ArticleNature communications2026
MHC class II functions as a host-specific entry receptor for representative human and swine H3N2 influenza A viruses.
Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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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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
4 citing papers in PubMed.
- The receptor landscape of influenza A viruses.Journal of virology · 2026Review
- Influenza.Nature reviews. Disease primers · 2026Review
- H5N1 influenza binding and cell entry via human class II MHC, and blocking by cross-reactive antibodies.bioRxiv : the preprint server for biology · 2026Article
- Protocol to measure the kinetics of MHC class II-influenza A binding using biolayer interferometry.STAR protocols · 2025Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Influenza A viruses (FLUAV) utilize sialic acid to enter host cells via the envelope's hemagglutinin (HA), and its affinity for host-specific sialic acid linkage configuration is a major host range determinant. However, some FLUAV subtypes (H17, H18, H19) use the major histocompatibility complex class II (MHCII) as an entry receptor instead of sialic acid (SA), challenging our knowledge about FLUAV tropism and interspecies transmission potential. Here, we show that H3N2 viruses can use MHCII as an alternative entry receptor in a host-specific manner, and adaptation of human viruses to pigs increases affinity for the MHCII swine leukocyte antigen (SLA). By using two prototypic human-seasonal (hVIC/11) and swine-adapted (sOH/04) H3N2 viruses we found that expression of the human (HLA) but not the swine MHCII conferred replication of hVIC/11 in desialylated, non-susceptible cells. Further, expression of SLA in non-susceptible cells conferred susceptibility to infection by sOH/04. Introduction of point mutations near the hVIC/11 HA receptor-binding site (RBS) allowed the use of both human and swine MHCII. Our findings revealed that MHCII can serve as a sialic acid-independent entry receptor to H3N2 FLUAV in a host-specific manner, with potential implications for the viral pathogenesis and adaptation to a new species.
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