How to Disassemble a Virus Capsid A Computational Approach

• Type: Article in International Conference Proceedings Book
• Date: 2017

Authors

Piedade, CA (Author) Other; Ferreira, AEN (Author) Other; Cordeiro, C (Author) Other

Conference proceedings International

Title: PROCEEDINGS OF THE 10TH INTERNATIONAL JOINT CONFERENCE ON BIOMEDICAL ENGINEERING SYSTEMS AND TECHNOLOGIES, VOL 3: BIOINFORMATICS

Pages: 217-222

10th International Joint Conference on Biomedical Engineering Systems and Technologies

Porto, PORTUGAL, FEB 21-23, 2017

Indexing

ISI Web of Knowledge - 1 Citation

Scopus - 1 Citation

Other information

Authenticus ID: P-00N-4Q8

DOI: 10.5220/0006249802170222

Abstract (EN): In contrast with the assembly process of virus particles, which has been the focus of many experimental and theoretical studies, the disassembly of virus protein capsids, a key event during infection, has generally been overlooked. Although the nature of the intracellular triggers that promote subunit disassembly may be diverse, here we postulate that the order of subunit removal is mainly determined by each virus structural geometry and the strength of subunit interactions. Following this assumption, we modelled the early stages of virus disassembly of T = 1 icosahedral viruses, predicting the sequence of removal of up to five subunits in a sample of 51 structures. We used combinatorics and geometry, to find non-geometrically identical capsid fragments and estimated their energy by three different heuristics based on the number of weak inter-subunit contacts. We found a main disassembly pathway common to a large group of viruses consisting of the removal of a triangular trimer. Densoviruses lose a square-shaped tetramer while Human Adenoviruses lose a pentagonshaped pentamer. Results were virtually independent of the heuristic measure used. These findings suggest that particular subunit interactions might be an important target for novel antiviral drugs designed to interfere

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 6