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Table of Contents
Vol. 111, No. 4, 1996
Issue release date: 1996
Section title: Original Paper
Int Arch Allergy Immunol 1996;111:385–395
(DOI:10.1159/000237397)

Isolation and Expression of a cDNA Clone Encoding an Alternaria alternata Alt a 1 Subunit

De Vouge M.W.a · Thaker A.J.a · A. Curran I.H.a · Zhang L.a · Muradia G.a · Rode H.b · Vijay H.M.a
aLife Sciences Division, Bureau of Drug Research, and bBureau of Biologies, Drugs Directorate, Health Protection Branch, Health Canada, Ottawa, Canada

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Article / Publication Details

First-Page Preview
Abstract of Original Paper

Received: October 25, 1995
Accepted: June 26, 1996
Published online: September 04, 2009
Issue release date: 1996

Number of Print Pages: 11
Number of Figures: 0
Number of Tables: 0

ISSN: 1018-2438 (Print)
eISSN: 1423-0097 (Online)

For additional information: http://www.karger.com/IAA

Abstract

Alternaria alternata is recognized as an important source of fungal aeroallergens. Alt a 1, the major allergen of this mold, is a dimer of disulfide-linked sub-units that migrate in SDS-PAGE under reducing conditions at apparent Ms of 14,500 and 16,000. IgE antibodies to this protein are present in the sera of > 90% of A. alternata-sensitive individuals. Previous studies from this laboratory showed that the N-termini twenty amino acids of the purified subunits are nearly identical. We now report the isolation of clones from an A. alternata (strain 34–016) cDNA library constructed in λgt11, using rabbit IgG antiserum against partially purified Alt a 1. One of nineteen clones selected from screens totalling 305,000 pfu (rb51) was sequenced, and determined to harbor an insert of 660 bp. An in-frame open reading frame within the cloned insert encodes a peptide of Mr 16,960 that bears no significant homology to known allergens or proteins. The size of the rb51 transcript was determined to be ≈ 0.7 kb by Northern analysis of A. alternata total RNA. The largely hydrophobic N-terminal region of the peptide contains an α-helical domain and other features characteristic of membrane targeting or secretory signals. The peptide sequence downstream of this region matches previously sequenced Alt a 1 N-terminal from two independent sources at 17 of 20, and 24 of 26 positions. Recombinant Alt a 1 expressed as a secreted protein in Pichia pastoris exists as a dimer in conditioned medium, as shown by immunoblotting under nonreducing conditions. Recombinant Alt a 1, like the natural allergen in A. alternata extracts, is also reactive with serum IgE from A.alternata-sensitive individuals.

© 1996 S. Karger AG, Basel


Article / Publication Details

First-Page Preview
Abstract of Original Paper

Received: October 25, 1995
Accepted: June 26, 1996
Published online: September 04, 2009
Issue release date: 1996

Number of Print Pages: 11
Number of Figures: 0
Number of Tables: 0

ISSN: 1018-2438 (Print)
eISSN: 1423-0097 (Online)

For additional information: http://www.karger.com/IAA


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Drug Dosage: The authors and the publisher have exerted every effort to ensure that drug selection and dosage set forth in this text are in accord with current recommendations and practice at the time of publication. However, in view of ongoing research, changes in government regulations, and the constant flow of information relating to drug therapy and drug reactions, the reader is urged to check the package insert for each drug for any changes in indications and dosage and for added warnings and precautions. This is particularly important when the recommended agent is a new and/or infrequently employed drug.
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