L4 - Viral structure Flashcards

1
Q

Many viruses exhibit icosahedral symmetry, characterised by 20 triangular faces and 12 vertices.

A

Many viruses exhibit icosahedral symmetry, characterised by 20 triangular faces and 12 vertices.

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2
Q

What are the key features of an icosahedron in virus structure?

A

An icosahedron has rotational symmetry axes of 2-, 3-, and 5-fold, which dictate its overall shape and assembly.

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3
Q

How does helical symmetry differ from icosahedral symmetry in viruses?

A

Helical symmetry involves the formation of a nucleocapsid with a spiral or rod-like structure, common among enveloped RNA viruses.

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4
Q

Why is understanding virus symmetry important for structural studies?

A

It aids in determining the assembly, stability, and potential targets for antiviral drugs.

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5
Q

What advantage does cryo-electron microscopy offer over traditional electron microscopy?

A

Cryo-EM preserves the native hydrated state of viruses and enables high-resolution 3D reconstructions.

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6
Q

How does X‑ray crystallography contribute to our understanding of virus structure?

A

It provides atomic resolution details of virus components, although it requires the virus or its parts to form crystals.

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7
Q

What role does cryo-electron tomography play in virus research?

A

It allows for visualisation of large, asymmetrical biological assemblies, including viruses in a near-native state.

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8
Q

How have AI approaches, such as AlphaFold, advanced virus structural studies?

A

They refine cryo-EM reconstructions, predict protein structures from sequences, and aid in mapping evolutionary relationships.

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9
Q

What was significant about the X‑ray structure determination of poliovirus?

A

It revealed the “β‐jelly roll” structure of capsid proteins and provided a framework for understanding viral assembly.

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10
Q
A
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11
Q

What is the benefit of combining X‑ray and cryo‑EM techniques in viral studies?

A

This combination allows for the detailed characterisation of both static high-resolution structures and dynamic viral rearrangements.

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12
Q

How can structural knowledge of viruses be applied in medical research?

A

It underpins rational drug design, structure-based vaccine development, and even strategies for rational attenuation of viruses.

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13
Q

What are the key areas covered in the study of virus structure?

A

The study includes virus symmetry, methods to determine structures (e.g. cryo-EM, X‑ray crystallography), atomic-resolution structures, and applications such as antiviral drug design and vaccine development.

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14
Q

How has structural knowledge advanced our understanding of virus entry and evolution?

A

Detailed structures reveal dynamic rearrangements during entry, inform fusion mechanisms, and help trace evolutionary relationships among viruses.

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15
Q

Why is it important to study virus structure at atomic resolution?

A

Atomic-level details allow for precise identification of functional domains, interactions with host receptors, and targeted design of antiviral compounds.

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16
Q

In what ways is virus structure utilised in modern medicine?

A

It is applied to structure-based vaccine design, rational drug design, and even the attenuation of viruses for safe vaccine development.

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17
Q

What is icosahedral symmetry and why is it common in viruses?

A

Icosahedral symmetry refers to a spherical arrangement with 20 triangular faces and 12 vertices, optimising structural stability and efficient assembly with limited genetic material.

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18
Q

How many faces and vertices does an icosahedron have?

A

An icosahedron has 20 faces and 12 vertices.

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19
Q

What are the rotational symmetry axes in an icosahedron?

A

The axes are 2-fold, 3-fold, and 5-fold, which determine the uniform distribution of capsid proteins.

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20
Q

Why is icosahedral symmetry advantageous for virus assembly?

A

It allows viruses to form a closed shell using multiple copies of a few protein types, minimising genetic complexity while maximising structural strength.

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21
Q

What characterises helical virus structures?

A

Helical viruses have a nucleocapsid that forms a spiral or rod-like structure, often seen in enveloped RNA viruses.

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22
Q

How does the assembly of helical viruses differ from icosahedral viruses?

A

Helical viruses assemble by polymerising capsid proteins along the viral RNA, forming a flexible and elongated structure.

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23
Q

In what types of viruses are helical structures typically observed?

A

They are common in many enveloped animal RNA viruses, such as those in the Paramyxoviridae family.

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24
Q

Why might a helical structure be beneficial for certain viruses?

A

Helical structures can accommodate long strands of RNA and may allow for greater flexibility in the virus particle.

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25
Q

What are the main techniques used to study virus structure?

A

Key methods include electron microscopy (EM), cryo-electron microscopy (cryo-EM), and X‑ray crystallography.

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26
Q

How does cryo-EM differ from traditional EM?

A

Cryo-EM involves rapid freezing of samples in their native hydrated state, preserving natural structure and enabling high-resolution 3D reconstructions.

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27
Q

What is a limitation of X‑ray crystallography in virus studies?

A

It requires the formation of crystals, which may be challenging for large or flexible virus particles.

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28
Q

How has the resolution of cryo-EM advanced in recent years?

A

Cryo-EM resolution has improved to below 2 Å, allowing for near-atomic detail in virus structures.

29
Q

What was significant about the X‑ray structure of poliovirus?

A

The structure revealed a “β‑jelly roll” motif in the capsid proteins, enhancing understanding of virus assembly and stability.

30
Q

How has the structure of influenza haemagglutinin (HA) contributed to our knowledge of virus entry?

A

The X‑ray structure of HA delineated receptor-binding and fusion domains, clarifying how the virus binds to host cells and initiates fusion

31
Q

What does the combination of X‑ray and cryo‑EM studies provide in viral structural analysis?

A

It integrates high-resolution static details with dynamic, near-native state visualisation, leading to a comprehensive understanding of viral architecture.

32
Q

Why are structural studies of viruses critical for developing antiviral therapies?

A

Detailed structures enable the design of molecules that specifically target viral components, disrupting key processes such as fusion and replication.

33
Q

How are X‑ray and cryo‑EM techniques combined to study flaviviruses?

A

X‑ray crystallography provides atomic details of individual proteins, while cryo‑EM visualises the intact virus particle and its overall architecture.

34
Q

What is the advantage of combining these two methods for flaviviruses?

A

The integration allows researchers to map high-resolution protein structures onto the overall virion, revealing how structural rearrangements occur during maturation and fusion.

35
Q

How does the flavivirus E protein change upon exposure to acidic pH?

A

It undergoes a conformational rearrangement from a dimeric to a trimeric postfusion state, facilitating membrane fusion.

36
Q

What are some applications of the structural knowledge obtained from flavivirus studies?

A

These include rational vaccine design, antiviral drug development, and improved understanding of virus-host interactions and immune evasion.

37
Q

How does structural information contribute to rational antiviral drug design?

A

It allows for the identification of binding sites and active domains on viral proteins, enabling the design of inhibitors that disrupt critical viral functions.

38
Q

What role does virus structure play in vaccine development?

A

Structural insights enable the design of immunogens that mimic the native virus, eliciting a robust immune response.

39
Q

How can structural studies inform the rational attenuation of viruses for vaccine use?

A

By understanding the structural determinants of virulence, specific mutations can be introduced to reduce pathogenicity without compromising immunogenicity.

40
Q

In what way does structural information help in understanding virus evolution?

A

Comparative analysis of virus structures can reveal conserved elements and evolutionary relationships, informing both epidemiology and the development of broad-spectrum antivirals.

41
Q

What is recombineering, and how is it used in virus research?

A

Recombineering is a genetic engineering technique that allows for targeted modifications of viral genomes, aiding in functional studies and vaccine development.

42
Q

How do viral envelopes contribute to host cell entry?

A

Viral envelopes help the virus fuse with host cell membranes, facilitating entry and infection.

43
Q

What is the role of spike proteins in enveloped viruses?

A

Spike proteins mediate attachment and entry into host cells by binding to specific receptors.

44
Q

How does the presence of an envelope impact viral stability?

A

Enveloped viruses are often less stable in the environment but can evade the immune system more effectively.

45
Q

What factors determine whether a virus has an envelope?

A

A virus acquires an envelope if it buds from the host cell membrane rather than lysing the cell.

46
Q

Why do some viruses lack an envelope, and how does this affect their transmission?

A

Non-enveloped viruses are generally more resistant to environmental conditions and tend to spread via the fecal-oral route.

47
Q

What distinguishes a capsid from an envelope in viral structure?

A

The capsid is a protein shell that encloses the viral genome, whereas an envelope is derived from the host membrane and surrounds the capsid.

48
Q

How does icosahedral symmetry contribute to efficient genome packaging?

A

Icosahedral symmetry allows viruses to form stable, closed structures using minimal genetic material.

49
Q

What is the significance of helical symmetry in viral architecture?

A

Helical symmetry enables flexible genome encapsidation and is commonly seen in RNA viruses.

50
Q

What are the key differences between icosahedral and helical virus structures?

A

Icosahedral viruses form compact, spherical particles, while helical viruses form elongated, rod-like structures.

51
Q

How does electron microscopy contribute to viral morphology studies?

A

Electron microscopy provides a general view of viral morphology, including size and shape.

52
Q

What are the limitations of traditional electron microscopy in studying virus structure?

A

Traditional electron microscopy has limited resolution and may not reveal fine structural details.

53
Q

Why is cryo-electron microscopy particularly useful for studying viruses?

A

Cryo-EM allows for high-resolution imaging of viruses in a near-native hydrated state.

54
Q

How does rapid freezing in cryo-EM preserve viral structure?

A

Rapid freezing prevents ice crystal formation, preserving the virus in a close-to-natural conformation.

55
Q

What advantage does cryo-EM have over X-ray crystallography in viral studies?

A

Cryo-EM does not require crystallization and can resolve flexible or complex viral structures.

56
Q

Why is crystallization a challenge in X-ray crystallography for viruses?

A

Crystallization can be difficult for large or dynamic viruses, limiting the applicability of X-ray crystallography.

57
Q

What are some key viral components that have been studied using X-ray crystallography?

A

Hemagglutinin and neuraminidase from influenza viruses have been studied using X-ray crystallography.

58
Q

How does structural knowledge of viruses aid in vaccine development?

A

Understanding virus structure helps in designing vaccines that target key viral proteins.

59
Q

Why is the stabilization of viral proteins important for vaccine efficacy?

A

Stabilizing viral proteins ensures they maintain the correct conformation for an effective immune response.

60
Q

How has structural virology contributed to the development of SARS-CoV-2 vaccines?

A

Structural virology enabled the design of stabilized spike protein variants used in COVID-19 vaccines.

61
Q

What is an example of a drug that was designed based on viral structural knowledge?

A

Neuraminidase inhibitors, such as oseltamivir (Tamiflu), were developed based on viral structural insights.

62
Q

How does structural knowledge help in designing antiviral drugs?

A

Identifying viral entry mechanisms and active sites enables the creation of targeted antiviral drugs.

63
Q

What role does viral structure play in understanding zoonotic transmission?

A

Structural comparisons help predict how viruses evolve and jump between species.

64
Q

How does AlphaFold contribute to structural virology?

A

AlphaFold predicts viral protein structures from sequence data, accelerating structural analysis.

65
Q

What are the benefits of using AI-based tools in viral structure prediction?

A

AI tools streamline the identification of viral epitopes and drug targets by predicting structural conformations.

66
Q

How has AI advanced the study of flaviviruses?

A

AI-based approaches have revealed new structural variants in flaviviruses, improving vaccine and drug strategies.

67
Q

What structural features of flaviviruses have been identified using AI tools?

A

Structural studies have mapped flavivirus surface proteins, aiding in understanding their immune evasion strategies.

68
Q

How do structural studies contribute to understanding virus-host interactions?

A

Viral evolution studies inform strategies to develop broad-spectrum antivirals and future vaccines.

69
Q

Why is studying viral evolution important for vaccine and drug development?