Receptor-binding properties of influenza viruses isolated from gulls

Gambaryan, Alexandra; Matrosovich, Tatyana; Boravleva, Elizaveta; Nf, Lomakina; Yamnikova, S. S.; Tuzikov, Alexander; Pazynina, Galina V.; Bovin, Nicolai V.; Fouchier, Ron A. M.; Klenk, Hans‐Dieter; Matrosovich, Mikhail

doi:10.1016/j.virol.2018.07.004

Cited by 34 publications

(45 citation statements)

References 44 publications

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“…The K218Q mutant showed reduced binding to nonfucosylated analogues 3=SLN, SLe c , and Su-3=SLN and increased binding to fucosylated receptors SLe x and 6-Su-SLe x . These observations confirm previous reports on the important role of the amino acid in position 218 for the recognition of fucose (24,33,(35)(36)(37)(38). The binding of the double mutant KN/KQ to all tested sialylglycopolymers (SGPs) was significantly lower than the binding of single mutants and below the detection limit of the assay.…”

Section: Resultssupporting

confidence: 90%

HA-Dependent Tropism of H5N1 and H7N9 Influenza Viruses to Human Endothelial Cells Is Determined by Reduced Stability of the HA, Which Allows the Virus To Cope with Inefficient Endosomal Acidification and Constitutively Expressed IFITM3

Hensen

Matrosovich

Roth³

et al. 2019

J Virol

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Previous studies revealed that certain avian influenza A viruses (IAVs), including zoonotic H5N1 and H7N9 IAVs, infect cultured human lung microvascular endothelial cells (HULEC) more efficiently than other IAVs and that tropism to HULEC is determined by viral hemagglutinin (HA). To characterize mechanisms of HA-mediated endotheliotropism, we used 2:6 recombinant IAVs harboring HAs from distinctive avian and human viruses and found that efficient infection of HULEC correlated with low conformational stability of the HA. We next studied effects on viral infectivity of single-point amino acid substitutions in the HA of 2:6 recombinant virus A/Vietnam/1203/2004-PR8 (H5N1). Substitutions H8Q, H103Y, T315I, and K582I (K58I in the HA2 subunit), which increased stability of the HA, markedly reduced viral infectivity for HULEC, whereas substitutions K189N and K218Q, which altered typical H5N1 virus-like receptor specificity and reduced binding avidity of the HA, led to only marginal reduction of infectivity. None of these substitutions affected virus infection in MDCK cells. We confirmed the previous observation of elevated basal expression of IFITM3 protein in HULEC and found that endosomal acidification is less efficient in HULEC than in MDCK cells. In accord with these findings, counteraction of IFITM3-mediated restriction by amphotericin B and reduction of endosomal pH by moderate acidification of the extracellular medium enhanced infectivity of viruses with stable HA for HULEC without significant effect on infectivity for MDCK cells. Collectively, our results indicate that relatively high pH optimum of fusion of the HA of zoonotic H5N1 and H7N9 IAVs allows them to overcome antiviral effects of inefficient endosomal acidification and IFITM3 in human endothelial cells. IMPORTANCE Receptor specificity of the HA of IAVs is known to be a critical determinant of viral cell tropism. Here, we show that fusion properties of the HA may also play a key role in the tropism. Thus, we demonstrate that IAVs having a relatively low pH optimum of fusion cannot efficiently infect human endothelial cells owing to their relatively high endosomal pH and increased expression of fusion-inhibiting IFITM3 protein. These restrictions can be overcome by IAVs with elevated pH of fusion, such as zoonotic H5N1 and H7N9. Our results illustrate that the infectivity of IAVs depends on an interplay between HA conformational stability, endosomal acidification and IFITM3 expression in target cells, and the extracellular pH. Given significant variation of levels of HA stability among animal, human, and zoonotic IAVs, our findings prompt further studies on the fusion-dependent tropism of IAVs to different cell types in humans and its role in viral host range and pathogenicity.

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Section: Resultssupporting

confidence: 90%

HA-Dependent Tropism of H5N1 and H7N9 Influenza Viruses to Human Endothelial Cells Is Determined by Reduced Stability of the HA, Which Allows the Virus To Cope with Inefficient Endosomal Acidification and Constitutively Expressed IFITM3

Hensen

Matrosovich

Roth³

et al. 2019

J Virol

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“…IAVs from avians, either wild birds or domestic birds, typically prefer the α2,3Sia terminal. Surprisingly, a recent study showed that some gull/tern H16 viruses prefer α2,6Neu5Ac over or equal to the α2,3Neu5Ac terminal of synthetic sialylglycopolymers [23]. It was suggested that the particularly distinctive receptor-binding specificity of H16 viruses may be related to their HAs containing A138S (found in human 1977-derived H1N1 viruses, reducing binding to α2,3Neu5Ac receptors) and E190T (the amino acid (aa) at position 190 determining binding specificity of H1N1 viruses to the sialyl linkage type) [23].…”

Section: Influenza a (H1-h16) Viruses Use Siaα23/26gal Receptorsmentioning

confidence: 97%

Host Receptors of Influenza Viruses and Coronaviruses—Molecular Mechanisms of Recognition

Sriwilaijaroen

Suzuki

2020

Vaccines

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Among the four genera of influenza viruses (IVs) and the four genera of coronaviruses (CoVs), zoonotic αIV and βCoV have occasionally caused airborne epidemic outbreaks in humans, who are immunologically naïve, and the outbreaks have resulted in high fatality rates as well as social and economic disruption and losses. The most devasting influenza A virus (IAV) in αIV, pandemic H1N1 in 1918, which caused at least 40 million deaths from about 500 million cases of infection, was the first recorded emergence of IAVs in humans. Usually, a novel human-adapted virus replaces the preexisting human-adapted virus. Interestingly, two IAV subtypes, A/H3N2/1968 and A/H1N1/2009 variants, and two lineages of influenza B viruses (IBV) in βIV, B/Yamagata and B/Victoria lineage-like viruses, remain seasonally detectable in humans. Both influenza C viruses (ICVs) in γIV and four human CoVs, HCoV-229E and HCoV-NL63 in αCoV and HCoV-OC43 and HCoV-HKU1 in βCoV, usually cause mild respiratory infections. Much attention has been given to CoVs since the global epidemic outbreaks of βSARS-CoV in 2002–2004 and βMERS-CoV from 2012 to present. βSARS-CoV-2, which is causing the ongoing COVID-19 pandemic that has resulted in 890,392 deaths from about 27 million cases of infection as of 8 September 2020, has provoked worldwide investigations of CoVs. With the aim of developing efficient strategies for controlling virus outbreaks and recurrences of seasonal virus variants, here we overview the structures, diversities, host ranges and host receptors of all IVs and CoVs and critically review current knowledge of receptor binding specificity of spike glycoproteins, which mediates infection, of IVs and of zoonotic, pandemic and seasonal CoVs.

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“…Despite their avian origin, human viruses exhibit a preference for glycan receptors with terminal NeuAcα2-6Gal linkages ( Figure 2 ), while avian viruses recognize receptors with the NeuAcα2-3Gal linkage, commonly referred to as ‘avian-type’ and ‘human-type’ receptor specificity [ 2 •• , 8 ]. These receptor differences result from only two amino acid mutations in the receptor binding pocket of the hemagglutinin, and are widely believed to mediate species specificity and tissue tropism [ 11 , 12 •• ]. Human viruses are believed to acquire human-type receptor specificity due to the abundant expression of α2-6-linked SAs on glycans of epithelial cells in the upper airway, a phenotype also exhibited in ferrets which are used as a model for respiratory droplet transmission of human influenza [ 13 , 14 , 15 • ].…”

Section: Membrane-enveloped Virusesmentioning

confidence: 99%

Virus recognition of glycan receptors

Thompson

Vries

Paulson

2019

Current Opinion in Virology

118

132

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Attachment of viruses to cell-surface receptors is the initial step in infection. Many mammalian viruses have evolved to recognize receptors that are glycans on cell-surface glycoproteins or glycolipids. Although glycans are a ubiquitous component of mammalian cells, the types of terminal structures expressed vary among different cell-types and tissues, and even between comparable cells and tissues from different species, frequently leading to specific tissue and species tropisms as a direct consequence of glycan receptor recognition. Covering the majority of known virus families, this review provides an overview of mammalian viruses that use glycans as receptors, and their roles in determining in host recognition and tropism.

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Receptor-binding properties of influenza viruses isolated from gulls

Cited by 34 publications

References 44 publications

HA-Dependent Tropism of H5N1 and H7N9 Influenza Viruses to Human Endothelial Cells Is Determined by Reduced Stability of the HA, Which Allows the Virus To Cope with Inefficient Endosomal Acidification and Constitutively Expressed IFITM3

HA-Dependent Tropism of H5N1 and H7N9 Influenza Viruses to Human Endothelial Cells Is Determined by Reduced Stability of the HA, Which Allows the Virus To Cope with Inefficient Endosomal Acidification and Constitutively Expressed IFITM3

Host Receptors of Influenza Viruses and Coronaviruses—Molecular Mechanisms of Recognition

Virus recognition of glycan receptors

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