Evaluation of recombinant MGL_1304 produced by Pichia pastoris for clinical application to sweat allergy | Zendy

Takanobu Kan | Zendy; Takaaki Hiragun | Zendy; Kaori Ishii | Zendy; Makiko Hiragun | Zendy; Yuhki Yanase | Zendy; Akio Tanaka | Zendy; Michihiro Hide | Zendy

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Evaluation of recombinant MGL_1304 produced by Pichia pastoris for clinical application to sweat allergy

Author(s) -

Takanobu Kan,

Takaaki Hiragun,

Kaori Ishii,

Makiko Hiragun,

Yuhki Yanase,

Akio Tanaka,

Michihiro Hide

Publication year - 2015

Publication title -

allergology international

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.49

H-Index - 58

eISSN - 1440-1592

pISSN - 1323-8930

DOI - 10.1016/j.alit.2015.03.003

Subject(s) - pichia pastoris , recombinant dna , antigen , escherichia coli , biology , immunoglobulin e , histamine , western blot , degranulation , microbiology and biotechnology , allergen , allergy , immunology , antibody , biochemistry , gene , endocrinology , receptor

We previously identified MGL_1304 secreted by Malassezia globosa as a sweat antigen for patients with atopic dermatitis (AD) and cholinergic urticaria (ChU). However, purifying native MGL_1304 from human sweat or culture supernatant of M. globosa (sup-MGL_1304) is costly and time-consuming. Moreover, recombinant MGL_1304 expressed by using Escherichia coli (TF-rMGL_1304) needs a large chaperon protein and lacks the original glycosylation of yeasts. Thus, we generated a recombinant MGL_1304 by Pichia pastoris (P-rMGL_1304) and investigated its characteristic features.

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