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MHC class II proteins mediate cross-species entry of bat influenza viruses

ABSTRACT: MHC class II proteins mediate cross-species entry of bat influenza viruses

PROVIDER: PRJNA803440 | ENA |

REPOSITORIES: ENA

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	SRR17883884.fastq.gz	Fastqsanger.gz
	SRR17883885.fastq.gz	Fastqsanger.gz

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MHC class II proteins mediate cross-species entry of bat influenza viruses

Project description:Zoonotic influenza A viruses of avian origin can cause severe disease in individuals, or even global pandemics, and thus pose a threat to human populations. Waterfowl and shorebirds are believed to be the reservoir for all influenza A viruses, but this has recently been challenged by the identification of novel influenza A viruses in bats. The major bat influenza A virus envelope glycoprotein, haemagglutinin, does not bind the canonical influenza A virus receptor, sialic acid or any other glycan, despite its high sequence and structural homology with conventional haemagglutinins. This functionally uncharacterized plasticity of the bat influenza A virus haemagglutinin means the tropism and zoonotic potential of these viruses has not been fully determined. Here we show, using transcriptomic profiling of susceptible versus non-susceptible cells in combination with genome-wide CRISPR-Cas9 screening, that the major histocompatibility complex class II (MHC-II) human leukocyte antigen DR isotype (HLA-DR) is an essential entry determinant for bat influenza A viruses. Genetic ablation of the HLA-DR α-chain rendered cells resistant to infection by bat influenza A virus, whereas ectopic expression of the HLA-DR complex in non-susceptible cells conferred susceptibility. Expression of MHC-II from different bat species, pigs, mice or chickens also conferred susceptibility to infection. Notably, the infection of mice with bat influenza A virus resulted in robust virus replication in the upper respiratory tract, whereas mice deficient for MHC-II were resistant. Collectively, our data identify MHC-II as a crucial entry mediator for bat influenza A viruses in multiple species, which permits a broad vertebrate tropism.

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MHC class II proteins mediate sialic acid independent entry of human and avian H2N2 influenza A viruses

Project description:Influenza A viruses (IAV) cause seasonal outbreaks that pose a substantial burden on human health. They are also a zoonotic threat as avian and swine IAV can be a source for pandemic influenza. Receptor specificity is a critical determinant of tropism, host range and transmissibility of IAV and thus, plays a crucial role in zoonotic IAV infections1-3. Avian, swine and human IAV bind sialic acid on host cell glycans as their common receptor but differ in sialic acid specificity4,5. In contrast, bat IAV of the H17 and H18 subtypes cannot use sialic acid and require MHC class II complexes for host cell entry6-8. It is unknown how this difference in receptor specificity evolved and if dual receptor specificity for sialic acid and MHC class II is possible. Here, we show that human H2N2 IAV and related avian H2N2 possess dual receptor specificity. In addition to their known sialic acid-dependent entry they can use MHC class II as alternative entry pathway, independent of sialic acid. Of note, MHC class II from humans, pigs, ducks, swans and chickens but not from bats can mediate H2 IAV entry and the ability to use this alternative entry pathway is conserved in current Eurasian avian H2 IAV. Our results demonstrate that IAV can possess dual receptor specificity for sialic acid and MHC class II and suggest a role for MHC class II-dependent entry in zoonotic IAV infections.

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Project description:MHC class II proteins mediate sialic acid independent entry of human and avian H2N2 influenza A viruses

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Evolutionarily conserved amino acids in MHC-II mediate bat influenza A virus entry into human cells.

Project description:The viral hemagglutinins of conventional influenza A viruses (IAVs) bind to sialylated glycans on host cell surfaces for attachment and subsequent infection. In contrast, hemagglutinins of bat-derived IAVs target major histocompatibility complex class II (MHC-II) for cell entry. MHC-II proteins from various vertebrate species can facilitate infection with the bat IAV H18N11. Yet, it has been difficult to biochemically determine the H18:MHC-II binding. Here, we followed a different approach and generated MHC-II chimeras from the human leukocyte antigen DR (HLA-DR), which supports H18-mediated entry, and the nonclassical MHC-II molecule HLA-DM, which does not. In this context, viral entry was supported only by a chimera containing the HLA-DR α1, α2, and β1 domains. Subsequent modeling of the H18:HLA-DR interaction identified the α2 domain as central for this interaction. Further mutational analyses revealed highly conserved amino acids within loop 4 (N149) and β-sheet 6 (V190) of the α2 domain as critical for virus entry. This suggests that conserved residues in the α1, α2, and β1 domains of MHC-II mediate H18-binding and virus propagation. The conservation of MHC-II amino acids, which are critical for H18N11 binding, may explain the broad species specificity of this virus.

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