Aromatic interactions define the binding of the alphavirus spike to its nucleocapsid
Skoging, U ; Vihinen, Mauno LU
; Nilsson, L
and Liljestrom, P
(1996)
In Structure
4(5).
p.519-529
- Abstract
- Background: Most enveloped viruses bud from infected cells by a process in which viral intracellular core components interact with cytoplasmic domains of transmembrane spike glycoproteins. We have demonstrated previously that a tyrosine motif in the cytoplasmic domain of the Semliki Forest virus (SFV) spike glycoprotein E2 is absolutely essential for budding, In contrast, hardly anything is known regarding which region of the capsid protein is involved in spike binding, Therefore, the mechanism by which spikes are selectively sorted into the viral bud or by which energy is provided for envelopment, remains unclear, Results: Molecular models of the SFV capsid protein (SFCP) and the cytoplasmic domain of the spike protein were fitted as a... (More)
- Background: Most enveloped viruses bud from infected cells by a process in which viral intracellular core components interact with cytoplasmic domains of transmembrane spike glycoproteins. We have demonstrated previously that a tyrosine motif in the cytoplasmic domain of the Semliki Forest virus (SFV) spike glycoprotein E2 is absolutely essential for budding, In contrast, hardly anything is known regarding which region of the capsid protein is involved in spike binding, Therefore, the mechanism by which spikes are selectively sorted into the viral bud or by which energy is provided for envelopment, remains unclear, Results: Molecular models of the SFV capsid protein (SFCP) and the cytoplasmic domain of the spike protein were fitted as a basis for a reverse genetics approach to characterizing the interaction between these two proteins: Biochemical analysis of mutants defined a hydrophobic pocket of the capsid protein that is involved both in spike binding and nucleocapsid assembly, Conclusions: We suggest that aromatic residues in the capsid protein serve to bind the side chain of the essential E2 tyrosine providing both specificity for spike incorporation and energy for budding. The same hydrophobic pocket also appears to play a role in capsid assembly. Furthermore, the results suggest that budding may occur in the absence of preformed nucleocapsids. This is the first demonstration of the molecular mechanisms of spike-nucleocapsid interactions during virus budding. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/3853088
- author
- Skoging, U
; Vihinen, Mauno
LU
; Nilsson, L
and Liljestrom, P
- publishing date
- 1996
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- alphavirus, Semliki Forest virus, tyrosine signal, virus assembly, virus, budding
- in
- Structure
- volume
- 4
- issue
- 5
- pages
- 519 - 529
- publisher
- Cell Press
- external identifiers
-
- wos:A1996UP28900005
- scopus:0030585135
- ISSN
- 0969-2126
- DOI
- 10.1016/S0969-2126(96)00058-5
- language
- English
- LU publication?
- no
- id
- d829b53c-7f4a-4c94-8895-01ac5732670d (old id 3853088)
- date added to LUP
- 2016-04-01 11:44:06
- date last changed
- 2022-04-05 04:17:14
@article{d829b53c-7f4a-4c94-8895-01ac5732670d,
abstract = {{Background: Most enveloped viruses bud from infected cells by a process in which viral intracellular core components interact with cytoplasmic domains of transmembrane spike glycoproteins. We have demonstrated previously that a tyrosine motif in the cytoplasmic domain of the Semliki Forest virus (SFV) spike glycoprotein E2 is absolutely essential for budding, In contrast, hardly anything is known regarding which region of the capsid protein is involved in spike binding, Therefore, the mechanism by which spikes are selectively sorted into the viral bud or by which energy is provided for envelopment, remains unclear, Results: Molecular models of the SFV capsid protein (SFCP) and the cytoplasmic domain of the spike protein were fitted as a basis for a reverse genetics approach to characterizing the interaction between these two proteins: Biochemical analysis of mutants defined a hydrophobic pocket of the capsid protein that is involved both in spike binding and nucleocapsid assembly, Conclusions: We suggest that aromatic residues in the capsid protein serve to bind the side chain of the essential E2 tyrosine providing both specificity for spike incorporation and energy for budding. The same hydrophobic pocket also appears to play a role in capsid assembly. Furthermore, the results suggest that budding may occur in the absence of preformed nucleocapsids. This is the first demonstration of the molecular mechanisms of spike-nucleocapsid interactions during virus budding.}},
author = {{Skoging, U and Vihinen, Mauno and Nilsson, L and Liljestrom, P}},
issn = {{0969-2126}},
keywords = {{alphavirus; Semliki Forest virus; tyrosine signal; virus assembly; virus; budding}},
language = {{eng}},
number = {{5}},
pages = {{519--529}},
publisher = {{Cell Press}},
series = {{Structure}},
title = {{Aromatic interactions define the binding of the alphavirus spike to its nucleocapsid}},
url = {{http://dx.doi.org/10.1016/S0969-2126(96)00058-5}},
doi = {{10.1016/S0969-2126(96)00058-5}},
volume = {{4}},
year = {{1996}},
}