PMID- 29577951
OWN - NLM
STAT- MEDLINE
DCOM- 20180918
LR  - 20180918
IS  - 1872-7492 (Electronic)
IS  - 0168-1702 (Linking)
VI  - 249
DP  - 2018 Apr 2
TI  - Interaction of porcine reproductive and respiratory syndrome virus major envelope 
      proteins GP5 and M with the cellular protein Snapin.
PG  - 85-92
LID - S0168-1702(17)30947-4 [pii]
LID - 10.1016/j.virusres.2018.03.010 [doi]
AB  - BACKGROUND: Porcine reproductive and respiratory syndrome (PRRS) is characterized 
      by abortions in pregnant sows and respiratory disease, particularly in young 
      pigs. The causative agent is porcine reproductive and respiratory syndrome virus 
      (PRRSV), a member of the arterivirus family. GP5 and M are the major envelope 
      proteins encoded by PRRSV. To further characterize these two viral proteins, a 
      yeast two-hybrid approach was utilized to identify interacting partners of PRRSV 
      GP5 and M proteins. METHODS: Interacting partners of PRRSV GP5 and M were 
      identified using a porcine macrophage cDNA library yeast two-hybrid screen. 
      Subsequently, the interactions between PRRSV GP5/M and the cellular protein 
      Snapin were mapped using truncated versions of the GP5 and M proteins in a yeast 
      two-hybrid assay to localize the interactions. The Snapin gene from the African 
      green monkey kidney cell line MARC-145, which is permissive to PRRSV, was cloned 
      and sequenced, and compared to porcine Snapin. Cellular Snapin expression was 
      reduced in PRRSV-infected cells via Snapin-specific siRNA targeting. RESULTS: 
      Here we show that the cellular Snap-Associated Protein (Snapin), an accessory 
      protein of the SNARE membrane fusion network and also a member of the BLOC-1 
      complex, specifically interacts with GP5 and M. Inhibition of Snapin expression 
      via siRNA targeting of Snapin results in the reduction of PRRSV replication. 
      CONCLUSIONS: The PRRSV GP5 and M proteins are known to form a heterodimeric 
      complex which is important for viral structure and infectivity, and both PRRSV 
      proteins can interact with cellular Snapin. Snapin knock-down suggests these 
      interactions could be important in the PRRSV lifecycle. GP5 and M proteins may 
      interact with Snapin to exploit its roles in intracellular transport and membrane 
      fusion.
CI  - Published by Elsevier B.V.
FAU - Hicks, Julie A
AU  - Hicks JA
AD  - Department of Animal Science, North Carolina State University, Raleigh, NC, USA. 
      Electronic address: jahicks3@ncsu.edu.
FAU - Yoo, Dongwan
AU  - Yoo D
AD  - Department of Pathobiology, University of Illinois at Urbana-Champaign, Urbana, 
      IL, USA. Electronic address: dyoo@illinois.edu.
FAU - Liu, Hsiao-Ching
AU  - Liu HC
AD  - Department of Animal Science, North Carolina State University, Raleigh, NC, USA. 
      Electronic address: hc_liu@ncsu.edu.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
DEP - 20180322
PL  - Netherlands
TA  - Virus Res
JT  - Virus research
JID - 8410979
RN  - 0 (M protein, porcine reproductive and respiratory syndrome virus)
RN  - 0 (Vesicular Transport Proteins)
RN  - 0 (Viral Envelope Proteins)
RN  - 0 (Viral Matrix Proteins)
RN  - 0 (glycoprotein 5, PRRSV)
SB  - IM
MH  - Animals
MH  - Gene Expression Profiling
MH  - Gene Knockdown Techniques
MH  - *Host-Pathogen Interactions
MH  - Macrophages/virology
MH  - Porcine respiratory and reproductive syndrome virus/*physiology
MH  - Protein Binding
MH  - *Protein Interaction Mapping
MH  - Swine
MH  - Two-Hybrid System Techniques
MH  - Vesicular Transport Proteins/genetics/*metabolism
MH  - Viral Envelope Proteins/*metabolism
MH  - Viral Matrix Proteins/*metabolism
MH  - Virus Replication
OTO - NOTNLM
OT  - BLOC-1 complex
OT  - GP5
OT  - M
OT  - PRRSV
OT  - SNARE complex
OT  - Snapin
EDAT- 2018/03/27 06:00
MHDA- 2018/09/19 06:00
CRDT- 2018/03/27 06:00
PHST- 2017/12/22 00:00 [received]
PHST- 2018/03/18 00:00 [revised]
PHST- 2018/03/19 00:00 [accepted]
PHST- 2018/03/27 06:00 [pubmed]
PHST- 2018/09/19 06:00 [medline]
PHST- 2018/03/27 06:00 [entrez]
AID - S0168-1702(17)30947-4 [pii]
AID - 10.1016/j.virusres.2018.03.010 [doi]
PST - ppublish
SO  - Virus Res. 2018 Apr 2;249:85-92. doi: 10.1016/j.virusres.2018.03.010. Epub 2018 
      Mar 22.