Viruses and bacteria have developed a great variety of mechanisms to attack their hosts and to bring about disease. However, even "innocent"; protein such as the prion, which has come to particular prominence through the BSE crisis, can transform itself into a pathogen through its specific structural properties. This module highlights how structural and functional features of proteins contribute to the pathogenic nature of their parent organism, or how structural information can give insight into future drug design or help combat the emerging threat of drug resistance. Detailed knowledge of the structure and function of ‘pathogenic’ macromolecules provides targets for therapeutic intervention. Lectures and student-centred activities will explore this subject under these headlines:

• Viruses: virus-encoded capsid and cytoslic proteins, viral entry into host cells
• Mechanisms of bacterial host-cell attachment and invasion
• Action of antibiotics and mechanisms of antibiotic resistance
• Novel viral pro-drug therapies

Protein (mis-)folding in amyloid structures and prion-related diseases

.By the end of the module students should be able to:

• explore the structures of pathogenic macromolecules and protein assemblies using molecular graphics software; analyse and discuss their properties by tackling problem-based questions
• research and jointly prepare a group poster demonstrating the relationship between structure and function of a case-study ‘pathogenic macromolecule’ and outline potential future experiments; present the poster to other students on a one-to-one basis to peers
• independently outline the structures of selected viruses, viral and bacterial proteins, explaining how these structures relate to their pathogenic function, and discuss how we may use structural biology to aid attempts to develop novel therapies or combat emerging threats such as drug resistence
• ​independently discuss the problem of  protein misfolding, describing the role of misfolded proteins in disease processes