PMID- 20484506
OWN - NLM
STAT- MEDLINE
DCOM- 20100720
LR  - 20211020
IS  - 1098-5514 (Electronic)
IS  - 0022-538X (Print)
IS  - 0022-538X (Linking)
VI  - 84
IP  - 15
DP  - 2010 Aug
TI  - Congregation of orthopoxvirus virions in cytoplasmic A-type inclusions is 
      mediated by interactions of a bridging protein (A26p) with a matrix protein 
      (ATIp) and a virion membrane-associated protein (A27p).
PG  - 7592-602
LID - 10.1128/JVI.00704-10 [doi]
AB  - Some orthopoxviruses, e.g., the cowpox, ectromelia, and raccoonpox viruses, form 
      large, discrete cytoplasmic inclusions within which mature virions (MVs) are 
      embedded by a process called occlusion. These inclusions, which may protect 
      occluded MVs in the environment, are composed of aggregates of the A-type 
      inclusion protein (ATIp), which is truncated in orthopoxviruses such as vaccinia 
      virus (VACV) and variola virus that fail to form inclusions. In addition to an 
      intact ATIp, occlusion requires the A26 protein (A26p). Although VACV contains a 
      functional A26p, determined by complementation of a cowpox virus 
      occlusion-defective mutant, its role in occlusion was unknown. We found that 
      restoration of the full-length ATI gene was sufficient for VACV inclusion 
      formation and the ensuing occlusion of MVs. A26p was present in inclusions even 
      when virion assembly was inhibited, suggesting a direct interaction of A26p with 
      ATIp. Analysis of a panel of ATIp mutants indicated that the C-terminal repeat 
      region was required for inclusion formation and the N-terminal domain for 
      interaction with A26p and occlusion. A26p is tethered to MVs via interaction with 
      the A27 protein (A27p); A27p was not required for association of A26p with ATIp 
      but was necessary for occlusion. In addition, the C-terminal domain of A26p, 
      which mediates A26p-A27p interactions, was necessary but insufficient for 
      occlusion. Taken together, the data suggest a model for occlusion in which A26p 
      has a bridging role between ATIp and A27p, and A27p provides a link to the MV 
      membrane.
FAU - Howard, Amanda R
AU  - Howard AR
AD  - Laboratory of Viral Diseases, National Institute of Allergy and Infectious 
      Diseases, National Institutes of Health, Bethesda, Maryland 20892-3210, USA.
FAU - Weisberg, Andrea S
AU  - Weisberg AS
FAU - Moss, Bernard
AU  - Moss B
LA  - eng
GR  - Intramural NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Intramural
DEP - 20100519
PL  - United States
TA  - J Virol
JT  - Journal of virology
JID - 0113724
RN  - 0 (A27 protein, vaccinia virus)
RN  - 0 (ATI protein, Vaccinia virus)
RN  - 0 (Carrier Proteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Viral Fusion Proteins)
RN  - 0 (Viral Proteins)
SB  - IM
MH  - Animals
MH  - Carrier Proteins/*metabolism
MH  - Cell Line
MH  - Chlorocebus aethiops
MH  - Humans
MH  - *Inclusion Bodies, Viral
MH  - Membrane Proteins
MH  - Protein Binding
MH  - *Protein Interaction Mapping
MH  - Vaccinia virus/*physiology
MH  - Viral Fusion Proteins/*metabolism
MH  - Viral Proteins/*metabolism
MH  - *Virus Assembly
PMC - PMC2897617
EDAT- 2010/05/21 06:00
MHDA- 2010/07/21 06:00
PMCR- 2011/02/01
CRDT- 2010/05/21 06:00
PHST- 2010/05/21 06:00 [entrez]
PHST- 2010/05/21 06:00 [pubmed]
PHST- 2010/07/21 06:00 [medline]
PHST- 2011/02/01 00:00 [pmc-release]
AID - JVI.00704-10 [pii]
AID - 0704-10 [pii]
AID - 10.1128/JVI.00704-10 [doi]
PST - ppublish
SO  - J Virol. 2010 Aug;84(15):7592-602. doi: 10.1128/JVI.00704-10. Epub 2010 May 19.