Mutations in Both the Surface and Transmembrane Envelope Glycoproteins of the RAV-2 Subgroup B Avian Sarcoma and Leukosis Virus Are Required to Escape the Antiviral Effect of a Secreted Form of the TvbS3 Receptor †
- Resource Type
- Authors
- William S. Payne; Mark J. Federspiel; Xueqian Yin; Deborah C. Melder; Jerry B. Dodgson
- Source
- Viruses
Volume 11
Issue 6
- Subject
- 0301 basic medicine
receptor usage
030106 microbiology
Mutant
Chick Embryo
Alpharetrovirus
Biology
Virus Replication
Article
Virus
Cell Line
03 medical and health sciences
Viral Envelope Proteins
Viral envelope
Viral entry
Virology
Animals
chemistry.chemical_classification
Avian Leukosis Virus
Lipid bilayer fusion
biology.organism_classification
Transmembrane protein
030104 developmental biology
Infectious Diseases
Avian Sarcoma Viruses
chemistry
Mutation
avian sarcoma and leukosis viruses
Receptors, Virus
Glycoprotein
envelope glycoprotein evolution
Chickens
- Language
- ISSN
- 1999-4915
The subgroup A through E avian sarcoma and leukosis viruses ASLV(A) through ASLV(E) are a group of highly related alpharetroviruses that have evolved to use very different host protein families as receptors. We have exploited genetic selection strategies to force the replication-competent ASLVs to naturally evolve and acquire mutations to escape the pressure on virus entry and yield a functional replicating virus. In this study, evolutionary pressure was exerted on ASLV(B) virus entry and replication using a secreted for of its Tvb receptor. As expected, mutations in the ASLV(B) surface glycoprotein hypervariable regions were selected that knocked out the ability for the mutant glycoprotein to bind the sTvbS3-IgG inhibitor. However, the subgroup B Rous associated virus 2 (RAV-2) also required additional mutations in the C-terminal end of the SU glycoprotein and multiple regions of TM highlighting the importance of the entire viral envelope glycoprotein trimer structure to mediate the entry process efficiently. These mutations altered the normal two-step ASLV membrane fusion process to enable infection.