8R5Z

Structure of coxsackievirus B5 capsid (mutant CVB5F.cas.genogroupB) - E particle

Summary for 8R5Z

• Entry DOI: 10.2210/pdb8r5z/pdb
• EMDB information: 18942 18944
• Descriptor: Genome polyprotein (1 entity in total)
• Functional Keywords: enterovirus, coxsackievirus, thermostable, mutant, virus
• Biological source: Coxsackievirus B5
• Total number of polymer chains: 3
• Total formula weight: 281386.08

Authors

Kumar, K.,Antanasijevic, A. (deposition date: 2023-11-19, release date: 2024-03-27, Last modification date: 2024-04-10)

Primary citation

Torii, S.,Gouttenoire, J.,Kumar, K.,Antanasijevic, A.,Kohn, T.
Influence of Amino Acid Substitutions in Capsid Proteins of Coxsackievirus B5 on Free Chlorine and Thermal Inactivation.
Environ Sci Technol., 58:5279-5289, 2024

PubMed Abstract: The sensitivity of enteroviruses to disinfectants varies among genetically similar variants and coincides with amino acid changes in capsid proteins, although the effect of individual substitutions remains unknown. Here, we employed reverse genetics to investigate how amino acid substitutions in coxsackievirus B5 (CVB5) capsid proteins affect the virus' sensitivity to free chlorine and heat treatment. Of ten amino acid changes observed in CVB5 variants with free chlorine resistance, none significantly reduced the chlorine sensitivity, indicating a minor role of the capsid composition in chlorine sensitivity of CVB5. Conversely, a subset of these amino acid changes located at the C-terminal region of viral protein 1 led to reduced heat sensitivity. Cryo-electron microscopy revealed that these changes affect the assembly of intermediate viral states (altered and empty particles), suggesting that the mechanism for reduced heat sensitivity could be related to improved molecular packing of CVB5, resulting in greater stability or altered dynamics of virus uncoating during infection.

PubMed: 38488515
DOI: 10.1021/acs.est.3c10409

Experimental method

ELECTRON MICROSCOPY (2.6 Å)