title: Identification of amino acid changes in the envelope glycoproteins of bovine viral diarrhea viruses isolated from alpaca that may be involved in host adaptation.
abstract: Bovine viral diarrhea viruses (BVDV) are most commonly associated with infections of cattle. However, BVDV are often isolated from closely related ruminants with a number of BVDV-1b viruses being isolated from alpacas that were both acutely and persistently infected. The complete nucleotide sequence of the open reading frame of eleven alpaca-adapted BVDV isolates and the region encoding the envelope glycoproteins of an additional three isolates were determined. With the exception of one, all alpaca isolates were >99.2% similar at the nucleotide level. The Hercules isolate was more divergent, with 95.7% sequence identity to the other viruses. Sequence similarity of the 14 viruses indicated they were isolates of a single BVDV strain that had adapted to and were circulating through alpaca herds. Hercules was a more distantly related strain that has been isolated only once in Canada and represented a separate adaptation event that possessed the same adaptive changes. Comparison of amino acid sequences of alpaca and bovine-derived BVDV strains revealed three regions with amino acid sequences unique to all alpaca isolates. The first contained two small in-frame deletions near the N-terminus of the E2 glycoprotein. The second was found near the C-terminus of the E2 protein where four altered amino acids were located within a 30 amino acid domain that participates in E2 homodimerization. The third region contained three variable amino acids in the C-terminus of the E(rns) within the amphipathic helix membrane anchor. These changes were found in the polar side of the amphipathic helix and resulted in an increased charge within the polar face. Titration of bovine and alpaca viruses in both bovine and alpaca cells indicated that with increased charge in the amphipathic helix, the ability to infect alpaca cells also increased.
authors.affiliation: USDA, Agricultural Research Service, National Animal Disease Center, Ruminant Diseases and Immunology Research Unit, 1920 Dayton Avenue, Ames, IA 50010, USA. Electronic address: john.neill@ars.usda.gov.
authors.forename: John D
authors.initials: JD
authors.lastname: Neill
authors.affiliation: Animal Health Diagnostic Center, College of Veterinary Medicine, Cornell University, Ithaca, NY, USA.
authors.forename: Edward J
authors.initials: EJ
authors.lastname: Dubovi
authors.affiliation: USDA, Agricultural Research Service, National Animal Disease Center, Ruminant Diseases and Immunology Research Unit, 1920 Dayton Avenue, Ames, IA 50010, USA.
authors.forename: Julia F
authors.initials: JF
authors.lastname: Ridpath
mesh_terms: D000222:Adaptation, Physiological; D000595:Amino Acid Sequence; D000596:Amino Acids; D000818:Animals; D002161:Camelids, New World / Q000821:virology*; D002170:Canada; D002417:Cattle; D001908:Diarrhea Viruses, Bovine Viral / Q000235:genetics / Q000302:isolation & purification / Q000502:physiology*; D015967:Gene Expression Regulation, Viral / Q000502:physiology; D014759:Viral Envelope Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
chemical_list: D000596:Amino Acids; D014759:Viral Envelope Proteins
keywords: Camelid; Genetic change; Host adaptation; Persistent infection; Phylogenetic analysis