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Paul Azzinaro
Foreign Animal Disease Research
Visiting Scientist

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Publications (Clicking on the reprint icon Reprint Icon will take you to the publication reprint.)
Prophylactic treatment with PEGylated bovine FN-lambda3 effectively bridges the gap in vaccine-induced immunity against FMD in cattle Reprint Icon - (Peer Reviewed Journal)
Attreed, S.E., Silva, C.M., Rodriguez-Calzada, M., Mogulothu, A., Abbott, S.T., Azzinaro, P.A., Canning, P., Skidmore, L., Nelson, J., Knudsen, N., Medina, G.N., De Los Santos, T., Diaz-San Segundo, F. 2024. Prophylactic treatment with PEGylated bovine FN-lambda3 effectively bridges the gap in vaccine-induced immunity against FMD in cattle. Frontiers in Microbiology. 15. https://doi.org/10.3389/fmicb.2024.1360397.
Understanding the molecular mechanisms of attenuation in codon deoptimized FMDV strains Reprint Icon - (Abstract Only)
Medina, G.N., Spinard Iii, E.J., Azzinaro, P.A., Rodriguez-Calzada, M., Rieder, A.E., Diaz San Segundo, F.C., De Los Santos, T.B. 2023. Understanding the molecular mechanisms of attenuation in codon deoptimized FMDV strains. Meeting Abstract. https://doi.org/10.3390/v15061332.
Deoptimization of FMDV P1 region results in robust serotype-independent viral attenuation Reprint Icon - (Peer Reviewed Journal)
Medina, G.N., Diaz-San Segundo, F., Spinard III, E.J., Azzinaro, P.A., Rodriguez-Calzada, M., Gutkoska, J.R., Kloc, A., Rieder, A.E., Mueller, S., De Los Santos, T.B. 2023. Deoptimization of FMDV P1 region results in robust serotype-independent viral attenuation. Viruses. 15(6). https://doi.org/10.3390/v15061332.
Evaluation of potential recombination events in codon deoptimized FMDV strains Reprint Icon - (Abstract Only)
Spinard, E., Fish, I., Azzinaro, P.A., Hartwig, E.J., Smoliga, G.R., Mogulothu, A., Rodriguez-Calzada, M., Arzt, J., De Los Santos, T.B., Medina, G.N. 2023. Evaluation of potential recombination events in codon deoptimized FMDV strains. Meeting Abstract. https://doi.org/10.3390/v15030670.
Evaluation of potential in vitro recombination events in codon deoptimized FMDV strains Reprint Icon - (Peer Reviewed Journal)
Spinard III, E.J., Fish, I., Azzinaro, P.A., Rodriguez-Calzada, M., Hartwig, E.J., Smoliga, G.R., Arzt, J., De Los Santos, T.B., Medina, G.N. 2022. Evaluation of potential in vitro recombination events in codon deoptimized FMDV strains. Viruses. 15(3). https://doi.org/10.3390/v15030670.
Structural predictions of the complete ASFV-G proteome Reprint Icon - (Peer Reviewed Journal)
Spinard III, E.J., Azzinaro, P.A., Rai, A., Espinoza, N.N., Ramirez Medina, E., Borca, M.V., Gladue, D.P. 2022. Structural predictions of the complete ASFV-G proteome. Microbiology Resource Announcements. 11(12):e0088122. https://doi.org/10.1128/mra.00881-22.
Mutation of FMDV Lpro H138 reside outside substrate binding domain drives viral attenuation in vitro and in swine Reprint Icon - (Peer Reviewed Journal)
Azzinaro, P.A., Medina, G.N., Rai, D., Ramirez Medina, E., Spinard Iii, E.J., Zhu, J.J., Rieder, A.E., De Los Santos, T.B., Diaz San Segundo, F.C. 2022. Mutation of FMDV Lpro H138 reside outside substrate binding domain drives viral attenuation in vitro and in swine. Frontiers in Veterinary Science. https://www.frontiersin.org/articles/10.3389/fvets.2022.1028077/full.
Mutation of FMDV Lpro residues outside substrate binding domain drives viral attenuation Reprint Icon - (Abstract Only)
Diaz San Segundo, F.C., Azzinaro, P.A., Zhu, J.J., Medina, G.N., De Los Santos, T.B. 2022. Mutation of FMDV Lpro residues outside substrate binding domain drives viral attenuation. Meeting Abstract. https://doi.org/10.3389/fvets.2022.1028077.
Foot-and-Mouth Disease virus interserotypic recombination in superinfected carrier cattle Reprint Icon - (Peer Reviewed Journal)
Fish, I., Bertram, M.R., Stenfeldt, C., Smoliga, G.R., Hartwig, E.J., Holinka-Patterson, L.G., De Los Santos, T.B., Spinard III, E.J., Medina, G.N., Arzt, J., Azzinaro, P.A. 2022. Foot-and-Mouth Disease virus interserotypic recombination in superinfected carrier cattle. Pathogens. https://doi.org/10.3390/pathogens11060644.
An Adventitious agent free clonal cell line that is highly susceptible to foot and mouth disease virus Reprint Icon - (Peer Reviewed Journal)
Larocco, M., Krug, P., Ahmed, Z., Rodriguez-Calzada1, M., Azzinaro, P.A., Rodriguez, L.L., De Los Santos, T.B., Medina, G.N. 2021. An Adventitious agent free clonal cell line that is highly susceptible to foot and mouth disease virus. Journal of Clinical Microbiology. https://doi.org/10.1016/j.biologicals.2021.05.003.
Use of Protein Pegylation to prolong the antiviral effect of IFN against FMDV Reprint Icon - (Peer Reviewed Journal)
Diaz San Segundo, F.C., Medina, G.N., Mogulothu, A., Azzinaro, P.A., Attreed, S.E., Gutkoska, J.R., Lombardi, K.R., Shields, J., Hudock, T.A., De Los Santos, T.B. 2021. Use of Protein Pegylation to prolong the antiviral effect of IFN against FMDV. Frontiers in Microbiology. https://doi.org/10.3389/fmicb.2021.668890.
Use of synonymous deoptimization for the development of modified live attenuated strains of foot and mouth disease virus Reprint Icon - (Peer Reviewed Journal)
Diaz San Segundo, F.C., Medina, G., Spinard, E., Kloc, A., Ramirez-Medina, E., Azzinaro, P.A., Mueller, S., Rieder, A.E., De Los Santos, T.B. 2021. Use of synonymous deoptimization for the development of modified live attenuated strains of foot and mouth disease virus. Frontiers in Microbiology. https://doi.org/10.3389/fmicb.2020.610286.
Impairment of the deISGylation activity of foot-and-mouth disease Lpro causes viral attenuation without affecting interferon expression during viral infection. Reprint Icon - (Peer Reviewed Journal)
Medina, G., Azzinaro, P.A., Ramirez-Medina, E., Gutkoska, J.R., Fang, De Los Santos, T.B. 2020. Impairment of the deISGylation activity of foot-and-mouth disease Lpro causes viral attenuation without affecting interferon expression during viral infection. Virology. https://doi.org/10.1128/JVI.00341-20.
SERTA domain containing protein 1 (SERTAD1) interacts with classical swine fever virus structural glycoprotein E2 which is involved in virus virulence in swine Reprint Icon - (Peer Reviewed Journal)
Vuono, E., Ramirez-Medina, E., Azzinaro, P.A., Berggren, K., Rai, A., Pruitt, S., Silva, E., Velazquez-Salinas, L., Borca, M.V., Gladue, D.P. 2020. SERTA domain containing protein 1 (SERTAD1) interacts with classical swine fever virus structural glycoprotein E2 which is involved in virus virulence in swine. Journal of Virology. https://doi.org/10.3390/v12040421.
Structural glycoprotein E2 of classical swine fever virus binding to host protein dynactin subunit (DCTN6) is necessary for virus virulence in swine Reprint Icon - (Peer Reviewed Journal)
Borca, M.V., Vuono, E.A., Ramirez-Medina, E., Azzinaro, P.A., Berggren, K.A., Singer, M., Rai, A., Pruitt, S., Silva, E., Velazquez-Salinas, L., Carrillo, C., Gladue, D.P. 2019. Structural glycoprotein E2 of classical swine fever virus binding to host protein dynactin subunit (DCTN6) is necessary for virus virulence in swine. Journal of Virology. https://doi.org/10.1128/JVI.01642-19.