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

被引:13
作者
Bussler, H
Linder, M
Linder, D
Reinwald, E
机构
[1] Free Univ Berlin, Inst Vet Biochem, D-14163 Berlin, Germany
[2] Univ Giessen, Inst Biochem, D-35392 Giessen, Germany
关键词
D O I
10.1074/jbc.273.49.32582
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
The disulfide bonds within a variant surface glycoprotein from Trypanosoma congolense have been determined. L-[S-35]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 mere 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 integrated into the A-type tertiary structure. This result implies that, despite their enormous amino acid sequence variability, variant surface glycoproteins, regardless of their subtype, can fold into a similar tertiary structure.
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页码:32582 / 32586
页数:5
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