PMID: 9829995Nov 26, 1998

Determination of the disulfide bonds within a B domain variant surface glycoprotein from Trypanosoma congolense

The Journal of Biological Chemistry
H BusslerE Reinwald

Abstract

The disulfide bonds within a variant surface glycoprotein from Trypanosoma congolense have been determined. L-[35S]Cysteine metabolically labeled protein was digested with trypsin, and radiolabeled peptides were separated by reversed-phase high performance liquid chromatography, and putative cystine-containing peptides were subdigested with other proteases and analyzed after further purification by amino acid sequencing and mass spectrometry. All eight cysteine residues of the protein, located within the N-terminal domain, are covalently linked. The four disulfide bonds are between cysteines 16/236, 171/193, 195/206, and 286/298. This is, for the first time, the determination of disulfide bonds within a variant surface glycoprotein belonging to the B-type. As all the eight cysteines of BENat 1.3 variant surface glycoprotein are positionally conserved, the cystine pattern of this protein can be regarded as a prototype of disulfide bonding within B-type variant surface glycoproteins. Although the cysteine residues of B-type variant surface glycoproteins are located at completely different positions in the protein chain compared with A-type variant surface glycoproteins, the positions of the disulfide bonds can easily be integrate...Continue Reading

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Citations

May 14, 2003·Molecular and Biochemical Parasitology·Jun WangGeorge A M Cross
Dec 13, 2000·Microbes and Infection·H TabelJ E Uzonna
Nov 30, 2011·Antioxidants & Redox Signaling·Saikh Jaharul HaqueSailen Barik
Jan 21, 2014·Protein Science : a Publication of the Protein Society·Matthew K Higgins, M Carrington
Nov 16, 2007·The Journal of Biological Chemistry·Nicola G JonesM Carrington
Nov 24, 2004·The Journal of Biological Chemistry·Anasuya ChattopadhyayM Carrington

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Disulfides
Peptide Mapping
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