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Engineering of a mini-trichosanthin that has lower antigenicity by deleting its C-terminal amino acid residues.

Abstract：

:Trichosanthin is a ribosome-inactivating protein that possesses antitumor and antiviral activities. Clinical trials of trichosanthin on AIDS patients, however, elicit anaphylactic reactions. To reduce the antigenicity of trichosanthin as a drug while preserving its biological activity, the C-terminal domain (residues 203 to 247), which contains a putative antigenic site, was systemically deleted. We have found that the minimum length of trichosanthin that can fold into an active conformation is residue 1 to 240. The mini-trichosanthin (C7) generated by deleting the last seven C-terminal amino acid residues has 2.7-fold decrease in antigenicity, 10-fold reduction in in vitro ribosome-inactivation activity, and in vivo cytotoxicity toward K562 cells, and 2-fold reduction in abortificient activity. Structural analyses of C7 indicate decrease in the helix content, increased exposure of Trp192, and lower thermodynamic stability. The deletion of the C-terminal residues (Leu241 to Ala247) probably perturbs local structure of the C-terminal antigenic epitope that results in the decrease in antigenicity and activities of C7.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Chan SH,Shaw PC,Mulot SF,Xu LH,Chan WL,Tam SC,Wong KB

doi

10.1006/bbrc.2000.2395

subject

Has Abstract

pub_date

2000-04-02 00:00:00

pages

279-85

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(00)92395-7

journal_volume

270

pub_type

杂志文章

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