ArticleProceedings of the National Academy of Sciences of the United States of America2006
Na+/H+ exchanger type 1 is a receptor for pathogenic subgroup J avian leukosis virus.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 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.
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Who cites it
65 citing papers in PubMed, 100 citations in OpenAlex.
- Genetic mutations within tva receptor gene confer resistance to ALV-A and ALV-K infection in chickens.Poultry science · 2026Article
- Role of O-linked glycosylation modification on internalization and replication of avian leukosis virus subgroup J.Veterinary research · 2026Article
- Deciphering host-virus interaction networks in ALV infection: an integrative multi-omics perspective.Frontiers in immunology · 2026Review
- A review of genetic variation underlying chicken phenotypic diversity.Poultry science · 2025Review
- Isolation and identification of avian leukosis virus subgroup J from Luohé Ma chicken.Virus genes · 2025Article
- Precise Editing of chNHE1 Gene via CRISPR/Cas9 Generates ALV-J-Resistant Chicken Primordial Germ Cell.Animals : an open access journal from MDPI · 2025Article
- Identification of Resistance Loci to Avian Leukosis via Genome-Wide Association Analysis in Chengkou Mountain Chickens.Animals : an open access journal from MDPI · 2025Article
- N6-methyladenosine modification of the subgroup J avian leukosis viral RNAs attenuates host innate immunity via MDA5 signaling.PLoS pathogens · 2025Article
- Analysis of the Transcriptional Control ofAnimals : an open access journal from MDPI · 2025Article
- Autophagy-mediated TET2 degradation by ALV-J Env protein suppresses innate immune activation to promote viral replication.Journal of virology · 2025Article
- Rapid adaptive evolution of avian leukosis virus subgroup J in response to biotechnologically induced host resistance.PLoS pathogens · 2024Article
- N123I mutation in the ALV-J receptor-binding domain region enhances viral replication ability by increasing the binding affinity with chNHE1.PLoS pathogens · 2024Article
- Article
- 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
- Advances on genetic and genomic studies of ALV resistance.Journal of animal science and biotechnology · 2022Review
- Residues L55 and W69 of Tva Mediate Entry of Subgroup A Avian Leukosis Virus.Journal of virology · 2022Article
- Glycosylation of ALV-J Envelope Protein at Sites 17 and 193 Is Pivotal in the Virus Infection.Journal of virology · 2022Article
- Avian Leucosis Virus-Host Interaction: The Involvement of Host Factors in Viral Replication.Frontiers in immunology · 2022Review
- 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
5 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Subgroup J avian leukosis virus (ALV-J) is a recently identified avian oncogenic retrovirus responsible for severe economic losses worldwide. In contrast with the other ALV subgroups, ALV-J predominantly induces myeloid leukosis in meat-type chickens. Despite significant homology with the other ALV subgroups across most of the genome, the envelope protein of ALV-J (EnvJ) shares low homology with the others. Pathogenicity and myeloid leukosis induction map to the env gene of ALV-J. A chimeric protein composed of the surface domain of EnvJ fused to the constant region of a rabbit IgG and mass spectrometry were used to identify the chicken Na(+)/H(+) exchanger type 1 (chNHE1) as a binding protein for ALV-J. Flow cytometry analysis and coprecipitation experiments demonstrated a specific interaction between EnvJ and chNHE1. When introduced into nonpermissive human 293T cells and quail QT6 cells, chNHE1 conferred susceptibility to EnvJ-mediated infection. Furthermore, 293T cells expressing chNHE1 fused with 293T cells expressing EnvJ in a low-pH-dependent manner. Together, these data identify chNHE1 as a cellular receptor for the highly pathogenic ALV-J.
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Registered trials
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.