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Published on: August 9, 2011
Insight into the three-dimensional structure of maize chlorotic mottle virus revealed by Cryo-EM single particle
Chun-Yan Wang1, Qin-Fen Zhang2, Yuan-Zhu Gao2
1Institute of Insect Science, Institute of Biotechnology, Zhejiang University, Hangzhou 310058, China.
Abstract:
Maize chlorotic mottle virus (MCMV) is the only member of the Machlomovirus genus in the family Tombusviridae. Here, we obtained the Cryo-EM structure of MCMV by single particle analysis with most local resolution at approximately 4 Å. The Cα backbone was built based on residues with bulky side chains. The resolved C-terminus of the capsid protein subunit and obvious openings at the 2-fold axis demonstrated the compactness of the asymmetric unit, which indicates an important role in the stability of MCMV. The Asp116 residue from each subunit around the 5-fold and 3-fold axes contributed to the negative charges in the centers of the pentamers and hexamers, which might serve as a solid barrier against the leakage of genomic RNA. Finally, the loops most exposed on the surface were analyzed and are proposed to be potential functional sites related to MCMV transmission.
Insights
The Maize chlorotic mottle virus (MCMV) structure was determined using Cryo-EM, revealing features crucial for its stability and potential transmission mechanisms. This research provides insights into the virus
Area of Science:
- Virology
- Structural Biology
- Biochemistry
Background:
- Maize chlorotic mottle virus (MCMV) is the sole member of the Machlomovirus genus within the Tombusviridae family.
- Understanding MCMV's structure is key to comprehending its stability and infectivity.
Purpose of the Study:
- To determine the high-resolution Cryo-EM structure of Maize chlorotic mottle virus (MCMV).
- To elucidate structural features related to MCMV stability and transmission.
Main Methods:
- Single particle Cryo-Electron Microscopy (Cryo-EM) analysis.
- Determination of the MCMV structure at approximately 4 Å resolution.
- Cα backbone construction and analysis of surface-exposed loops.
Main Results:
- The MCMV structure revealed a compact asymmetric unit, with the C-terminus of the capsid protein and 2-fold axis openings contributing to stability.
- Negative charges from Asp116 residues at the pentamer and hexamer centers may prevent genomic RNA leakage.
- Surface-exposed loops were identified as potential sites for MCMV transmission.
Conclusions:
- The determined MCMV structure provides critical insights into its stability mechanisms.
- Specific residues and surface loops are implicated in viral stability and transmission, offering targets for future research.
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