Structural biology of viral fibres

MVRaaij

 

Mark Van Raaij

Group Leader

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Research summary

Some viruses and bacteriophages attach to their host cell via proteins integral to their capsids, for example poliovirus, coxsackievirus and rhinovirus ('common cold virus'). Other viruses bind to their host cell receptors via specialised spike proteins (for example HIV, the AIDS-virus), or via specialised fibre proteins, like adenovirus, reovirus and bacteriophages like T4, T5, T7 and lambda (Ur). These fibres all have the same basic architecture: they are trimeric and contain an N-terminal virus or bacteriophage attachment domain, a long, thin, but stable shaft domain and a more globular C-terminal cell attachment domain.

 

 

Publications

Menéndez-Conejero R, Nguyen TH, Singh AK, Condezo GN, Marschang RE, van Raaij MJ, San Martín C. Structure of a Reptilian Adenovirus Reveals a Phage Tailspike Fold Stabilizing a Vertebrate Virus Capsid. Structure. 2017 Oct 3;25(10):1562-1573.e

Granell M, Namura M, Alvira S, Kanamaru S, van Raaij MJ. Crystal Structure of the Carboxy-Terminal Region of the Bacteriophage T4 Proximal Long Tail Fiber Protein Gp34. Viruses. 2017 Jun 30;9(7)

Garcia-Doval C, Castón JR, Luque D, Granell M, Otero JM, Llamas-Saiz AL, Renouard M, Boulanger P, van Raaij MJ. Structure of the receptor-binding carboxy-terminal domain of the bacteriophage T5 L-shaped tail fibre with and without its intra-molecular chaperone. Viruses 2015; 7: 6424-6440

Nguyen TH, Ballmann MZ, Do HT, Truong HN, Benko M, Harrach B, van Raaij MJ. Crystal structure of raptor adenovirus 1 fibre head and role of the beta-hairpin in siadenovirus fibre head domains. Virol J 2016; 13: 106

Nguyen TH, Thomas C, Timson D, van Raaij MJ Fasciola hepatica calcium-binding protein FhCaBP2: structure of the dynein light chain-like domain. Parasitol Res 2016; 115: 2879-2886

 

Fig1VanRaaijSome viruses and bacteriophages attach to their host cell via proteins integral to their capsids, for example poliovirus, coxsackievirus and rhinovirus ('common cold virus'). Other viruses bind to their host cell receptors via specialised spike proteins (for example HIV, the AIDS-virus), or via specialized fibre proteins, like adenovirus, reovirus and bacteriophages T4, T5 and T7. These fibres all have the same basic architecture; they are trimeric and have an N terminal virus or bacteriophage attachment domain, a long, thin but stable shaft domain, and a globular C-terminal cell attachment domain. These trimeric fibrous proteins are very stable to denaturation by temperature or detergents.

In 2013 and 2014, we determined the structures of the L-shaped tail fibre of bacteriophage T5 (the pb1 protein) with and without its C-terminal intramolecular chaperone, of the bacteriophage T4 fibre protein gp34, and of several animal adenovirus fibre proteins (snake atadenovirus 1, turkey siadenovirus 3, bovine atadenovirus 4, goose aviadenovirus 4 and mouse mastadenovirus 2).

Fig2VanRaaijKnowledge of the structures of viral and bacteriophage fibre proteins could lead to a variety of biotechnological applications. As adenovirus is used in experimental gene therapy, modification of its fibre should allow targeting to specific cell receptors. Modification of the bacteriophage fibre receptor binding specificities could permit improved detection and elimination of specific bacteria.

We also collaborated with other research groups in crystallisation and structure solutions for the proteins and peptides they produce, and determined structures of cyclic antibiotic peptides, bacterial dehydroquinases and shikimate kinases in complex with inhibitors, and of the bacteriophage K endolysin domain CHAPK.

 

grupoVanRaaij

 

Name
Position
Contact
Mark J. van Raaij Principal investigator
Pablo Soriano Maldonado Postdoctoral scientist
Thanh H. Nguyen Predoctoral scientists
Marta Sanz Gaitero Predoctoral scientists
Mateo Seoane Blanco Predoctoral scientists

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