DNA-mediated anisotropic mechanical reinforcement of a virus

被引:155
作者
Carrasco, C.
Carreira, A.
Schaap, I. A. T.
Serena, P. A.
Gomez-Herrero, J.
Mateu, M. G.
de Pablo, P. J. [1 ]
机构
[1] Univ Autonoma Madrid, Consejo Super Invest Cient, Dept Fis Mat Condensada C 3, E-28049 Madrid, Spain
[2] Univ Autonoma Madrid, Consejo Super Invest Cient, Ctr Biol Mol Severo Ochoa, E-28049 Madrid, Spain
[3] Natl Inst Med Res, London NW7 1AA, England
[4] CSIC, Inst Ciencia Mat, E-28049 Madrid, Spain
基金
英国医学研究理事会;
关键词
capsid; virion; nanomechanics; finite element methods; atomic force microscopy; PARVOVIRUS MINUTE VIRUS; AMINO-ACID-RESIDUES; VP1; N-TERMINUS; FUNCTIONAL IMPLICATIONS; FORCE MICROSCOPY; SPHERICAL VIRUS; MICE; CAPSIDS; DETERMINANTS; PARTICLES;
D O I
10.1073/pnas.0601881103
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
in this work, we provide evidence of a mechanism to reinforce the strength of an icosahedral virus by using its genomic DNA as a structural element. The mechanical properties of individual empty capsids and DNA-containing virions of the minute virus of mice are investigated by using atomic force microscopy. The stiffness of the empty capsid is found to be isotropic. Remarkably, the presence of the DNA inside the virion leads to an anisotropic reinforcement of the virus stiffness by approximate to 3%, 40%, and 140% along the fivefold, threefold, and twofold symmetry axes, respectively. A finite element model of the virus indicates that this anisotropic mechanical reinforcement is due to DNA stretches bound to 60 concavities of the capsid. These results, together with evidence of biologically relevant conformational rearrangements of the capsid around pores located at the fivefold symmetry axes, suggest that the bound DNA may reinforce the overall stiffness of the viral particle without canceling the conformational changes needed for its infectivity.
引用
收藏
页码:13706 / 13711
页数:6
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