Mutation W222L at the Receptor Binding Site of Hemagglutinin Could Facilitate Viral Adaption from Equine Influenza A(H3N8) Virus to Dogs

Wen, Feng; Blackmon, Sherry; Olivier, Alicia K.; Li, Lei; Guan, Minhui; Sun, Hailiang; Wang, Peng George; Wan, Xiu‐Feng

doi:10.1128/jvi.01115-18

Cited by 34 publications

(47 citation statements)

References 43 publications

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“…Variations in the amino acid sequences are tabulated in Additional file 3. Regarding the HA gene of CIV and EIV (the positioning or numbering of amino acid residues in the HA gene is based on the starting codon for H3 HA), as previously described by Wen et al [54], there was a W222L substitution at the receptor-binding site in all CIV HA genes. However, for the antigenic sites A to D [25], there was a N54K substitution at antigenic site C in the CIV HA gene.…”

Section: Resultsmentioning

confidence: 99%

“…An alternative hypothesis is that there was a “frozen” virus strain in circulation. However, taking together, this “successful” interspecies transmission was a “rarity”, as a unique combination of gene segments was required, plus a unique amino acid substitution at the receptor-binding site in the HA gene (W222L) [54]. Therefore, this interspecies transmission was not a “wholesale” event, but rather occurred during at least two events, one involving reassortment of a unique combination of gene segments and a mutation or adaptation at the receptor-binding site in the HA.…”

Section: Discussionmentioning

confidence: 99%

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Host-range shift of H3N8 canine influenza virus: a phylodynamic analysis of its origin and adaptation from equine to canine host

Wang

et al. 2019

Vet Res

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Prior to the emergence of H3N8 canine influenza virus (CIV) and the latest avian-origin H3N2 CIV, there was no evidence of a circulating canine-specific influenza virus. Molecular and epidemiological evidence suggest that H3N8 CIV emerged from H3N8 equine influenza virus (EIV). This host-range shift of EIV from equine to canine hosts and its subsequent establishment as an enzootic CIV is unique because this host-range shift was from one mammalian host to another. To further understand this host-range shift, we conducted a comprehensive phylodynamic analysis using all the available whole-genome sequences of H3N8 CIV. We found that (1) the emergence of H3N8 CIV from H3N8 EIV occurred in approximately 2002; (2) this interspecies transmission was by a reassortant virus of the circulating Florida-1 clade H3N8 EIV; (3) once in the canine species, H3N8 CIV spread efficiently and remained an enzootic virus; (4) H3N8 CIV evolved and diverged into multiple clades or sublineages, with intra and inter-lineage reassortment. Our results provide a framework to understand the molecular basis of host-range shifts of influenza viruses and that dogs are potential “mixing vessels” for the establishment of novel influenza viruses.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Host-range shift of H3N8 canine influenza virus: a phylodynamic analysis of its origin and adaptation from equine to canine host

Wang

et al. 2019

Vet Res

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“…Little is known about the glycans present on erythrocytes of different species, apart from two studies that describe that very few glycans with fucoses are present on chicken and mouse erythrocytes [33,34]. Influenza A viruses of different subtypes (H1, H3, H4, H5, H6, H7, H9, H13, H14) are known that (specifically) bind, or do not bind at all, to fucosylated and sulfated glycans [35][36][37][38][39][40][41][42]. Most relevant, avian, human, and seal H7…”

Section: Discussionmentioning

confidence: 99%

N-glycolylneuraminic acid binding of avian H7 influenza A viruses

Spruit

Zhu

Broszeit

et al. 2020

Preprint

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Influenza A viruses initiate infection by binding to glycans with terminal sialic acids present on the cell surface. Hosts of influenza A viruses variably express two major forms of sialic acid, N-acetylneuraminic acid (NeuAc) and N-glycolylneuraminic acid (NeuGc). NeuGc is produced in the majority of mammals including horses, pigs, and mice, but is absent in humans, ferrets, and birds. Intriguingly, the only known naturally occurring influenza A viruses that exclusively bind NeuGc are the extinct highly pathogenic equine H7N7 viruses. We determined the crystal structure of a representative equine H7 hemagglutinin (HA) in complex with its NeuGc ligand and observed a high similarity in the receptor-binding domain with an avian H7 HA. To determine the molecular basis for NeuAc and NeuGc specificity, we performed systematic mutational analyses, based on the structural insights, on two distant avian H7 HAs. We found that mutation A135E is key for binding α2,3-linked NeuGc but does not abolish NeuAc binding. Interestingly, additional mutations S128T, I130V, or a combination of T189A and K193R, converted from NeuAc to NeuGc specificity as determined by glycan microarrays. However, specific binding to NeuGc-terminal glycans on our glycan array did not always correspond with full NeuGc specificity on chicken and equine erythrocytes and tracheal epithelium sections. Phylogenetic analysis of avian and equine H7 HAs that investigated the amino acids at positions 128, 130, 135, 189, and 193 reveals a clear distinction between equine and avian residues. The highest variability in amino acids (four different residues) is observed at key position 135, of which only the equine glutamic acid leads to binding of NeuGc. The results demonstrate that avian H7 viruses, although genetically distinct from equine H7 viruses, can bind NeuGc after the introduction of two to three mutations, providing insights into the adaptation of H7 viruses to NeuGc receptors.Author summaryInfluenza A viruses cause millions of cases of severe illness and deaths annually. To initiate infection and replicate, the virus first needs to bind to a structure on the cell surface, like a key fitting in a lock. For influenza A virus, these ‘keys’ (receptors) on the cell surface are chains of sugar molecules (glycans). The terminal sugar on these glycans is often either N-acetylneuraminic acid (NeuAc) or N-glycolylneuraminic acid (NeuGc). Most influenza A viruses bind NeuAc, but a small minority binds NeuGc. NeuGc is present in species like horses, pigs, and mice, but not in humans, ferrets, and birds. Therefore, NeuGc binding could be a determinant of an Influenza A virus species barrier. Here, we investigated the molecular determinants of NeuGc specificity and the origin of viruses that bind NeuGc.

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“…A comparison of equine and canine H3N8 sequences highlighted key amino acid residues that may be involved in receptor binding specificity and host cell tropism (38,75,76). Interestingly, as for H3N2, structural, and receptor binding analyses support the role of the HA Trp222Leu mutation in facilitating viral interspecies transmission from equine to canine (77)(78)(79). However, CIV-H3N8 has not been found to be phenotypically different from equine H3N8 strains in terms of replicability and infectivity, thus suggesting that crossspecies transmission and adaptation of influenza viruses may be rather mediated by subtle changes in virus biology (76,80).…”

Section: Equine Interspecies Transmissionmentioning

confidence: 94%

Influenza A Virus Infection in Cats and Dogs: A Literature Review in the Light of the “One Health” Concept

Borland

Gracieux

Jones

et al. 2020

Front. Public Health

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Influenza A viruses are amongst the most challenging viruses that threaten both human and animal health. Constantly evolving and crossing species barrier, the emergence of novel zoonotic pathogens is one of the greatest challenges to global health security. During the last decade, considerable attention has been paid to influenza virus infections in dogs, as two canine H3N8 and H3N2 subtypes caused several outbreaks through the United States and Southern Asia, becoming endemic. Cats, even though less documented in the literature, still appear to be susceptible to many avian influenza infections. While influenza epidemics pose a threat to canine and feline health, the risks to humans are largely unknown. Here, we review most recent knowledge of the epidemiology of influenza A viruses in dogs and cats, existing evidences for the abilities of these species to host, sustain intraspecific transmission, and generate novel flu A lineages through genomic reassortment. Such enhanced understanding suggests a need to reinforce surveillance of the role played by companion animals-human interface, in light of the "One Health" concept and the potential emergence of novel zoonotic viruses.

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Mutation W222L at the Receptor Binding Site of Hemagglutinin Could Facilitate Viral Adaption from Equine Influenza A(H3N8) Virus to Dogs

Cited by 34 publications

References 43 publications

Host-range shift of H3N8 canine influenza virus: a phylodynamic analysis of its origin and adaptation from equine to canine host

Host-range shift of H3N8 canine influenza virus: a phylodynamic analysis of its origin and adaptation from equine to canine host

N-glycolylneuraminic acid binding of avian H7 influenza A viruses

Influenza A Virus Infection in Cats and Dogs: A Literature Review in the Light of the “One Health” Concept

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