PERTUSSIS TOXIN AND TARGET EUKARYOTIC CELLS - BINDING, ENTRY, AND ACTIVATION

被引：150

作者：

KASLOW, HR ^{[1
]}

BURNS, DL ^{[1
]}

机构：

[1] USDA,CTR BIOL EVALUAT & RES,BETHESDA,MD 20892

来源：

FASEB JOURNAL | 1992年 / 6卷 / 09期

关键词：

ADP-RIBOSYLTRANSFERASE; DETERGENT; DISULFIDE; DTT; G-PROTEIN; GLUTATHIONE; GLYCOLIPID; LIPID; NUCLEOTIDE; PHOSPHOLIPID; VACCINE;

D O I：

10.1096/fasebj.6.9.1612292

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Pertussis toxin, a protein virulence factor produced by Bordetella pertussis, is composed of an A protomer and a B oligomer. The A protomer consists of a single polypeptide, termed the S1 subunit, which disrupts transmembrane signaling by ADP-ribosylating eukaryotic G-proteins. The B oligomer, containing five polypeptides, binds to cell receptors (most likely containing carbohydrate) and delivers the S1 subunit. Current knowledge suggests that expression of ADP-ribosyltransferase activity in target eukaryotic cells arises after 1) nucleotides and membrane lipids allosterically promote the release of the S1 subunit; and 2) the single disulfide bond in the S1 subunit is reduced by reductants such as glutathione. This model suggests conditions for the proper use of the toxin as an experimental reagent.

引用

页码：2684 / 2690

页数：7

共 65 条

[1] INTERACTION OF LYMPHOID AND NONLYMPHOID CELLS WITH LYMPHOCYTOSIS-PROMOTING FACTOR OF BORDETELLA-PERTUSSIS [J].