Disulfide bond mapping of Pfs25, a recombinant malaria transmission blocking vaccine candidate

被引：10

作者：

Lee, Shwu-Maan ^{[1
]}

Plieskatt, Jordan ^{[1
]}

King, C. Richter ^{[1
]}

机构：

[1] PATH Malaria Vaccine Initiat MVI, 455 Massachusetts Ave NW,Suite 1000, Washington, DC 20001 USA

来源：

ANALYTICAL BIOCHEMISTRY | 2018年 / 542卷

基金：

比尔及梅琳达.盖茨基金会;

关键词：

Pfs25; Plasmodium falciparum; Malaria; Baculovirus; Disulfide; PLASMODIUM-FALCIPARUM; PICHIA-PASTORIS; PROTEIN; EXPRESSION; ANTIBODIES; ANTIGENS;

D O I：

10.1016/j.ab.2017.11.009

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

A liquid chromatography tandem-mass spectrometry method was developed to map the eleven disulfide bonds in Pfs25, a malaria transmission-blocking vaccine candidate. The compact and complex nature of Pfs25 has led to difficulties in prior peptide mapping efforts. Here, we report confirmation of proper disulfide pairing of a recombinant Pfs25, by optimizing denaturation and digestion with trypsin/Lys-C. The digested peptides were separated by reversed phase HPLC to obtain the peptide map and elucidate the disulfide linkages. MSE fragmentation confirmed the digested peptides and disulfide bonds. The eleven disulfide bonds and locations matched the predicted Pvs25 crystal structure, a Pfs25 homologue.

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收藏

页码：20 / 23

页数：4

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