Adenylate cyclase toxin-mediated delivery of the S1 subunit of pertussis toxin into mammalian cells | Zendy

Masaaki Iwaki | Zendy; Toshifumi Konda | Zendy

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Adenylate cyclase toxin-mediated delivery of the S1 subunit of pertussis toxin into mammalian cells

Author(s) -

Masaaki Iwaki,

Toshifumi Konda

Publication year - 2015

Publication title -

pathogens and disease

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.983

H-Index - 105

ISSN - 2049-632X

DOI - 10.1093/femspd/ftv110

Subject(s) - bordetella pertussis , adenylate cyclase toxin , pertussis toxin , adp ribosylation , cyclase , toxin , protein subunit , bordetella , pertactin , adenylate kinase , endocytosis , biochemistry , diphtheria toxin , biology , g protein , effector , epitope , chemistry , microbiology and biotechnology , antigen , receptor , bacteria , enzyme , nad+ kinase , genetics , gene

The adenylate cyclase toxin (ACT) of Bordetella pertussis internalizes its catalytic domain into target cells. ACT can function as a tool for delivering foreign protein antigen moieties into immune effector cells to induce a cytotoxic T lymphocyte response. In this study, we replaced the catalytic domain of ACT with an enzymatically active protein moiety, the S1 (ADP-ribosyltransferase) subunit of pertussis toxin (PT). The S1 moiety was successfully internalized independent of endocytosis into sheep erythrocytes. The introduced polypeptide exhibited ADP-ribosyltransferase activity in CHO cells and induced clustering typical to PT. The results indicate that ACT can act as a vehicle for not only epitopes but also enzymatically active peptides to mammalian cells.

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