UNSPECIFIED. (2005) Noncovalent Shiga-like toxin assemblies: Characterization by means of mass spectrometry and tandem mass spectrometry. BIOCHEMISTRY, 44 (23). pp. 8282-8290. ISSN 0006-2960

Full text not available from this repository.

Abstract

Shiga-like toxin 1 (SLTx), produced by enterohemorrhagic strains of Escherichia coli (EHEC), belongs to a family of structurally and functionally related AB(5) protein toxins that are associated with human disease. EHEC infection often gives rise to hemolytic colitis, while toxin-induced kidney damage is one of the major causes of hemolytic uremic syndrome (HUS) and acute renal failure in children. As such, an understanding and analysis of the noncovalent interactions that maintain the quaternary structure of this toxin are fundamentally important since such interactions have significant biochemical and medical implications. This paper reports on the analysis of the noncovalent homopentameric complex of Shiga-like toxin B chain (SLTx-B-5) using electrospray ionization (ESI) triple-quadrupole (QqQ) mass spectrometry (MS) and tandem mass spectrometry (MS/MS) and the analysis of the noncovalent hexameric holotoxin (SLTx-AB(5)) using ESI time-of-flight (TOF) MS. The triple-quadrupole analysis revealed highly charged monomer ions dissociate from the multiprotein complex to form dimer. trimer, and tetramer product ions, which were also seen to further dissociate. The ESI-TOFMS analysis of SLTx-AB5 revealed the complex remained intact and was observed in the gas phase over a range of pHs. Theses findings demonstrate that the gas-phase structure observed for both the holotoxin and the isoloated B chains correlates well with the structures reported to exist in the solution phase for these proteins. Such analysis provides a rapid screening technique for assessing the noncovalent structure of this family of proteins and other structurally related toxins.

Item Type:	Journal Article
Subjects:	Q Science > QD Chemistry
Journal or Publication Title:	BIOCHEMISTRY
Publisher:	AMER CHEMICAL SOC
ISSN:	0006-2960
Date:	14 June 2005
Volume:	44
Number:	23
Number of Pages:	9
Page Range:	pp. 8282-8290
Identification Number:	10.1021/bi0503706
Publication Status:	Published
URI:	http://wrap.warwick.ac.uk/id/eprint/6977

Data sourced from Thomson Reuters' Web of Knowledge

Request changes to a record

Actions (login required)

View Item