Structure and Receptor Specificity of the Hemagglutinin from an H5N1 Influenza Virus

Stevens, James; Blixt, Ola; Tumpey, Terrence M.; Taubenberger, Jeffery K.; Paulson, James C.; Wilson, Ian A.

doi:10.1126/science.1124513

Cited by 884 publications

(887 citation statements)

References 47 publications

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“…This finding demonstrated that the isolates with avian specific receptor binding properties can replicate and cause infection in equines. Different amino-acids that are implicated in receptor specificity Y98, S136, W153, H183, E190, K193 L194 E216 P221 K222 G225, Q226, S227, G228 (H3 influenza numbering) were tested [26]. Interestingly 98 (Y to N), 193 (K to R), 216 (E to K) and 221(P to S) which were found in the examined equine isolate have also been in many other isolates from the middle east in the flu database which raises a question as to what the impact of such substitution on HA binding to human receptors is.…”

Section: Resultsmentioning

confidence: 99%

Isolation and characterization of highly pathogenic avian influenza virus subtype H5N1 from donkeys

Abdel‐Moneim

Abdel-Ghany

Shany

2010

Journal of Biomedical Science

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BackgroundThe highly pathogenic H5N1 is a major avian pathogen that crosses species barriers and seriously affects humans as well as some mammals. It mutates in an intensified manner and is considered a potential candidate for the possible next pandemic with all the catastrophic consequences.MethodsNasal swabs were collected from donkeys suffered from respiratory distress. The virus was isolated from the pooled nasal swabs in specific pathogen free embryonated chicken eggs (SPF-ECE). Reverse transcriptase polymerase chain reaction (RT-PCR) and sequencing of both haemagglutingin and neuraminidase were performed. H5 seroconversion was screened using haemagglutination inhibition (HI) assay on 105 donkey serum samples.ResultsWe demonstrated that H5N1 jumped from poultry to another mammalian host; donkeys. Phylogenetic analysis showed that the virus clustered within the lineage of H5N1 from Egypt, closely related to 2009 isolates. It harboured few genetic changes compared to the closely related viruses from avian and humans. The neuraminidase lacks oseltamivir resistant mutations. Interestingly, HI screening for antibodies to H5 haemagglutinins in donkeys revealed high exposure rate.ConclusionsThese findings extend the host range of the H5N1 influenza virus, possess implications for influenza virus epidemiology and highlight the need for the systematic surveillance of H5N1 in animals in the vicinity of backyard poultry units especially in endemic areas.

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Section: Resultsmentioning

confidence: 99%

Isolation and characterization of highly pathogenic avian influenza virus subtype H5N1 from donkeys

Abdel‐Moneim

Abdel-Ghany

Shany

2010

Journal of Biomedical Science

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“…The soluble 09H1 (A/California/04/2009) was prepared based on the method described by Stevens et al in a baculovirus expression system (Stevens et al, , 2006Ekiert et al, 2009). The construct incorporated a C-terminal thrombin cleavage site, a trimerizing sequence ('foldon') and a hexa His-tag at the extreme C terminus of the construct to enable protein purification.…”

Section: Resultsmentioning

confidence: 99%

Crystal structure of the swine-origin A (H1N1)-2009 influenza A virus hemagglutinin (HA) reveals similar antigenicity to that of the 1918 pandemic virus

Zhang

Shi

et al. 2010

Protein Cell

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“…[11] Considering that glycans are ubiquitous biomolecules, which, in many cases, are key to protein function, [12][13][14] it is evident that glycans are useful means for addressing various questions in the fields of basic and applied research, relating to the areas of biomimetics, drug targeting, vaccine design, [15] or diagnostics. [16,17] Vital cellular functions that are regulated or influenced by glycans include, for instance, recognition, signaling, trafficking, biological half life, and adhesion events; several immunological phenomena are also enabled and enhanced through glycan "signals" on proteins. Thus, engineering of tailor-made ("functional") glycoproteins (neoglycoproteins) will decisively change our capability to influence and control complex biological systems.…”

Section: Introductionmentioning

confidence: 99%

Recombinant Glycans on an S‐Layer Self‐Assembly Protein: A New Dimension for Nanopatterned Biomaterials

Steiner

Hanreich

Kainz

et al. 2008

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Crucial biological phenomena are mediated through carbohydrates that are displayed in a defined manner and interact with molecular scale precision. We lay the groundwork for the integration of recombinant carbohydrates into a "biomolecular construction kit" for the design of new biomaterials, by utilizing the self-assembly system of the crystalline cell surface (S)-layer protein SgsE of Geobacillus stearothermophilus NRS 2004/3a. SgsE is a naturally O-glycosylated protein, with intrinsic properties that allow it to function as a nanopatterned matrix for the periodic display of glycans. By using a combined carbohydrate/protein engineering approach, two types of S-layer neoglycoproteins are produced in Escherichia coli. Based on the identification of a suitable periplasmic targeting system for the SgsE self-assembly protein as a cellular prerequisite for Europe PMC Funders Author ManuscriptsEurope PMC Funders Author Manuscripts protein glycosylation, and on engineering of one of the natural protein O-glycosylation sites into a target for N-glycosylation, the heptasaccharide from the AcrA protein of Campylobacter jejuni and the O7 polysaccharide of E. coli are co-or post-translationally transferred to the S-layer protein by the action of the oligosaccharyltransferase PglB. The degree of glycosylation of the Slayer neoglycoproteins after purification from the periplasmic fraction reaches completeness. Electron microscopy reveals that recombinant glycosylation is fully compatible with the S-layer protein self-assembly system. Tailor-made ("functional") nanopatterned, self-assembling neoglycoproteins may open up new strategies for influencing and controlling complex biological systems with potential applications in the areas of biomimetics, drug targeting, vaccine design, or diagnostics.

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Structure and Receptor Specificity of the Hemagglutinin from an H5N1 Influenza Virus

Cited by 884 publications

References 47 publications

Isolation and characterization of highly pathogenic avian influenza virus subtype H5N1 from donkeys

Isolation and characterization of highly pathogenic avian influenza virus subtype H5N1 from donkeys

Crystal structure of the swine-origin A (H1N1)-2009 influenza A virus hemagglutinin (HA) reveals similar antigenicity to that of the 1918 pandemic virus

Recombinant Glycans on an S‐Layer Self‐Assembly Protein: A New Dimension for Nanopatterned Biomaterials

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