title: Identification of two residues within the LDL-A module of Tva that dictate the altered receptor specificity of mutant subgroup A avian sarcoma and leukosis viruses.
abstract: Avian sarcoma and leukosis virus subgroup A (ASLV-A) entry is mediated by interactions between the viral glycoprotein EnvA and its cognate receptor Tva. Previously, some interesting mutants of ASLV-A have been selected by others which can use chicken Tva, but not quail Tva, for efficient entry. The mutant phenotypes are caused by two point mutations within the surface subunit of EnvA (S. L. Holmen, D. C. Melder, and M. J. Federspiel, J. Virol. 75:726-737, 2001). In this study, we have shown that the altered receptor specificity maps to the LDL-A module of Tva. Further, we have identified two residues in the chicken LDL-A module that allow more efficient viral entry by the mutant viruses. These results demonstrate that the altered receptor specificity of the mutant viruses is determined by specific interactions with residues in the LDL-A module of Tva.
authors.affiliation: Department of Microbiology and Immunology, College of Medicine, University of Illinois at Chicago, Chicago, IL 60612, USA.
authors.forename: Tia
authors.initials: T
authors.lastname: Rai
authors.forename: Michael
authors.initials: M
authors.lastname: Caffrey
authors.forename: Lijun
authors.initials: L
authors.lastname: Rong
mesh_terms: D000596:Amino Acids / Q000378:metabolism*; D000818:Animals; D001354:Avian Leukosis Virus / Q000378:metabolism*; D030161:Avian Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001358:Avian Sarcoma Viruses / Q000378:metabolism*; D002645:Chickens; D057927:Hydrophobic and Hydrophilic Interactions; D017434:Protein Structure, Tertiary; D011991:Receptors, Virus / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
chemical_list: D000596:Amino Acids; D030161:Avian Proteins; D011991:Receptors, Virus; C088745:Tva receptor