Detection of circulating Asian H5N1 viruses by a newly established monoclonal antibody

Du, Anariwa; Daidoji, Tomo; Koma, Takaaki; Ibrahim, Madiha S.; Nakamura, Shota; Silva, U. Chandimal de; Ueda, Mayo; Yang, Cheng-Song; Yasunaga, Teruo; Ikuta, Kazuyoshi; Nakaya, Takaaki

doi:10.1016/j.bbrc.2008.11.022

Cited by 23 publications

(17 citation statements)

References 18 publications

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“…The infected samples were subjected to Western blotting and probed with an anti-AIV (Dk/HK) polyclonal antibody (18), or an antiglucose-regulated protein 78 (GRP78) (Santa Cruz Biotechnology, Santa Cruz, CA), anticalnexin (Affinity BioReagents, Golden CO), anti-phosphorylated protein kinase R-like endoplasmic reticulum (ER) protein (P-PERK) (Cell Signaling), anti-Bcl-2 (BD Biosciences, San Jose, CA), or anti-Bax (Santa Cruz Biotechnology) MAb, followed by a horseradish peroxidase-conjugated secondary antibody (65). Blots were visualized as described above.…”

Section: Detection Of Camentioning

confidence: 99%

Highly Pathogenic H5N1 Avian Influenza Virus Induces Extracellular Ca ²⁺ Influx, Leading to Apoptosis in Avian Cells

Ueda

Daidoji²,

et al. 2010

J Virol

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In this study, we show that the highly pathogenic H5N1 avian influenza virus (AIV) . Thus, we investigated the molecular mechanisms of apoptosis induced by H5N1-AIV infection. Caspase-dependent and -independent pathways contributed to the cytopathic effects. We further showed that, in the induction of apoptosis, the hemagglutinin of H5N1-AIV played a major role and its cleavage sequence was not critical. We also observed outer membrane permeabilization and loss of the transmembrane potential of the mitochondria of infected DEF, indicating that mitochondrial dysfunction was caused by the H5N1-AIV infection. (

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Section: Detection Of Camentioning

confidence: 99%

Highly Pathogenic H5N1 Avian Influenza Virus Induces Extracellular Ca ²⁺ Influx, Leading to Apoptosis in Avian Cells

Ueda

Daidoji²,

et al. 2010

J Virol

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“…In [12], a similar domain was found in the N-terminus of the HA protein comprising residues 42 -75, which encompassed the domain 46:65 found in this study. The epitope mapping analysis in [19,20,21] reported that several anti-HA monoclonal antibodies (MAbs) could recognize the amino acids of HA at positions 1 -86, 20 -312, 136 -141, 151 -162, and 273 -342, illustrating that our domains might be recognized by these MAbs.…”

Section: Conserved Domains In Ha1 Of Avian H5n1mentioning

confidence: 99%

Identification of highly conserved domains in hemagglutinin associated with the receptor binding specificity of influenza viruses: 2009 H1N1, avian H5N1, and swine H1N2

Hu¹

2010

JBiSE

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The hemagglutinin (HA) of influenza viruses facilitates receptor binding and membrane fusion, which is the initial step of virus infection. Human influenza viruses preferentially bind to receptors with α2-6 linkages to galactose (SAα2,6Gal), whereas avian influenza viruses prefer receptors with α2-3 linkages to galactose (SAα2,3Gal). The current 2009 H1N1 pandemic is caused by a novel influenza A virus that has its genetic materials from birds, humans, and pigs. Its pandemic nature is characterized clearly by its dual binding to the α2-3 as well as α2-6 receptors, because the seasonal human H1N1 virus only binds to the α2-6 receptor. In a previous study, the informational spectrum method (ISM), a bioinformatics technique, was applied to uncover one highly conserved region in the HA protein associated with receptor binding preference in each of various influenza subtypes. In the present study, we extended the previous work by discovering multiple such domains in HA of 2009 H1N1 and avian H5N1 to expand our repertoire of known key regions in HA responsible for receptor binding affinity. Three such domains in HA of 2009 H1N1 were found at residue positions 106 to 130, 150 to 174, and 191 to 221, and another three domains in HA of avian H5N1 were located at residue positions 46 to 65, 136 to 153, and 269 to 286. These identified domains could be utilized as therapeutic and diagnostic targets for the prevention and treatment of influenza infection.

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“…However, the OM-b and AY-2C2 coverage of human and avian H5N1 strains isolated from Africa in 2010–2013 was only 20.2% (data not shown). This is probably because the mAbs did not recognize several of the evolved clade 2.2.1 viruses [30], [40]. Of note, we previously showed that OM-b and AY-2C2 mAbs were able to bind with A/turkey/Turkey/1/2005, which classified as an early clade 2.2.1 virus [14].…”

Section: Discussionmentioning

confidence: 99%

Broad Cross-Reactive Epitopes of the H5N1 Influenza Virus Identified by Murine Antibodies against the A/Vietnam/1194/2004 Hemagglutinin

et al. 2014

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There is an urgent need for a rapid diagnostic system to detect the H5 subtype of the influenza A virus. We previously developed monoclonal antibodies (mAbs) against the H5 hemagglutinin (HA) for use in a rapid diagnostic kit. In this study, we determined the epitopes of the anti-H5 HA murine mAbs OM-b, AY-2C2, and YH-1A1. Binding assays of the mAbs to different strains of H5 HAs indicated that OM-b and AY-2C2 cross-reacted with HAs from clades 1, 2.1.3.2, 2.2, and 2.3.4, whereas YH-1A1 failed to bind to those of clades 2.1.3.2 and 2.3.4. HA chimeras revealed that the epitopes for each of the mAbs were in the HA1 region. Analysis of escape mutants revealed that OM-b and AY-2C2 mAbs interacted mainly with amino acid residues D43 and G46, and the YH-1A1 mAb interacted with G139 and K or R140 of H5 HA. Multiple alignments of H5 HA protein sequences showed that D43 and G46 were very conserved among H5N1 HAs, except those in clade 2.2.1 and clade 7 (88.7%). The epitope for YH-1A1 mAb was highly variable in the HAs of H5N1, although it was well conserved in those of H5N2-N9. The OM-b and AY-2C2 mAbs could bind to the HAs of clades 1.1 and 2.3.2.1 that are currently epidemic in Asia, and we conclude that these would be effective for the detection of H5N1 infections in this region.

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Detection of circulating Asian H5N1 viruses by a newly established monoclonal antibody

Cited by 23 publications

References 18 publications

Highly Pathogenic H5N1 Avian Influenza Virus Induces Extracellular Ca ²⁺ Influx, Leading to Apoptosis in Avian Cells

Highly Pathogenic H5N1 Avian Influenza Virus Induces Extracellular Ca ²⁺ Influx, Leading to Apoptosis in Avian Cells

Identification of highly conserved domains in hemagglutinin associated with the receptor binding specificity of influenza viruses: 2009 H1N1, avian H5N1, and swine H1N2

Broad Cross-Reactive Epitopes of the H5N1 Influenza Virus Identified by Murine Antibodies against the A/Vietnam/1194/2004 Hemagglutinin

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Detection of circulating Asian H5N1 viruses by a newly established monoclonal antibody

Cited by 23 publications

References 18 publications

Highly Pathogenic H5N1 Avian Influenza Virus Induces Extracellular Ca 2+ Influx, Leading to Apoptosis in Avian Cells

Highly Pathogenic H5N1 Avian Influenza Virus Induces Extracellular Ca 2+ Influx, Leading to Apoptosis in Avian Cells

Identification of highly conserved domains in hemagglutinin associated with the receptor binding specificity of influenza viruses: 2009 H1N1, avian H5N1, and swine H1N2

Broad Cross-Reactive Epitopes of the H5N1 Influenza Virus Identified by Murine Antibodies against the A/Vietnam/1194/2004 Hemagglutinin

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Highly Pathogenic H5N1 Avian Influenza Virus Induces Extracellular Ca ²⁺ Influx, Leading to Apoptosis in Avian Cells

Highly Pathogenic H5N1 Avian Influenza Virus Induces Extracellular Ca ²⁺ Influx, Leading to Apoptosis in Avian Cells