical Chemistry, University of California, and § Department of Veterans Affairs Medical Center, San Francisco, CA 94121; and Department of Natural Sciences, Notre Dame de Namur University, Belmont, CA 94002

Among the most frequent anaphylactic reactions to insects are those attributed to reduviid bugs. We report the purification and identification of the major salivary allergen of these insects. This 20-kDa protein (procalin) is a member of the lipocalin family, which includes salivary allergens from other invertebrates and mammals. An expression system capable of producing reagent quantities of recombinant allergen was developed in Saccharomyces cerevisiae. Antisera produced against recombinant protein cross-reacts with ELISA with salivary allergen. Recombinant Ag is also shown to react with sera from an allergic patient but not with control sera. By immunolocalization, the source of the salivary Ag is the salivary gland epithelium and its secretions.




This article has been cited by other articles:


Home page
Int ImmunolHome page
S. Saarelainen, T. Zeiler, J. Rautiainen, A. Narvanen, M. Rytkonen-Nissinen, R. Mantyjarvi, P. Vilja, and T. Virtanen
Lipocalin allergen Bos d 2 is a weak immunogen
Int. Immunol., April 1, 2002; 14(4): 401 - 409.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Website Copyright © 2001 by The American Association of Immunologists, Inc. All rights reserved.
All Contents Copyright © 2001 by The American Association of Immunologists, Inc. All rights reserved.