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IgE reactivity to native and recombinant Hev b 13: An allergenic protein from Hevea brasiliensis latex (Record no. 60688)

MARC details
000 -LEADER
fixed length control field	02398nam a2200169Ia 4500
100 ## - MAIN ENTRY--AUTHOR NAME
Personal name	Arif Siti Arija M
245 #0 - TITLE STATEMENT
Title	IgE reactivity to native and recombinant Hev b 13: An allergenic protein from Hevea brasiliensis latex
260 ## - PUBLICATION, DISTRIBUTION, ETC. (IMPRINT)
Name of publisher	IRRDB Conference: NR Industry: Responding to Globalization 7-8 September 2004, Kunming International Convention & Exhibition Center, China
520 ## - SUMMARY, ETC.
Summary, etc	The newly named latex allergen, Hev b 13, had been thought to be a variant of Hev b 7 (a patatin homologue) because of the close similarity in molecular weight and isoelectric point of these two proteins. The fact that both proteins showed esterase activity added to the confusion. One key characteristic of Hev b 13 appeared to confirm its identity with Hev b 7, was that IgE binding of Hev b 13 could be inhibited by patatin. For a time, therefore, Hev b 13 was known as Hev b 7b. When the full cDNA sequence of Hev b 13 was elucidated, no translated amino acid sequence homology was found between Hev b 13 to patatin and Hev b 7. While Hev b 13 and patatin shared no common amino acid sequences, one characteristic that the two proteins did have in common was that they were both glycosylated. The inhibition of IgE binding to Hev b 13 by patatin was due primarily to cross-reactive carbohydrate determinants (CCD) on the two proteins. There was no IgE binding when deglycosylated and periodated Hev b 13 were used in ELISA reaction and Western blots. No IgE inhibition to native Hev b 13 was detected when deglycosylated patatin was used as the inhibitor. To study further the role of the Hev b 13 glycan in IgE-recognition, an unglycosylated recombinant version of the protein was synthesised in Escherichia coli, using the pMal-c2 vector. A protein of 86 kDa was obtained and this corresponded to the expected size of the MBP-Hev b 13 fusion protein. The recombinant protein was recognized by the monoclonal and polyclonal antibodies against Hev b 13, thus confirming its identity. However, the recombinant protein had no binding affinity to IgE. All these results point to the carbohydrate moiety of the glycoprotein playing a much more important role in IgE binding than the amino acid domain.
650 ## - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical Term	Allergenic protein
650 ## - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical Term	Hev b 13
650 ## - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical Term	Hevea latex
650 ## - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical Term	IgE reactivity
700 ## - ADDED ENTRY--PERSONAL NAME
Personal name	Yeang H Y
942 ## - ADDED ENTRY ELEMENTS (KOHA)
Koha item type	Journals

Holdings
Withdrawn status	Lost status	Damaged status	Not for loan	Home library	Current library	Shelving location	Date acquired	Koha item type
			Journals	RRII Library	RRII Library	Physiology	17/12/2021	Journals