Publication

Understanding Adenovirus maturation: A nanomechanics approach

Denning, D., Bennett, S., Mullen, T., Moyer, C., Wuite, G. J., Nemerow, G. & Roos, W. H., 1-Jul-2017, In : European Biophysics Journal. 46, Supplement 1, p. S184 1 p.

Research output: Contribution to journalMeeting AbstractAcademic

APA

Denning, D., Bennett, S., Mullen, T., Moyer, C., Wuite, G. J., Nemerow, G., & Roos, W. H. (2017). Understanding Adenovirus maturation: A nanomechanics approach. European Biophysics Journal, 46(Supplement 1), S184. https://doi.org/10.1007/s00249-017-1222-x

Author

Denning, D. ; Bennett, S. ; Mullen, T. ; Moyer, C. ; Wuite, G.J. ; Nemerow, G. ; Roos, W.H. / Understanding Adenovirus maturation: A nanomechanics approach. In: European Biophysics Journal. 2017 ; Vol. 46, No. Supplement 1. pp. S184.

Harvard

Denning, D, Bennett, S, Mullen, T, Moyer, C, Wuite, GJ, Nemerow, G & Roos, WH 2017, 'Understanding Adenovirus maturation: A nanomechanics approach', European Biophysics Journal, vol. 46, no. Supplement 1, pp. S184. https://doi.org/10.1007/s00249-017-1222-x

Standard

Understanding Adenovirus maturation: A nanomechanics approach. / Denning, D.; Bennett, S.; Mullen, T.; Moyer, C.; Wuite, G.J.; Nemerow, G.; Roos, W.H.

In: European Biophysics Journal, Vol. 46, No. Supplement 1, 01.07.2017, p. S184.

Research output: Contribution to journalMeeting AbstractAcademic

Vancouver

Denning D, Bennett S, Mullen T, Moyer C, Wuite GJ, Nemerow G et al. Understanding Adenovirus maturation: A nanomechanics approach. European Biophysics Journal. 2017 Jul 1;46(Supplement 1):S184. https://doi.org/10.1007/s00249-017-1222-x


BibTeX

@article{0cb848bf3aae4b98a824ef89fa2edc29,
title = "Understanding Adenovirus maturation: A nanomechanics approach",
abstract = "The ability of adenoviruses to infect a broad range of species and tissues has led to a widespread interest in their biological functioning. However, there remains a big gap in our understanding of their assembly and maturation pathways. Here, we present AFM (Atomic Force Microscopy) nanoindentation and fatigue studies1,2 of adenovirus capsids3 at different stages of maturation. Surprisingly, we find that the intermediate (no DNA) immature capsid is mechanically indistinguishable as compared with the mature (DNA filled), suggesting a major stabilizing role of the scaffold protein.3 However, these capsids have distinctly different disassembly pathways, as indicated by a mechanically-induced fatigue analysis. Additionally, we observed that mutation of the protease cleavage site of the precursor protein VI yields a maturation-intermediate capsid, G33A, which has reduced infectivity and releases half as many pentons as the WT capsid. The presented results strongly indicate that the reduced infectivity results from a reduction in protein VI exposure, partially inhibiting lysis of the endosome and leading to abortive infection.",
keywords = "proteinase, scaffold protein, Adenoviridae, atomic force microscopy, endosome, exposure, fatigue, gene inactivation, gene mutation, infection, lysis, maturation, molecular mechanics, nonhuman, precursor, virus capsid",
author = "D. Denning and S. Bennett and T. Mullen and C. Moyer and G.J. Wuite and G. Nemerow and W.H. Roos",
year = "2017",
month = "7",
day = "1",
doi = "10.1007/s00249-017-1222-x",
language = "English",
volume = "46",
pages = "S184",
journal = "European Biophysics Journal",
issn = "0175-7571",
number = "Supplement 1",

}

RIS

TY - JOUR

T1 - Understanding Adenovirus maturation: A nanomechanics approach

AU - Denning, D.

AU - Bennett, S.

AU - Mullen, T.

AU - Moyer, C.

AU - Wuite, G.J.

AU - Nemerow, G.

AU - Roos, W.H.

PY - 2017/7/1

Y1 - 2017/7/1

N2 - The ability of adenoviruses to infect a broad range of species and tissues has led to a widespread interest in their biological functioning. However, there remains a big gap in our understanding of their assembly and maturation pathways. Here, we present AFM (Atomic Force Microscopy) nanoindentation and fatigue studies1,2 of adenovirus capsids3 at different stages of maturation. Surprisingly, we find that the intermediate (no DNA) immature capsid is mechanically indistinguishable as compared with the mature (DNA filled), suggesting a major stabilizing role of the scaffold protein.3 However, these capsids have distinctly different disassembly pathways, as indicated by a mechanically-induced fatigue analysis. Additionally, we observed that mutation of the protease cleavage site of the precursor protein VI yields a maturation-intermediate capsid, G33A, which has reduced infectivity and releases half as many pentons as the WT capsid. The presented results strongly indicate that the reduced infectivity results from a reduction in protein VI exposure, partially inhibiting lysis of the endosome and leading to abortive infection.

AB - The ability of adenoviruses to infect a broad range of species and tissues has led to a widespread interest in their biological functioning. However, there remains a big gap in our understanding of their assembly and maturation pathways. Here, we present AFM (Atomic Force Microscopy) nanoindentation and fatigue studies1,2 of adenovirus capsids3 at different stages of maturation. Surprisingly, we find that the intermediate (no DNA) immature capsid is mechanically indistinguishable as compared with the mature (DNA filled), suggesting a major stabilizing role of the scaffold protein.3 However, these capsids have distinctly different disassembly pathways, as indicated by a mechanically-induced fatigue analysis. Additionally, we observed that mutation of the protease cleavage site of the precursor protein VI yields a maturation-intermediate capsid, G33A, which has reduced infectivity and releases half as many pentons as the WT capsid. The presented results strongly indicate that the reduced infectivity results from a reduction in protein VI exposure, partially inhibiting lysis of the endosome and leading to abortive infection.

KW - proteinase

KW - scaffold protein

KW - Adenoviridae

KW - atomic force microscopy

KW - endosome

KW - exposure

KW - fatigue

KW - gene inactivation

KW - gene mutation

KW - infection

KW - lysis

KW - maturation

KW - molecular mechanics

KW - nonhuman

KW - precursor

KW - virus capsid

U2 - 10.1007/s00249-017-1222-x

DO - 10.1007/s00249-017-1222-x

M3 - Meeting Abstract

VL - 46

SP - S184

JO - European Biophysics Journal

JF - European Biophysics Journal

SN - 0175-7571

IS - Supplement 1

ER -

ID: 46990415