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A truncated apoptin protein variant selectively kills cancer cells.

Abstract：

:Apoptin is a nonstructural protein encoded by one of the three open reading frames of the chicken anemia virus genome. It has attracted a great deal of interest due to its ability to induce apoptosis in multiple transformed and malignant mammalian cell lines without affecting primary and non-transformed cells. However, the use of Apoptin as an anticancer drug is restricted by its strong tendency to aggregate. A number of methods to overcome this problem have been proposed, including transduction techniques to deliver the Apoptin gene into tumor cells, but all such methods have certain drawbacks. Here we describe that a truncated variant of Apoptin, lacking residues 1 to 43, is a soluble, non-aggregating protein that maintains most of the biological properties of wild-type Apoptin when transfected into cells. We show that the cytotoxic effect of this variant is also present when it is added exogenously to cancer cells, but not to normal cells. In addition to the interest this protein has attracted as a promising therapeutic strategy, it is also an excellent model to study the structural properties of Apoptin and how they relate to its mechanism of action.

journal_name

Invest New Drugs

journal_title

Investigational new drugs

authors

Ruiz-Martínez S,Castro J,Vilanova M,Bruix M,Laurents DV,Ribó M,Benito A

doi

10.1007/s10637-017-0431-6

subject

Has Abstract

pub_date

2017-06-01 00:00:00

pages

260-268

issue

3

eissn

0167-6997

issn

1573-0646

pii

10.1007/s10637-017-0431-6

journal_volume

35

pub_type

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