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ARS Home » Midwest Area » Ames, Iowa » National Animal Disease Center » Ruminant Diseases and Immunology Research » Research » Publications at this Location » Publication #266484

Title: Molecular biology of bovine viral diarrhea virus

Author
item Neill, John

Submitted to: Biologicals
Publication Type: Review Article
Publication Acceptance Date: 7/6/2012
Publication Date: 1/1/2013
Citation: Neill, J.D. 2013. Molecular biology of bovine viral diarrhea virus. Biologicals. 41:2-7.

Interpretive Summary: Bovine viral diarrhea virus (BVDV) is ubiquitous world-wide and is an important pathogen of cattle. It can have a profound impact on production and is known to facilitate infections by secondary pathogens. This paper is a review article describing the molecular biology of BVDV. It is meant to serve as a reference for the biology of BVDV for the readers of the special edition of Biologicals entitled “Aspects of immunology of bovine viral diarrhea virus”. The paper describes the recent knowledge of BVDV from replication to function of viral proteins to aspects of viral genome sequence diversity.

Technical Abstract: Bovine viral diarrhea viruses (BVDV) are arguably the most important viral pathogen of ruminants worldwide and can cause severe economic loss. Clinical symptoms of the disease caused by BVDV range from subclinical to severe acute hemorrhagic syndrome, with the severity of disease being strain dependent. These viruses are classified as members of the Pestivirus genus of the Flaviviridae. BVDV are considered primarily a pathogen of cattle but can infect most ruminant species. The virus particle consists of a lipid bilayer membrane surrounding the encapsidated genomic RNA. Inserted in the outer membrane are two virus-encoded glycoproteins that contain the major antigenic determinants of the virus as well as receptor binding and cell fusion functions. A third glycoprotein is weakly associated with the virion, but also possesses unique features that play important roles in suppression of innate immunity. The viral proteins are proteolytically cleaved from the polyprotein by different proteases. The viral proteins are encoded in a single, large open reading frame. The structural proteins are processed by cellular signal peptidases while the processing of the nonstructural proteins is by the viral serine protease. The virus is assembled and matures in the endoplasmic reticulum and golgi bodies of the cell. The virus is released via exocytosis, where viral proteins are not exposed on the surface of the cell.