Structure, function and dynamics in adenovirus maturation

Area of Science:

• Virology
• Molecular Biology
• Structural Biology

Background:

• Adenoviruses are non-enveloped icosahedral viruses with a dsDNA genome packaged within a capsid.
• The viral genome forms a compact core with histone-like proteins.
• Maturation is a critical step for adenovirus infectivity, involving significant structural and biochemical changes.

Purpose of the Study:

• To review current knowledge on adenovirus maturation.
• To elucidate the mechanisms and significance of proteolytic cleavage by the adenovirus protease (AVP).
• To understand how maturation impacts virion stability, uncoating, and infectivity.

Main Methods:

• Review of existing literature on adenovirus structure, assembly, and maturation.
• Analysis of the role of the viral protease (AVP) in processing capsid and core proteins.
• Discussion of the functional consequences of protein cleavage on virion architecture and infectivity.

Main Results:

• Adenovirus maturation is orchestrated by proteolytic cleavage of precursor proteins by AVP.
• AVP utilizes a unique "molecular sled" mechanism for efficient substrate targeting along the viral genome.
• Maturation converts the immature, stable virion into a metastable state, facilitating uncoating and genome delivery.
• Processing of the L1 52/55k packaging protein by AVP is essential for its removal during maturation.

Conclusions:

• Adenovirus maturation is a complex process involving precise proteolytic events crucial for viral lifecycle.
• The metastable nature of the mature virion is key to its infectivity, enabling efficient uncoating.
• Understanding adenovirus maturation provides insights into viral assembly, genome packaging, and host-cell entry mechanisms.