ReviewViruses2019
Reverse Engineering Provides Insights on the Evolution of Subgroups A to E Avian Sarcoma and Leukosis Virus Receptor Specificity.
Review in Viruses, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
20 citing papers in PubMed, 33 citations in OpenAlex.
- Residues Y142, I143, T146, Q206, S215, R228, G267, and M268 in the surface glycoprotein of FGV-like subgroup A avian leukosis virus are the key sites determining Tva receptor binding and infectivity.Veterinary research · 2026Article
- Research Progress on Pathogenesis and Prevention of Avian Leukosis Virus J Subgroup (ALV-J).Veterinary sciences · 2026Review
- A review of genetic variation underlying chicken phenotypic diversity.Poultry science · 2025Review
- Multi-clade co-evolution and differential replication efficiencies of subgroup A avian leukosis virus in Chinese guinea fowl.BMC veterinary research · 2025Article
- A Simple and Adaptable Method for Cloning Genes Into Transposon Vectors Using Topo and Restriction Systems for Chicken Embryo Transgenesis.Bio-protocol · 2025Article
- Single Amino Acid Residue W33 ofViruses · 2025Article
- Isolation and molecular characterization of subgroup J avian leukosis virus in native chicken breeds of China during 2022-2025.Frontiers in microbiology · 2025Article
- N123I mutation in the ALV-J receptor-binding domain region enhances viral replication ability by increasing the binding affinity with chNHE1.PLoS pathogens · 2024Article
- Simultaneous Detection of Three Subgroups of Avian Leukosis Virus Using the Nanoparticle-Assisted PCR Assay.Viruses · 2023Article
- Avian Leukosis: Will We Be Able to Get Rid of It?Animals : an open access journal from MDPI · 2023Review
- Unique Structure and Distinctive Properties of the Ancient and Ubiquitous Gamma-Type Envelope Glycoprotein.Viruses · 2023Review
- Residues L55 and W69 of Tva Mediate Entry of Subgroup A Avian Leukosis Virus.Journal of virology · 2022Article
- The key amino acid sites 199-205, 269, 319, 321 and 324 of ALV-K env contribute to the weaker replication capacity of ALV-K than ALV-A.Retrovirology · 2022Article
- Chicken hepatomegaly and splenomegaly associated with novel subgroup J avian leukosis virus infection.BMC veterinary research · 2022Article
- Residues 140-142, 199-200, 222-223, and 262 in the Surface Glycoprotein of Subgroup A Avian Leukosis Virus Are the Key Sites Determining Tva Receptor Binding Affinity and Infectivity.Frontiers in microbiology · 2022Article
- Knock-Out of Retrovirus Receptor GeneViruses · 2021Article
- Novel mutation of avian leukosis virus subgroup J from Tibetan chickens.Poultry science · 2021Article
- The Bipartite Sequence Motif in the N and C Termini of gp85 of Subgroup J Avian Leukosis Virus Plays a Crucial Role in Receptor Binding and Viral Entry.Journal of virology · 2020Article
- Single Amino Acids G196 and R198 in hr1 of Subgroup K Avian Leukosis Virus Glycoprotein Are Critical for Tva Receptor Binding.Frontiers in microbiology · 2020Article
- Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The initial step of retrovirus entry-the interaction between the virus envelope glycoprotein trimer and a cellular receptor-is complex, involving multiple, noncontiguous determinants in both proteins that specify receptor choice, binding affinity and the ability to trigger conformational changes in the viral glycoproteins. Despite the complexity of this interaction, retroviruses have the ability to evolve the structure of their envelope glycoproteins to use a different cellular protein as receptors. The highly homologous subgroup A to E Avian Sarcoma and Leukosis Virus (ASLV) glycoproteins belong to the group of class 1 viral fusion proteins with a two-step triggering mechanism that allows experimental access to intermediate structures during the fusion process. We and others have taken advantage of replication-competent ASLVs and exploited genetic selection strategies to force the ASLVs to naturally evolve and acquire envelope glycoprotein mutations to escape the pressure on virus entry and still yield a functional replicating virus. This approach allows for the simultaneous selection of multiple mutations in multiple functional domains of the envelope glycoprotein that may be required to yield a functional virus. Here, we review the ASLV family and experimental system and the reverse engineering approaches used to understand the evolution of ASLV receptor usage.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.