Production and diagnostic application of monoclonal antibodies against influenza virus H5

Yang, Ming; Clavijo, Alfonso; Graham, Jill; Salo, Tim; Hole, Kate; Berhane, Yohannes

doi:10.1016/j.jviromet.2009.08.006

Cited by 14 publications

(18 citation statements)

References 21 publications

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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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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 prototype DAS ELISA described in this study is able to differentiate H7 AI viruses from other AI virus subtypes and detect various H7 strains, while only an H7N1 virus was examined with the H7 capture ELISA described by Velumani et al (35). The assay can detect H7 virus with an HA titer of Ն4, which is similar to detection by an H5-specific DAS ELISA (39). Immunochromatographic strips for rapid detection of influenza viruses using two specific MAbs have been reported for H5, H7, and H9 virus subtypes (14,32,21).…”

Section: Discussionmentioning

confidence: 73%

“…The procedures for immunohistochemistry and immunofluorescence assays were performed as previously described (39). Briefly, Madin-Darby canine kidney (MDCK) cells were grown on microscope slides.…”

Section: Preparation Of Virusesmentioning

confidence: 99%

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Evaluation of Diagnostic Applications of Monoclonal Antibodies against Avian Influenza H7 Viruses

Yang

Clavijo

Graham

et al. 2010

Clin Vaccine Immunol

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“…In addition, the competitive enzyme-linked immunosorbent assay (cELISA) is beginning to gain acceptance. Recently, a cELISA for the hemagglutinin protein of H5N1 was developed using an insect cell-expressed recombinant antigen (12), obviating the need to handle live AI virus and removing the associated biocontainment constraints required for HI testing. Potentially, the cELISA could have a wide usage in assessing the host response to vaccination.…”

mentioning

confidence: 99%

A Single Electroporation Delivery of a DNA Vaccine Containing the Hemagglutinin Gene of Asian H5N1 Avian Influenza Virus Generated a Protective Antibody Response in Chickens against a North American Virus Strain

Ogunremi

Pasick

Kobinger

et al. 2013

Clin Vaccine Immunol

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Production and diagnostic application of monoclonal antibodies against influenza virus H5

Cited by 14 publications

References 21 publications

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

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

Evaluation of Diagnostic Applications of Monoclonal Antibodies against Avian Influenza H7 Viruses

A Single Electroporation Delivery of a DNA Vaccine Containing the Hemagglutinin Gene of Asian H5N1 Avian Influenza Virus Generated a Protective Antibody Response in Chickens against a North American Virus Strain

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