2019
DOI: 10.1038/s41586-019-0955-3
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MHC class II proteins mediate cross-species entry of bat influenza viruses

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Cited by 109 publications
(121 citation statements)
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“…Yet, from [42,43]. This is not unprecedented since bat viruses have been shown to 'jump' the species barrier frequently to infect new species [44][45][46][47][48][49][50]. However, since bats were in hibernation when the outbreak occurred, and it was uncertain whether bats were sold at the market, the virus is more likely to have been transmitted via members have been shown to transfer long chain fatty acids to cysteine residues of cellular and viral proteins.…”
Section: Origin and Evolution Of 2019-ncovmentioning
confidence: 99%
“…Yet, from [42,43]. This is not unprecedented since bat viruses have been shown to 'jump' the species barrier frequently to infect new species [44][45][46][47][48][49][50]. However, since bats were in hibernation when the outbreak occurred, and it was uncertain whether bats were sold at the market, the virus is more likely to have been transmitted via members have been shown to transfer long chain fatty acids to cysteine residues of cellular and viral proteins.…”
Section: Origin and Evolution Of 2019-ncovmentioning
confidence: 99%
“…While the receptor for HL18 has yet to be reported, the major histocompatibility complex class II human leukocyte antigen DR isotype (HLA-DR) has been identified as a receptor required for host cell attachment for HL17 (Karakus et al 2019). Interestingly, both HL17 and HL18 do not exhibit great structural divergence from typical HA molecules, indicating that few alterations to the HA scaffold have been required to utilize this proteinaceous receptor (Karakus et al 2019). Indeed, in contrast to the relatively large structural distances observed for NL10 and NL11 from classical influenza virus NAs (Fig.…”
Section: Novel Roles For Structurally Distinct Influenza Virus Glycopmentioning
confidence: 99%
“…The hemagglutinin (HA) of avian IAVs have a preference for sialic acids that display an 2, 3-linkage to the penultimate sugar, whereas human IAVs preferentially bind to the 2,6 linkage [4,5]. In two striking studies, Karakus et al and Giotis et al identified major histocompatibility complex class II (MHCII) as a receptor for bat H17N10 and H18N11 viruses [6,7]. Karakus et al used transcriptomic profiling and genome-wide CRISPR-Cas9 screening of susceptible and non-susceptible cells to identify and characterize MHCII as an entry determinant for bat H17N10 and H18N11 viruses [6].…”
mentioning
confidence: 99%
“…In two striking studies, Karakus et al and Giotis et al identified major histocompatibility complex class II (MHCII) as a receptor for bat H17N10 and H18N11 viruses [6,7]. Karakus et al used transcriptomic profiling and genome-wide CRISPR-Cas9 screening of susceptible and non-susceptible cells to identify and characterize MHCII as an entry determinant for bat H17N10 and H18N11 viruses [6]. The authors also observed that bat H17N10 and H18N11 viruses could initiate virus entry via MHCII homologs encoded by multiple bat species, pigs, humans and chickens [6].…”
mentioning
confidence: 99%