Selection of a Subgroup A Avian Leukosis Virus [ALV(A)] Envelope Resistant to Soluble ALV(A) Surface Glycoprotein

The host developing resistance to retroviral infection is believed to be a major force in the evolution of multiple receptor usage by retroviruses. The avian leukosis–sarcoma virus (ALV) group of retroviruses provides a powerful system for studying the envelope–receptor interactions involved in retr...

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Bibliographic Details
Published in:Virology (New York, N.Y.) N.Y.), 2000-08, Vol.273 (2), p.364-373
Main Authors: Holmen, Sheri L., Federspiel, Mark J.
Format: Article
Language:English
Subjects:
Alpharetrovirus
Amino Acid Sequence
Animals
Avian leukosis virus
Capsid
Capsid Proteins
Cell Separation
Chickens
Cloning, Molecular
Enzyme-Linked Immunosorbent Assay
Flow Cytometry
Molecular Sequence Data
Rabbits
Receptors, IgG - metabolism
Retroviridae Proteins
Viral Core Proteins
Viral Envelope Proteins - metabolism
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Summary:The host developing resistance to retroviral infection is believed to be a major force in the evolution of multiple receptor usage by retroviruses. The avian leukosis–sarcoma virus (ALV) group of retroviruses provides a powerful system for studying the envelope–receptor interactions involved in retrovirus entry; different members of this group of closely related viruses use distinct cellular receptors. Analysis of the ALV envelope subgroups suggests that the different ALVs evolved from a common ancestor by mutations in the env gene. Cells and animals that express subgroup A ALV envelope glycoproteins are highly resistant to ALV(A) infection due to receptor interference. In this study, we tested whether expression of a soluble form of subgroup A surface glycoprotein (SU) would result in receptor interference and whether this interference would select for resistant viruses with altered receptor usage. Chicken cells expressing the secreted ALV(A) SU immunoadhesin SU(A)-rIgG, which contains the subgroup A SU domain fused to the constant region of a rabbit immunoglobulin (IgG) heavy chain, showed significant receptor interference. A variant virus resistant to SU(A)-rIgG receptor interference was obtained. This virus had a six-amino-acid deletion in the subgroup A hr1 that altered receptor usage. This approach may identify regions of SU that play a critical role in receptor specificity.
ISSN:0042-6822
1096-0341
DOI:10.1006/viro.2000.0424