Author:
Vernhes Emeline,Renouard Madalena,Gilquin Bernard,Cuniasse Philippe,Durand Dominique,England Patrick,Hoos Sylviane,Huet Alexis,Conway James F.,Glukhov Anatoly,Ksenzenko Vladimir,Jacquet Eric,Nhiri Naïma,Zinn-Justin Sophie,Boulanger Pascale
Abstract
Abstract
Bacteriophage capsids constitute icosahedral shells of exceptional stability that protect the viral genome. Many capsids display on their surface decoration proteins whose structure and function remain largely unknown. The decoration protein pb10 of phage T5 binds at the centre of the 120 hexamers formed by the major capsid protein. Here we determined the 3D structure of pb10 and investigated its capsid-binding properties using NMR, SAXS, cryoEM and SPR. Pb10 consists of an α-helical capsid-binding domain and an Ig-like domain exposed to the solvent. It binds to the T5 capsid with a remarkably high affinity and its binding kinetics is characterized by a very slow dissociation rate. We propose that the conformational exchange events observed in the capsid-binding domain enable rearrangements upon binding that contribute to the quasi-irreversibility of the pb10-capsid interaction. Moreover we show that pb10 binding is a highly cooperative process, which favours immediate rebinding of newly dissociated pb10 to the 120 hexamers of the capsid protein. In extreme conditions, pb10 protects the phage from releasing its genome. We conclude that pb10 may function to reinforce the capsid thus favouring phage survival in harsh environments.
Publisher
Springer Science and Business Media LLC
Reference46 articles.
1. Dokland, T. Freedom and restraint: themes in virus capsid assembly. Struct. Lond. Engl. 1993 8, R157–162 (2000).
2. Lander, G. C. et al. Bacteriophage lambda stabilization by auxiliary protein gpD: timing, location, and mechanism of attachment determined by cryo-EM. Struct. Lond. Engl. 1993 16, 1399–1406 (2008).
3. Qin, L., Fokine, A., O’Donnell, E., Rao, V. B. & Rossmann, M. G. Structure of the small outer capsid protein, Soc: a clamp for stabilizing capsids of T4-like phages. J. Mol. Biol. 395, 728–741 (2010).
4. Sathaliyawala, T. et al. Functional analysis of the highly antigenic outer capsid protein, Hoc, a virus decoration protein from T4-like bacteriophages. Mol. Microbiol. 77, 444–455 (2010).
5. Zairi, M., Stiege, A. C., Nhiri, N., Jacquet, E. & Tavares, P. The collagen-like protein gp12 is a temperature-dependent reversible binder of SPP1 viral capsids. J. Biol. Chem. 289, 27169–27181 (2014).
Cited by
26 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献