Changes in the stability and biomechanics of P22 bacteriophage capsid during maturation

dc.contributor.authorKant, Ravi
dc.contributor.authorLlauro, Aida
dc.contributor.authorRayaprolu, Vamseedhar
dc.contributor.authorQazi, Shefah
dc.contributor.authorde Pablo, Pedro J.
dc.contributor.authorDouglas, Trevor
dc.contributor.authorBothner, Brian
dc.date.accessioned2018-09-27T19:45:04Z
dc.date.available2018-09-27T19:45:04Z
dc.date.issued2018-06
dc.description.abstractThe capsid of P22 bacteriophage undergoes a series of structural transitions during maturation that guide it from spherical to icosahedral morphology. The transitions include the release of scaffold proteins and capsid expansion. Although P22 maturation has been investigated for decades, a unified model that incorporates thermodynamic and biophysical analyses is not available. A general and specific model of icosahedral capsid maturation is of significant interest to theoreticians searching for fundamental principles as well as virologists and material scientists seeking to alter maturation to their advantage. To address this challenge, we have combined the results from orthogonal biophysical techniques including differential scanning fluorimetry, atomic force microscopy, circular dichroism, and hydrogen-deuterium exchange mass spectrometry. By integrating these results from single particle and population measurements, an energy landscape of P22 maturation from procapsid through expanded shell to wiffle ball emerged, highlighting the role of metastable structures and the thermodynamics guiding maturation. The propagation of weak quaternary interactions across symmetric elements of the capsid is a key component for stability in P22. A surprising finding is that the progression to wiffle ball, which lacks pentamers, shows that chemical and thermal stability can be uncoupled from mechanical rigidity, elegantly demonstrating the complexity inherent in capsid protein interactions and the emergent properties that can arise from icosahedral symmetry. On a broader scale, this work demonstrates the power of applying orthogonal biophysical techniques to elucidate assembly mechanisms for supramolecular complexes and provides a framework within which other viral systems can be compared.en_US
dc.identifier.citationKant, Ravi, Aida Llauro, Vamseedhar Rayaprolu, Shefah Qazi, Pedro J. de Pablo, Trevor Douglas, and Brian Bothner. "Changes in the stability and biomechanics of P22 bacteriophage capsid during maturation." BBA - Biochimica et Biophysica Acta 1862, no. 6 (June 2018): 1492-1504. DOI:10.1016/j.bbagen.2018.03.006.en_US
dc.identifier.issn0006-3002
dc.identifier.urihttps://scholarworks.montana.edu/handle/1/14874
dc.language.isoenen_US
dc.rightsThis Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s).en_US
dc.rights.urihttp://rightsstatements.org/vocab/InC/1.0/en_US
dc.titleChanges in the stability and biomechanics of P22 bacteriophage capsid during maturationen_US
dc.typeArticleen_US
mus.citation.extentfirstpage1492en_US
mus.citation.extentlastpage1504en_US
mus.citation.issue6en_US
mus.citation.journaltitleBiochimica et Biophysica Actaen_US
mus.citation.volume1862en_US
mus.contributor.orcidBothner, Brian|0000-0003-1295-9609en_US
mus.data.thumbpage8en_US
mus.identifier.categoryLife Sciences & Earth Sciencesen_US
mus.identifier.doi10.1016/j.bbagen.2018.03.006en_US
mus.relation.collegeCollege of Agricultureen_US
mus.relation.departmentChemistry & Biochemistry.en_US
mus.relation.departmentMicrobiology & Cell Biology.en_US
mus.relation.universityMontana State University - Bozemanen_US

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