Structure and Physics of Viruses by Mauricio G. Mateu

Author:Mauricio G. Mateu
Language: eng
Format: epub
Publisher: Springer Netherlands, Dordrecht

Although one can generally speak about scaffolding proteins, and indeed many viruses have such proteins, scaffolding functions can also be performed by flexible regions of the capsid proteins, which establish interactions during assembly that are later removed via conformational changes or cleavage by viral proteases. For example, bacteriophage HK97 (Siphoviridae) does not encode a scaffold protein. Instead, a 103 residue stretch at the N-terminus of the capsid protein, known as the delta-domain, performs the scaffold function [65]. The delta domain is located towards the interior of the capsid and mediates interactions between capsomers during assembly. Once the procapsid is completed, and before the DNA is packaged, the delta domain is cleaved out by the viral protease, allowing the transition to the next assembly intermediate [62]. Adenovirus may use a dual system, including both a separate scaffolding protein [66] and flexible regions of minor capsid proteins removed by the viral protease during maturation [67].

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