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Title: Interaction of CSFV E2 protein with swine host factors as detected by yeast two-hybrid system

Author
item GLADUE, DOUGLAS - University Of Connecticut
item BAKER-BRANSTETTER, RYAN - Oak Ridge Institute For Science And Education (ORISE)
item Holinka-Patterson, Lauren
item FERNANDEZ-SAINZ, IGNACIO - University Of Connecticut
item O'DONNELL, VIVIAN - University Of Connecticut
item FLETCHER, PAIGE - Oak Ridge Institute For Science And Education (ORISE)
item LU, ZHIQIANG - Us Deparment Of Homeland Security
item Borca, Manuel

Submitted to: PLOS ONE
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 11/26/2013
Publication Date: 1/8/2014
Citation: Gladue, D.P., Baker-Branstetter, R., Holinka-Patterson, L.G., Fernandez-Sainz, I.J., O'Donnell, V., Fletcher, P., Lu, Z., Borca, M.V. 2014. Interaction of CSFV E2 protein with swine host factors as detected by yeast two-hybrid system . PLoS One. 9(1):e68532.

Interpretive Summary: Classical swine fever (CSFV) and bovine viral diarrhea virus (BVDV) cause important disease in swine and cattle respectively. Both are members of the same group of viruses known as pestiviruses. E2 is one of three proteins on the viral surface of pestiviruses that is involved in several critical functions, including virus entry into target cells, induction of the host protective immune response and determining virulence in animals. However, so far there is no information regarding the interactions that this important virus protein establishes with host proteins during the virus infection. Here, we utilized a well know methodology, the yeast two-hybrid system, to identify host cell proteins that specifically interact with E2 proteins of CSFV and BVDV. We were able to identify fifty-seven cellular proteins which bound E2 from both CSFV and BVDV. The binding sites for these cellular proteins on E2 are very dependent on protein structure. The possible roles of the identified host proteins are discussed as the results presented here will be important for future studies to elucidate mechanisms of host protein-virus interactions during pestivirus infection. This information can be utilized in the development of better vaccines to control these diseases.

Technical Abstract: E2 is one of the envelope glycoproteins of pestiviruses, including classical swine fever virus (CSFV) and bovine viral diarrhea virus (BVDV). E2 is involved in several critical functions, including virus entry into target cells, induction of a protective immune response and virulence in swine. However, there is no information regarding any host binding partners for the E2 proteins. Here, we utilized the yeast two-hybrid system and identified fifty-seven host proteins as positive binding partners which bound E2 from both CSFV and BVDV with the exception of two proteins that were found to be positive for binding only to CSFV E2. Alanine scanning of CSFV E2 demonstrated that the binding sites for these cellular proteins on E2 are likely non-linear binding sites. The possible roles of the identified host proteins are discussed as the results presented here will be important for future studies to elucidate mechanisms of host protein-virus interactions during pestivirus infection. However, due to the limitations of the yeast two hybrid system, the proteins identified is not exhaustive and each interaction identified needs to be confirmed by independent experimental approaches in the context of virus-infected cells before any definitive conclusion can be drawn on relevance for the virus life cycle.