Abstract
Aim: The present study evaluated the structural changes resulting from the interaction between a recombinant influenza A virus M2 protein and aluminum hydroxide adjuvant to investigate the antigen for further immunological studies. Materials & methods: Membrane protein II was produced from the H1N1 subtype of human influenza A virus. The interaction between M2 protein and alum inum hydroxide adjuvant was evaluated by physicochemical techniques including scanning electron microscope, UV-Vis spectra, Fourier-transform infrared spectroscopy and circular dichroism spectroscopy. Results: Physicochemical methods showed high-level protein adsorption and accessibility to the effective parts of the protein. Conclusion: It was concluded that M2 protein secondary structural perturbations, including the α-helix-to-β-sheet transition, enhanced its mechanical properties toward adsorption.
Supplementary data
To view the supplementary data that accompany this paper please visit the journal website at:www.tandfonline.com/doi/full/10.2217/fvl-2019-0019
Author contributions
M Saleh contributed to the concept and design, and developed the protocol, acquisition, analysis and interpretation of data, drafted the manuscript, wrote and prepared the manuscript and performed critical revision of the manuscript for important intellectual content. J Nowroozi contributed to the concept and design, provided supervision, administrative, technical and material support. F Fotouhi contributed to the concept and design, provided supervision, administrative, technical and material support. B Farahmand contributed to the concept and design, developed the original idea and the protocol and provided administrative, technical and material support and also performed supervision and interpretation of data.
Acknowledgments
This study was performed in the Department of Influenza and Respiratory viruses, Pasteur Institute of Iran, Tehran, Iran. We hereby appreciate all the staff valuable assistance and cooperation.
Financial & competing interests disclosure
This work was supported by the Pasteur Institute of Iran (grant number 944). The authors have no other relevant affiliations or financial involvement with any organization or entity with a financial interest in or financial conflict with the subject matter or materials discussed in the manuscript apart from those disclosed.
No writing assistance was utilized in the production of this manuscript.
Ethical conduct of research
Ethics approval and consent to participate were received. All animal experiments were approved and performed based on the guidelines of the Ethical Committee of the Pasteur Institute of Iran, Tehran, Iran (IR.PII.REC.1394.39 & IR.PII.REC.1395.82).