Evolution of the receptor binding phenotype of influenza A (H5) viruses

Gambaryan, Alexandra; Tuzikov, Alexander; Pazynina, Galina V.; Bovin, Nicolai V.; Balish, Amanda; Klimov, Alexander

doi:10.1016/j.virol.2005.08.035

Cited by 183 publications

(164 citation statements)

References 20 publications

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“…A͞Hong Kong͞213͞03 (HK213) contains a mutation at residue 223 (H5 numbering; residue 227 by H3 numbering) within the receptor-binding domain of the HA and was shown to bind to both ␣2,6 and ␣2,3 SA in vitro (13). Therefore, three ferrets were inoculated i.n.…”

Section: Resultsmentioning

confidence: 99%

Lack of transmission of H5N1 avian–human reassortant influenza viruses in a ferret model

Maines

Chen

Matsuoka

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

319

360

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Avian influenza A H5N1 viruses continue to spread globally among birds, resulting in occasional transmission of virus from infected poultry to humans. Probable human-to-human transmission has been documented rarely, but H5N1 viruses have not yet acquired the ability to transmit efficiently among humans, an essential property of a pandemic virus. The pandemics of 1957 and 1968 were caused by avian-human reassortant influenza viruses that had acquired human virus-like receptor binding properties. However, the relative contribution of human internal protein genes or other molecular changes to the efficient transmission of influenza viruses among humans remains poorly understood. Here, we report on a comparative ferret model that parallels the efficient transmission of H3N2 human viruses and the poor transmission of H5N1 avian viruses in humans. In this model, an H3N2 reassortant virus with avian virus internal protein genes exhibited efficient replication but inefficient transmission, whereas H5N1 reassortant viruses with four or six human virus internal protein genes exhibited reduced replication and no transmission. These findings indicate that the human virus H3N2 surface protein genes alone did not confer efficient transmissibility and that acquisition of human virus internal protein genes alone was insufficient for this 1997 H5N1 virus to develop pandemic capabilities, even after serial passages in a mammalian host. These results highlight the complexity of the genetic basis of influenza virus transmissibility and suggest that H5N1 viruses may require further adaptation to acquire this essential pandemic trait. transmissibility ͉ pandemic virus properties ͉ pandemic influenza ͉ animal model ͉ receptor specificity

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Section: Resultsmentioning

confidence: 99%

Lack of transmission of H5N1 avian–human reassortant influenza viruses in a ferret model

Maines

Chen

Matsuoka

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

319

360

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“…The hydrophilic interaction between avian H3 and avian Neu5Ac2-3Gal largely stabilized the complex with the large desolvation energy penalty and the solute entropic penalty to give the G bind advantage of -6.8 kcal/mol than the G bind in avian H3-human Neu5Ac2-6Gal complex. These approaches with the amino acid sequence alignments of comprehensive HA [61,[63][64][65][66][67] provided the chemical insight into the roots of selective HA binding to the sialosides.…”

Section: The Fragment Molecular Orbital Study Of the Influenza Hemaggmentioning

confidence: 99%

Chemical Insight Into the Influenza A Virus Hemagglutinin Binding to the Sialoside Revealed by the Fragment Molecular Orbital Method

Sawada¹

2012

TOGLYJ

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Abstract:The present mini-review aims first at an introduction to two thermodynamic essentials of the binding between the influenza A virus hemagglutinin (HA) and the cell surface receptor sialoside, (1) the equilibrium 1:1 binding of the HA with the sialoside, (2) the polyvalent effect of the HA binding to the polyvalent sialoside. Second, the review introduces the fragment molecular orbital (FMO) studies of the HA-sialoside (1:1) complexes. The recent FMO method with the polarizable continuum model as one of the residue-based energy analysis method has revealed the role of key amino acid residue on the selective HA subtype H3 binding to the sialosides.

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“…Considering the corresponding amino acids at the same sites in human H1N1 HA, the two amino acids E216 and P221 in North American avian H5N1 appeared to favor human-type binding. In addition to the critical mutations discussed above, avian H5N1 HA mutations L133V, A137V [35], N186K, Q196R [36], E190D, G225D [37], G228S [38] were shown to enhance its human-type binding, and mutations Q226L and G228S to reduce its avian-type binding affinity [35], and mutation S227N to reduce its avian-type binding and increase its human-type binding affinity [39].…”

Section: Mutations In Ha Capable Of Changing Binding Preferencementioning

confidence: 99%

Characterization of asian and north American avian H5N1

2011

AJMB

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Since the emerge of the highly pathogenic avian H5N1 virus in Asia in 1996, the possibility for this virus to cross species barriers to infect humans and its ability to cause large outbreaks in birds have been a public health concern. This virus has been spreading from Asia to Europe and Africa by migratory birds with North America as its next possible stop. In this study, an ensemble of computational techniques including Random Forests, Informational Spectrum Method, Entropy, and Mutual Information were employed to unravel the distinct characteristics of Asian and North American avian H5N1 in comparison with human and swine H5N1. Critical differences were identified in the HA cleavage and binding sites, the HA receptor selection, the interaction patterns of HA and NA, and NP, PA, PB1, and PB2, and the important sites in the influenza proteins including HA, NA, M1, M2, NS1, NS2, NP, PA, PB1, PB1-F2, and PB2.

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Evolution of the receptor binding phenotype of influenza A (H5) viruses

Cited by 183 publications

References 20 publications

Lack of transmission of H5N1 avian–human reassortant influenza viruses in a ferret model

Lack of transmission of H5N1 avian–human reassortant influenza viruses in a ferret model

Chemical Insight Into the Influenza A Virus Hemagglutinin Binding to the Sialoside Revealed by the Fragment Molecular Orbital Method

Characterization of asian and north American avian H5N1

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