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-Structure paper
タイトル | Influence of Amino Acid Substitutions in Capsid Proteins of Coxsackievirus B5 on Free Chlorine and Thermal Inactivation. |
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ジャーナル・号・ページ | Environ Sci Technol, Vol. 58, Issue 12, Page 5279-5289, Year 2024 |
掲載日 | 2024年3月26日 |
著者 | Shotaro Torii / Jérôme Gouttenoire / Kiruthika Kumar / Aleksandar Antanasijevic / Tamar Kohn / |
PubMed 要旨 | 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 ...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. |
リンク | Environ Sci Technol / PubMed:38488515 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.6 - 3.6 Å |
構造データ | EMDB-18942, PDB-8r5x: EMDB-18943, PDB-8r5y: EMDB-18944, PDB-8r5z: |
化合物 | ChemComp-PLM: |
由来 |
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キーワード | VIRUS / Enterovirus / coxsackievirus / thermostable / mutant |