Major capsid reinforcement by a minor protein in herpesviruses and phage.
Sae-Ueng, Udom ; Liu, Ting ; Catalano, Carlos Enrique ; Huffman, Jamie B ; Homa, Fred L and Evilevitch, Alex LU
(2014)
In Nucleic Acids Research
42(14).
p.9096-9107
- Abstract
- Herpes simplex type 1 virus (HSV-1) and bacteriophage λ capsids undergo considerable structural changes during self-assembly and DNA packaging. The initial steps of viral capsid self-assembly require weak, non-covalent interactions between the capsid subunits to ensure free energy minimization and error-free assembly. In the final stages of DNA packaging, however, the internal genome pressure dramatically increases, requiring significant capsid strength to withstand high internal genome pressures of tens of atmospheres. Our data reveal that the loosely formed capsid structure is reinforced post-assembly by the minor capsid protein UL25 in HSV-1 and gpD in bacteriophage λ. Using atomic force microscopy nano-indentation analysis, we show... (More)
- Herpes simplex type 1 virus (HSV-1) and bacteriophage λ capsids undergo considerable structural changes during self-assembly and DNA packaging. The initial steps of viral capsid self-assembly require weak, non-covalent interactions between the capsid subunits to ensure free energy minimization and error-free assembly. In the final stages of DNA packaging, however, the internal genome pressure dramatically increases, requiring significant capsid strength to withstand high internal genome pressures of tens of atmospheres. Our data reveal that the loosely formed capsid structure is reinforced post-assembly by the minor capsid protein UL25 in HSV-1 and gpD in bacteriophage λ. Using atomic force microscopy nano-indentation analysis, we show that the capsid becomes stiffer upon binding of UL25 and gpD due to increased structural stability. At the same time the force required to break the capsid increases by ∼70% for both herpes and phage. This demonstrates a universal and evolutionarily conserved function of the minor capsid protein: facilitating the retention of the pressurized viral genome in the capsid. Since all eight human herpesviruses have UL25 orthologs, this discovery offers new opportunities to interfere with herpes replication by disrupting the precise force balance between the encapsidated DNA and the capsid proteins crucial for viral replication. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/4581445
- author
- Sae-Ueng, Udom
; Liu, Ting
; Catalano, Carlos Enrique
; Huffman, Jamie B
; Homa, Fred L
and Evilevitch, Alex
LU
- organization
- publishing date
- 2014
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Nucleic Acids Research
- volume
- 42
- issue
- 14
- pages
- 9096 - 9107
- publisher
- Oxford University Press
- external identifiers
-
- pmid:25053840
- wos:000343219200029
- scopus:84906220782
- pmid:25053840
- ISSN
- 1362-4962
- DOI
- 10.1093/nar/gku634
- language
- English
- LU publication?
- yes
- id
- 89a4cfc0-c268-45ce-ab86-d21ec063db9a (old id 4581445)
- date added to LUP
- 2016-04-01 11:06:38
- date last changed
- 2022-04-05 00:05:38
@article{89a4cfc0-c268-45ce-ab86-d21ec063db9a,
abstract = {{Herpes simplex type 1 virus (HSV-1) and bacteriophage λ capsids undergo considerable structural changes during self-assembly and DNA packaging. The initial steps of viral capsid self-assembly require weak, non-covalent interactions between the capsid subunits to ensure free energy minimization and error-free assembly. In the final stages of DNA packaging, however, the internal genome pressure dramatically increases, requiring significant capsid strength to withstand high internal genome pressures of tens of atmospheres. Our data reveal that the loosely formed capsid structure is reinforced post-assembly by the minor capsid protein UL25 in HSV-1 and gpD in bacteriophage λ. Using atomic force microscopy nano-indentation analysis, we show that the capsid becomes stiffer upon binding of UL25 and gpD due to increased structural stability. At the same time the force required to break the capsid increases by ∼70% for both herpes and phage. This demonstrates a universal and evolutionarily conserved function of the minor capsid protein: facilitating the retention of the pressurized viral genome in the capsid. Since all eight human herpesviruses have UL25 orthologs, this discovery offers new opportunities to interfere with herpes replication by disrupting the precise force balance between the encapsidated DNA and the capsid proteins crucial for viral replication.}},
author = {{Sae-Ueng, Udom and Liu, Ting and Catalano, Carlos Enrique and Huffman, Jamie B and Homa, Fred L and Evilevitch, Alex}},
issn = {{1362-4962}},
language = {{eng}},
number = {{14}},
pages = {{9096--9107}},
publisher = {{Oxford University Press}},
series = {{Nucleic Acids Research}},
title = {{Major capsid reinforcement by a minor protein in herpesviruses and phage.}},
url = {{http://dx.doi.org/10.1093/nar/gku634}},
doi = {{10.1093/nar/gku634}},
volume = {{42}},
year = {{2014}},
}