structural biology of viral fibers


members (left-to-right)

Mateo Seoane Blanco - doctoral student (FPI fellowship)
Thanh H. Nguyen - doctoral student
Marta Sanz Gaitero - doctoral student (RISAM fellowship)
Pablo Soriano Maldonado
- postdoc
Mark J van Raaij - cientifico titular
Antonio Pichel Beleiro
- doctoral student (RISAM fellowship)

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 specialized spike proteins (for example HIV, the AIDS-virus), or via specialized fiber proteins, like adenovirus, reovirus and many bacteriophages.
Virus fibers 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. Their detailed folds are very diverse and often reveal novel features.
These trimeric, fibrous proteins are very stable to denaturation by temperature or detergents. Our goal is to determine the structures of these proteins and thus to make an extensive inventory of stable trimeric folds present in nature. We also want to explain how they bind their receptors and therefore aim to crystallize them with receptor analogues.

30 june 2017: paper on phage T4 gp34 structure published in Viruses
april 2017: Mark appointed Section Editor of Acta Crystallographica F

structure gallery

bacteriophage fibers

adenovirus proteins

bacteriophage endolysins

bacterial dehydroquinase, shikimate kinase



webpage @ CNB-CSIC


Section Editor of Acta Crystallographica F, Structural Biology Communications

Deputy Section Editor of Virology Journal
Academic Editor of PLoS One