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Surface Plasmon Resonance Immunosensor for Detection of PB1-F2 Influenza A Virus Protein in Infected Biological Samples | OMICS International | Abstract
ISSN: 2155-9872

Journal of Analytical & Bioanalytical Techniques
Open Access

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Research Article

Surface Plasmon Resonance Immunosensor for Detection of PB1-F2 Influenza A Virus Protein in Infected Biological Samples

Jasmina Vidic*, Christophe Chevalier, Ronan Le Goffic, Anna Miodek, Christiane Bourdieu, Charles-Adrien Richard, Mohammed Moudjou and Bernard Delmas

Virologie et Immunologie Moléculaires, Institut National de la Recherche Agronomique, France

*Corresponding Author:
Jasmina Vidic
Virologie et Immunologie Moléculaires
Institut National de la Recherche Agronomique
78350 Jouy en Josas, France
Tel: +0033134652623
Fax: +0033134652621
E-mail: [email protected]

Received date: February 22, 2013; Accepted date: April 02, 2013; Published date: April 04, 2013

Citation: Vidic J, Chevalier C, Le Goffic R, Bourdieu C, Richard CA, et al. (2013) Surface Plasmon Resonance Immunosensor for Detection of PB1-F2 Influenza A Virus Protein in Infected Biological Samples. J Anal Bioanal Tech S7:006. doi: 10.4172/2155-9872.S7-006

Copyright: © 2013 Vidic J, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.


The detection and evaluation of concentration of influenza virus proteins in biological samples is critical in a broad range of medical and biological investigations regarding the concern over potential outbreaks of virulent influenza strains in animals and humans. This paper describes a sensitive, label-free approach for the detection of a virulence factor PB1-F2. PB1-F2 is a small, 90 amino acid long polypeptide expressed in influenza A viruses, which generally exacerbate virus pathogenicity. The developed immunosensoris based on a non-the-chipcovalently immobilized specific monoclonal anti-PB1-F2 antibody and a SPR technology. The immunosensor was calibrated using purified full length PB1-F2 protein. Itdetected PB1-F2 with the linear range extended from 10 to 500 nM, repeatability of 5% for 500 nM PB1-F2 and showed saturationof protein concentrations higher than 1 μM. The sensor can quantify PB1-F2 in its monomeric form but not when its oligomerization was induced by preincubation in 0.05% SDS. The immunosensor was successfully applied in the detection and quantification of PB1-F2 in infected mouse lungs and cell lines, providing temporal expression profiles of PB1-F2 during viral infection. In lungs of infected mice, the influenza virus structural nucleoprotein NP was detected in parallel using a specific anti-NP antibody. This parallel detection of PB1-F2 and NP suggests that applied sensor chip technology may be amenable to an arrow immunosensor for simultaneous detection of all known influenza virus proteins in infected tissues and cells.


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