Alterations in Receptor Binding Properties of Recent Human Influenza H3N2 Viruses Are Associated with Reduced Natural Killer Cell Lysis of Infected Cells

Owen, Rachel E.; Yamada, Eriko; Thompson, Catherine; Phillipson, Louisa; Thompson, Clare; Taylor, E. G.; Zambon, Maria; Osborn, Helen M. I.; Barclay, William; Borrow, Persephone

doi:10.1128/jvi.01217-07

Cited by 52 publications

(44 citation statements)

References 37 publications

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“…We further showed that IV infection in mice is lethal in the absence of murine Ncr1 (11). Recently, Owen et al reported that alterations in HA binding properties of recent human influenza H3N2 viruses are associated with reduced NK cell lysis of infected cells (20). The pathogenicity of IV H5N1 strains in humans has been attributed mostly or partially to antigenic changes in the IV HA that render virus-specific immunity incapable of timely response to the developing infection (9,21).…”

mentioning

confidence: 59%

H5-Type Influenza Virus Hemagglutinin Is Functionally Recognized by the Natural Killer-Activating Receptor NKp44

Hershkovitz

Peiris

et al. 2008

J Virol

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mentioning

confidence: 59%

H5-Type Influenza Virus Hemagglutinin Is Functionally Recognized by the Natural Killer-Activating Receptor NKp44

Hershkovitz

Peiris

et al. 2008

J Virol

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“…Reduction in affinity of human H3N2 viruses for avian receptors since the beginning of the pandemic in 1968 has meant that by the 1990s viruses with reduced ability to agglutinate chicken erythrocytes had emerged (8,9). Moreover, viruses isolated after 1999 were shown to have reduced affinity for both human and avian receptors, a feature that correlated with their poor growth properties in eggs and different cells in culture (9)(10)(11)(12)(13)(14). The evolution of the HA has resulted in at least three key changes that influence receptor binding.…”

mentioning

confidence: 99%

Evolution of the receptor binding properties of the influenza A(H3N2) hemagglutinin

Lin¹,

Xiong²,

Wharton³

et al. 2012

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

265

328

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The hemagglutinin (HA) of influenza A(H3N2) virus responsible for the 1968 influenza pandemic derived from an avian virus. On introduction into humans, its receptor binding properties had changed from a preference for avian receptors (α2,3-linked sialic acid) to a preference for human receptors (α2,6-linked sialic acid). By 2001, the avidity of human H3 viruses for avian receptors had declined, and since then the affinity for human receptors has also decreased significantly. These changes in receptor binding, which correlate with increased difficulties in virus propagation in vitro and in antigenic analysis, have been assessed by virus hemagglutination of erythrocytes from different species and quantified by measuring virus binding to receptor analogs using surface biolayer interferometry. Crystal structures of HA–receptor analog complexes formed with HAs from viruses isolated in 2004 and 2005 reveal significant differences in the conformation of the 220-loop of HA1, relative to the 1968 structure, resulting in altered interactions between the HA and the receptor analog that explain the changes in receptor affinity. Site-specific mutagenesis shows the HA1 Asp-225→Asn substitution to be the key determinant of the decreased receptor binding in viruses circulating since 2005. Our results indicate that the evolution of human influenza A(H3N2) viruses since 1968 has produced a virus with a low propensity to bind human receptor analogs, and this loss of avidity correlates with the marked reduction in A(H3N2) virus disease impact in the last 10 y.

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“…Polymer binding studies using assays similar to that presented here have been utilized extensively to investigate influenza virus binding preference (10,18,24,25,27,35,47). However, data presented herein suggest that binding preference in such assays does not correlate uniformly with the receptor determinants utilized for infection.…”

mentioning

confidence: 94%

“…Linear regression analysis of Scatchard plots was performed using Prism software (GraphPad, La Jolla, CA). The Neu5Ac␣2,3Gal␤1-4Glc␤ (2,3SL) polymer is widely utilized as the avian-like receptor analog, while the Neu5Ac␣2,6Gal␤1-4GlcNAc␤ (2,6SLN) polymer is utilized as the human-like analog (11,(24)(25)(26)35). To ensure that the different polymer backbones (lactose versus lactosamine) did not have major effects on binding affinity, we included 2,3SLN and found that viruses bound to 2,3SL and 2,3SLN with similar levels of affinity (Table 1).…”

mentioning

confidence: 99%

Amino Acid 226 in the Hemagglutinin of H4N6 Influenza Virus Determines Binding Affinity for α2,6-Linked Sialic Acid and Infectivity Levels in Primary Swine and Human Respiratory Epithelial Cells

Bateman

Busch

Karasin

et al. 2008

J Virol

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Avian lineage H4N6 influenza viruses previously isolated from pigs differ at hemagglutinin amino acids 226 and 228 from H4 subtype viruses isolated from birds. Using a parental H4N6 swine isolate and hemagglutinin mutant viruses (at residues 226 and/or 228), we determined that viruses which contain L226 had a higher affinity for sialic acid ␣2,6 galactose (SA␣2,6Gal) and a higher infectivity level for primary swine and human respiratory epithelial cells, whereas viruses which contain Q226 had lower SA␣2,6Gal affinity and lower infectivity levels for both types of cells. Using specific neuraminidases, we found that irrespective of their relative binding preferences, all of the influenza viruses examined utilized SA␣2,6Gal to infect swine and human cells.

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Alterations in Receptor Binding Properties of Recent Human Influenza H3N2 Viruses Are Associated with Reduced Natural Killer Cell Lysis of Infected Cells

Abstract: Natural killer (NK) cell recognition of influenza virus-infected cells involves hemagglutinin (

Cited by 52 publications

References 37 publications

H5-Type Influenza Virus Hemagglutinin Is Functionally Recognized by the Natural Killer-Activating Receptor NKp44

H5-Type Influenza Virus Hemagglutinin Is Functionally Recognized by the Natural Killer-Activating Receptor NKp44

Evolution of the receptor binding properties of the influenza A(H3N2) hemagglutinin

Amino Acid 226 in the Hemagglutinin of H4N6 Influenza Virus Determines Binding Affinity for α2,6-Linked Sialic Acid and Infectivity Levels in Primary Swine and Human Respiratory Epithelial Cells

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