Thermal stability of the hemagglutinin‐neuraminidase from Sendai virus evidences two folding domains

FEBS Letters

Manfrinato, Maria Cristina³  Dallocchio, Franco³  Tomasi, Maurizio¹  Bellini, Tiziana³  Masserini, Massimo² 

[1] Laboratorio di Biologia Cellulare, Istituto Superiore di Sanità, viale Regina Elena 299, 00161 Rome, Italy;Dipartimento di Medicina Sperimentale e Ambientale, Università di Milano-Bicocca, Via Saldini 50, 20133 Milan, Italy;Dipartimento di Biochimica e Biologia Molecolare, Università di Ferrara, via Borsari 46, 44100 Ferrara, Italy

关键词: β-Propeller;    Differential scanning calorimetry;    Paramyxovirus;    Thermal denaturation;    Neuraminidase;    Protein folding;   

DOI  :  10.1016/S0014-5793(01)02362-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The domain structure of hemagglutinin-neuraminidase from Sendai virus (cHN) was investigated by studying the thermal stability in the 20–100°C range. Differential scanning calorimetry evidences two conformational transitions. The first transition is apparently a reversible two-state process, with T _m 48.3°C, and is shifted to 50.1°C in the presence of the substrate analogue 2,3-dehydro-2-deoxy-N-acetyl neuraminic acid, meaning that the substrate binding domain is involved in the transition. The second transition, with apparent T _m 53.2°C, is accompanied by irreversible loss of enzymatic activity of the protein, and the presence of the substrate analogue does not affect the T _m. The data indicate that cHN is composed of two independent folding domains, and that only one domain is involved in the binding of the substrate. Our results suggest that the paramyxovirus neuraminidases have the folding properties of a two-domain protein.

【 授权许可】

Unknown