Interplay between the mechanics of bacteriophage fibers and the strength of virus-host links. Ares, P., Garcia-Doval, C., Llauro, A., Gomez-Herrero, J., van Raaij, M. J., & de Pablo, P. J. PHYSICAL REVIEW E, MAY 16, 2014. doi abstract bibtex Viral fibers play a central role in many virus infection mechanisms since they recognize the corresponding host and establish a mechanical link to its surface. Specifically, bacteriophages have to anchor to bacteria through the fibers surrounding the tail before starting the viral DNA translocation into the host. The protein gene product (gp) 37 from bacteriophage T4 long tail fibers forms a fibrous parallel homotrimer located at the distal end of the long tail fibers. Biochemical data indicate that, at least, three of these fibers are required for initial host cell interaction but do not reveal why three and no other numbers are required. By using atomic force microscopy, we obtained high-resolution images of gp37 fibers adsorbed on a mica substrate in buffer conditions and probed their local mechanical properties. Our experiments of radial indentation at the nanometer scale provided a radial stiffness of similar to 0.08 N/m and a breaking force of similar to 120 pN. In addition, we performed finite element analysis and determined a Young's modulus of similar to 20 MPa. From these mechanical parameters, we hypothesize that three viral fibers provide enough mechanical strength to prevent a T4 virus from being detached from the bacteria by the viral particle Brownian motion, delivering a biophysical justification for the previous biochemical data.
@article{ ISI:000339564500006,
Author = {Ares, P. and Garcia-Doval, C. and Llauro, A. and Gomez-Herrero, J. and
van Raaij, M. J. and de Pablo, P. J.},
Title = {{Interplay between the mechanics of bacteriophage fibers and the strength
of virus-host links}},
Journal = {{PHYSICAL REVIEW E}},
Year = {{2014}},
Volume = {{89}},
Number = {{5}},
Month = {{MAY 16}},
Abstract = {{Viral fibers play a central role in many virus infection mechanisms
since they recognize the corresponding host and establish a mechanical
link to its surface. Specifically, bacteriophages have to anchor to
bacteria through the fibers surrounding the tail before starting the
viral DNA translocation into the host. The protein gene product (gp) 37
from bacteriophage T4 long tail fibers forms a fibrous parallel
homotrimer located at the distal end of the long tail fibers.
Biochemical data indicate that, at least, three of these fibers are
required for initial host cell interaction but do not reveal why three
and no other numbers are required. By using atomic force microscopy, we
obtained high-resolution images of gp37 fibers adsorbed on a mica
substrate in buffer conditions and probed their local mechanical
properties. Our experiments of radial indentation at the nanometer scale
provided a radial stiffness of similar to 0.08 N/m and a breaking force
of similar to 120 pN. In addition, we performed finite element analysis
and determined a Young's modulus of similar to 20 MPa. From these
mechanical parameters, we hypothesize that three viral fibers provide
enough mechanical strength to prevent a T4 virus from being detached
from the bacteria by the viral particle Brownian motion, delivering a
biophysical justification for the previous biochemical data.}},
DOI = {{10.1103/PhysRevE.89.052710}},
Article-Number = {{052710}},
ISSN = {{2470-0045}},
EISSN = {{2470-0053}},
ResearcherID-Numbers = {{van Raaij, Mark J/B-3678-2009
de Pablo, Pedro/L-9392-2014
Ares, Pablo/N-2272-2017
Gomez-Herrero, Julio/B-6094-2013
}},
ORCID-Numbers = {{van Raaij, Mark J/0000-0002-4781-1375
de Pablo, Pedro/0000-0003-2386-3186
Ares, Pablo/0000-0001-5905-540X
Gomez-Herrero, Julio/0000-0001-8583-8061
Garcia Doval, Carmela/0000-0002-3422-9490}},
Unique-ID = {{ISI:000339564500006}},
}
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Specifically, bacteriophages have to anchor to bacteria through the fibers surrounding the tail before starting the viral DNA translocation into the host. The protein gene product (gp) 37 from bacteriophage T4 long tail fibers forms a fibrous parallel homotrimer located at the distal end of the long tail fibers. Biochemical data indicate that, at least, three of these fibers are required for initial host cell interaction but do not reveal why three and no other numbers are required. By using atomic force microscopy, we obtained high-resolution images of gp37 fibers adsorbed on a mica substrate in buffer conditions and probed their local mechanical properties. Our experiments of radial indentation at the nanometer scale provided a radial stiffness of similar to 0.08 N/m and a breaking force of similar to 120 pN. In addition, we performed finite element analysis and determined a Young's modulus of similar to 20 MPa. From these mechanical parameters, we hypothesize that three viral fibers provide enough mechanical strength to prevent a T4 virus from being detached from the bacteria by the viral particle Brownian motion, delivering a biophysical justification for the previous biochemical data.","doi":"10.1103/PhysRevE.89.052710","article-number":"052710","issn":"2470-0045","eissn":"2470-0053","researcherid-numbers":"van Raaij, Mark J/B-3678-2009 de Pablo, Pedro/L-9392-2014 Ares, Pablo/N-2272-2017 Gomez-Herrero, Julio/B-6094-2013 ","orcid-numbers":"van Raaij, Mark J/0000-0002-4781-1375 de Pablo, Pedro/0000-0003-2386-3186 Ares, Pablo/0000-0001-5905-540X Gomez-Herrero, Julio/0000-0001-8583-8061 Garcia Doval, Carmela/0000-0002-3422-9490","unique-id":"ISI:000339564500006","bibtex":"@article{ ISI:000339564500006,\nAuthor = {Ares, P. and Garcia-Doval, C. and Llauro, A. and Gomez-Herrero, J. and\n van Raaij, M. J. and de Pablo, P. J.},\nTitle = {{Interplay between the mechanics of bacteriophage fibers and the strength\n of virus-host links}},\nJournal = {{PHYSICAL REVIEW E}},\nYear = {{2014}},\nVolume = {{89}},\nNumber = {{5}},\nMonth = {{MAY 16}},\nAbstract = {{Viral fibers play a central role in many virus infection mechanisms\n since they recognize the corresponding host and establish a mechanical\n link to its surface. Specifically, bacteriophages have to anchor to\n bacteria through the fibers surrounding the tail before starting the\n viral DNA translocation into the host. The protein gene product (gp) 37\n from bacteriophage T4 long tail fibers forms a fibrous parallel\n homotrimer located at the distal end of the long tail fibers.\n Biochemical data indicate that, at least, three of these fibers are\n required for initial host cell interaction but do not reveal why three\n and no other numbers are required. By using atomic force microscopy, we\n obtained high-resolution images of gp37 fibers adsorbed on a mica\n substrate in buffer conditions and probed their local mechanical\n properties. Our experiments of radial indentation at the nanometer scale\n provided a radial stiffness of similar to 0.08 N/m and a breaking force\n of similar to 120 pN. In addition, we performed finite element analysis\n and determined a Young's modulus of similar to 20 MPa. 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