Cloning and sequencing of a cDNA expressing a recombinant house dust mite protein that binds human IgE and corresponds to an important low molecular weight allergen [published erratum appears in J Exp Med 1990 Apr 1;171(4):1387]

نویسندگان

  • E R Tovey
  • M C Johnson
  • A L Roche
  • G S Cobon
  • B A Baldo
چکیده

A cDNA clone coding for a mite allergen of mol wt approximately 14,000 has been isolated and its DNA sequence determined. The native component from mite extracts encoded by this DNA was identified by immunoprobing blots of mite body extract with human IgE eluted from the electroblotted cloned fusion polypeptides derived from the expressed cDNA clone. The clone encodes a polypeptide with a deduced mol wt of 17,460. The deduced amino acid sequence was not homologous to any known protein sequences and it contains no cysteine or tryptophan. On blots, 21 of 38 sera from mite-allergic subjects recognized the cloned material, and this recognition strongly correlated with IgE-binding to the native component on protein blots of mite extract.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

BriefDefinitive Report CLONING AND SEQUENCING OF A cDNA EXPRESSING A RECOMBINANT HOUSE DUST MITE PROTEIN THAT BINDS HUMAN IgE AND CORRESPONDS TO AN IMPORTANT LOW MOLECULAR WEIGHT ALLERGEN

The cloning of recombinant proteins offers the possibility ofproducing, identifying, and manipulating the important IgE-binding determinants present on proteins that are responsible for provoking allergic diseases (1) . Proteins produced by mites of the genus Dermatophagoides are among the most important allergens affecting man in terms of both the frequency of the response by allergic subjects...

متن کامل

Molecular Cloning, Characterization, and Expression of Cuc m 2, a Major Allergen in Cucumis melo

Background: Several studies reported the clinical features of IgE-mediated hypersensitivity after ingestion of melon. Melon allergy is a common IgE-mediated fruit allergy in Iran. This prompted us to investigate immunochemical and molecular properties of the major allergen in melon fruit, to compare the IgE-binding capacity of the natural protein with the recombinant allergen, and to determine ...

متن کامل

Molecular Cloning and Expression of Cro s 1: an Occupational Allergen from Saffron Pollen (Crocus sativus)

Background: The cultivation of saffron is expanding through the southeast of Iran, and allergy to saffron pollen occurs in workers involved in processing this plant. We aimed to clone, sequence and express a major allergen involved in saffron pollen allergy, and to compare the recombinant with the natural allergen. Methods: The N-terminal amino acid sequence of Cro s 1, an allergen from saff...

متن کامل

Sequence analysis of cDNA coding for a major house dust mite allergen, Der p 1. Homology with cysteine proteases

A cDNA clone coding for Der p 1, a major allergen from the house dust mite Dermatophagoides pteronyssinus, has been sequenced. It codes for a 222 residue mature protein with a derived molecular weight of 25,371 and contains 1 potential N-glycosylation site. In addition, the cDNA appears to code for a 13 residue proregion, and an incomplete signal peptide. The deduced sequence shows a high degre...

متن کامل

Microsoft Word - IAA357BF

The enzyme amylase was shown to be present in extracts prepared from both house dust and spent growth medium used in the culture of the mite Dermatophagoides pteronyssinus. In dust, it was shown to correlate with both mite counts and concentrations of the faecally derived mite allergen, Der p I. Mite amylase was isolated from the culture medium and shown to be a single chain protein with a mole...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • The Journal of Experimental Medicine

دوره 170  شماره 

صفحات  -

تاریخ انتشار 1989