ArticleJournal of virology2020
Three Amino Acid Changes in Avian Coronavirus Spike Protein Allow Binding to Kidney Tissue.
Article in Journal of virology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 64 citations in OpenAlex.
- Global transmission pathways and adaptive molecular evolution of avian infectious bronchitis GI-23 (Variant 2).Scientific reports · 2026Article
- Recombination with a vaccine strain drives the evolution of a more virulent phenotype in avian infectious bronchitis virus.Poultry science · 2026Article
- Accumulation of mutations in nsp4, E, and the S2 subunit underlies mammalian cell tropism expansion and virulence attenuation of avian coronavirus.PLoS pathogens · 2026Article
- Pathogenicity and Bioinformatics Analysis of Two GI-13 Infectious Bronchitis Virus Strains in China.Transboundary and emerging diseases · 2026Article
- The receptor binding properties of H5Ny influenza A viruses have evolved to bind to avian-type mucin-like O-glycans.PLoS pathogens · 2026Article
- Molecular surveillance of GI-19 lineage infectious bronchitis virus in China: divergent evolution and efficacy assessment of QXL87 vaccine against heterologous clades.BMC veterinary research · 2025Article
- Attenuation and altered replication of IBV strain tl/CH/LDT3/03 after serial passage in chicken embryo fibroblasts and Vero cells.Virus research · 2025Article
- The role of the S1 gene in glandular stomach pathogenesis and tropism of infectious bronchitis virus H120 strain in poultry.Microbiology spectrum · 2025Article
- Article
- Genomic Alterations of the Infectious Bronchitis Virus (IBV) Strain of the GI-23 Lineage Induced by Passages in Chickens and Quails.International journal of molecular sciences · 2025Article
- The Q226L mutation can convert a highly pathogenic H5 2.3.4.4e virus to bind human-type receptors.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Five Amino Acid Substitutions in the S1 Unit of Infectious Bronchitis Virus Are Critical Determinants Enhancing Its Adaptation to Vero Cells.Veterinary sciences · 2025Article
- The Q226L mutation can convert a highly pathogenic H5 2.3.4.4e virus to bind human-type receptors.bioRxiv : the preprint server for biology · 2025Article
- Infectious bronchitis-virus-like QX strain transmission, pathogenesis, replication, and host miRNA biogenesis pathway hijacking mechanism.Frontiers in cellular and infection microbiology · 2025Article
- The mammary glands of cows abundantly display receptors for circulating avian H5 viruses.Journal of virology · 2024Article
- Article
- ComplexJournal of virology · 2024Article
- Molecular characterization of a novel variant of infectious bronchitis virus from field outbreaks in backyard chicken population of North East India.Virus genes · 2024Article
- Pathogenicity and molecular characterization of a GI-19 infectious bronchitis virus isolated from East China.Frontiers in veterinary science · 2024Article
- Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Infectious bronchitis virus (IBV) infects ciliated epithelial cells in the chicken respiratory tract. While some IBV strains replicate locally, others can disseminate to various organs, including the kidney. Here, we elucidate the determinants for kidney tropism by studying interactions between the receptor-binding domain (RBD) of the viral attachment protein spike from two IBV strains with different tropisms. Recombinantly produced RBDs from the nephropathogenic IBV strain QX and from the nonnephropathogenic strain M41 bound to the epithelial cells of the trachea. In contrast, only QX-RBD binds more extensively to cells of the digestive tract, urogenital tract, and kidneys. While removal of sialic acids from tissues prevented binding of all proteins to all tissues, binding of QX-RBD to trachea and kidney could not be blocked by preincubation with synthetic alpha-2,3-linked sialic acids. The lack of binding of QX-RBD to a previously identified IBV-M41 receptor was confirmed by enzyme-linked immunosorbent assay (ELISA), demonstrating that tissue binding of QX-RBD is dependent on a different sialylated glycan receptor. Using chimeric RBD proteins, we discovered that the region encompassing amino acids 99 to 159 of QX-RBD was required to establish kidney binding. In particular, QX-RBD amino acids 110 to 112 (KIP) were sufficient to render IBV-M41 with the ability to bind to kidney, while the reciprocal mutations in IBV-QX abolished kidney binding completely. Structural analysis of both RBDs suggests that the receptor-binding site for QX is located at a different location on the spike than that of M41.
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