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Journal of Virology, March 2008, p. 2097-2105, Vol. 82, No. 5
0022-538X/08/$08.00+0     doi:10.1128/JVI.02206-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

A Single-Amino-Acid Substitution in the TvbS1 Receptor Results in Decreased Susceptibility to Infection by Avian Sarcoma and Leukosis Virus Subgroups B and D and Resistance to Infection by Subgroup E In Vitro and In Vivo{triangledown}

Markéta Reinisová,1,§ Filip Senigl,1,§ Xueqian Yin,2 Jirí Plachy,1 Josef Geryk,1 Daniel Elleder,1,{dagger} Jan Svoboda,1 Mark J. Federspiel,2* and Jirí Hejnar1*

Department of Cellular and Viral Genetics, Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, Prague, Czech Republic,1 Department of Molecular Medicine, Mayo Clinic, Rochester, Minnesota2

Received 9 October 2007/ Accepted 10 December 2007

The avian sarcoma and leukosis virus (ASLV) family of retroviruses contains five highly related envelope subgroups (A to E) thought to have evolved from a common viral ancestor in the chicken population. Three genetic loci in chickens determine the susceptibility or resistance of cells to infection by the subgroup A to E ASLVs. Some inbred lines of chickens display phenotypes that are somewhere in between either efficiently susceptible or resistant to infection by specific subgroups of ASLV. The tvb gene encodes the receptor for subgroups B, D, and E ASLVs. The wild-type TvbS1 receptor confers susceptibility to subgroups B, D, and E ASLVs. In this study, the genetic defect that accounts for the altered susceptibility of an inbred chicken line, line M, to infection by ASLV(B), ASLV(D), and ASLV(E) was identified. The tvb gene in line M, tvbr2, encodes a mutant TvbS1 receptor protein with a substitution of a serine for a cysteine at position 125 (C125S). Here, we show that the C125S substitution in TvbS1 significantly reduces the susceptibility of line M cells to infection by ASLV(B) and ASLV(D) and virtually eliminates susceptibility to ASLV(E) infection both in cultured cells and in the incidence and growth of avian sarcoma virus-induced sarcomas in chickens. The C125S substitution significantly reduces the binding affinity of the TvbS1 receptor for the subgroup B, D, and E ASLV envelope glycoproteins. These are the first results that demonstrate a possible role of the cysteine-rich domain 3 in the function of the Tvb receptors.

* Corresponding author. Mailing address for J. Hejnar: Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, Vídenská 1083, CZ-14220 Prague 4, Czech Republic. Phone: 420 296 443 443. Fax: 420 223 410 955. E-mail: hejnar{at}img.cas.cz. Mailing address for Mark J. Federspiel: Department of Molecular Medicine, Mayo Clinic, 200 First St., SW, Rochester, MN 55905. Phone: (507) 284-8895. Fax: (507) 266-2122. E-mail: federspiel.mark{at}mayo.edu

{triangledown} Published ahead of print on 19 December 2007.

§ M.R. and F.S. contributed equally to this work.

{dagger} Present address: The Infectious Disease Laboratory, The Salk Institute, La Jolla, San Diego, CA 92037-1099.

Journal of Virology, March 2008, p. 2097-2105, Vol. 82, No. 5
0022-538X/08/$08.00+0     doi:10.1128/JVI.02206-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.





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