Prestress Strengthens the Shell of Norwalk Virus Nanoparticles

被引:42
作者
Baclayon, Marian [1 ]
Shoemaker, Glen K. [2 ,3 ]
Uetrecht, Charlotte [2 ,3 ]
Crawford, Sue E. [4 ]
Estes, Mary K. [4 ]
Prasad, B. V. Venkataram [5 ]
Heck, Albert J. R. [2 ,3 ]
Wuite, Gijs J. L. [1 ]
Roos, Wouter H. [1 ]
机构
[1] Vrije Univ Amsterdam, Nat & Sterrenkunde & LaserLab, NL-1081 HV Amsterdam, Netherlands
[2] Univ Utrecht, Biomol Mass Spectrometry & Prote Grp, Bijvoet Ctr Biomol Res, NL-3584 CH Utrecht, Netherlands
[3] Univ Utrecht, Utrecht Inst Pharmaceut Sci, NL-3584 CH Utrecht, Netherlands
[4] Baylor Coll Med, Dept Mol Virol & Microbiol, Houston, TX 77030 USA
[5] Baylor Coll Med, Verna & Marrs McLean Dept Biochem & Mol Biol, Houston, TX 77030 USA
基金
加拿大自然科学与工程研究理事会;
关键词
AFM; nanoindentation; native mass spectrometry; viral nanoparticles; Noro virus; mechanical properties; MASS-SPECTROMETRY; CAPSID PROTEIN; VIRAL CAPSIDS; MECHANICAL-PROPERTIES; STABILITY; NANOINDENTATION; SEQUENCE; ANTIGEN; CELLS;
D O I
10.1021/nl202699r
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
We investigated the influence of the protruding domain of Norwalk virus-like particles (NVLP) on its overall structural and mechanical stability. Deletion of the protruding domain yields smooth mutant particles and our AFM nanoindentation measurements show a surprisingly altered indentation response of these particles. Notably, the brittle behavior of the NVLP as compared to the plastic behavior of the mutant reveals that the protruding domain drastically changes the capsid's material properties. We conclude that the protruding domain introduces prestress, thereby increasing the stiffness of the NVLP and effectively stabilizing the viral nanoparticles. Our results exemplify the variety of methods that nature has explored to improve the mechanical properties of viral capsids, which in turn provides new insights for developing rationally designed, self-assembled nanodevices.
引用
收藏
页码:4865 / 4869
页数:5
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