Divergent roles of ß- and γ-actin isoforms during spread of vaccinia virus.
Cytoskeleton (Hoboken)
; 74(4): 170-183, 2017 Apr.
Article
in En
| MEDLINE
| ID: mdl-28218453
ABSTRACT
Actin is a major component of the cytoskeleton and is present as two isoforms in non-muscle cells ß- and γ-cytoplasmic actin. These isoforms are strikingly conserved, differing by only four N-terminal amino acids. During spread from infected cells, vaccinia virus (VACV) particles induce localized actin nucleation that propel virus to surrounding cells and facilitate cell-to-cell spread of infection. Here we show that virus-tipped actin comets are composed of ß- and γ-actin. We employed isoform-specific siRNA knockdown to examine the role of the two isoforms in VACV-induced actin comets. Despite the high level of similarity between the actin isoforms, and their colocalization, VACV-induced actin nucleation was dependent exclusively on ß-actin. Knockdown of ß-actin led to a reduction in the release of virus from infected cells, a phenotype dependent on virus-induced Arp2/3 complex activity. We suggest that local concentrations of actin isoforms may regulate the activity of cellular actin nucleator complexes.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Vaccinia virus
/
Actins
/
Protein Isoforms
Limits:
Humans
Language:
En
Journal:
Cytoskeleton (Hoboken)
Year:
2017
Document type:
Article
Affiliation country: