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Dr Alexander Tarr's Outputs (5)

Monoclonal antibody AP33 defines a broadly neutralizing epitope on the hepatitis C virus E2 envelope glycoprotein (2005)
Journal Article
Owsianka, A., Tarr, A. W., Juttla, V. S., Lavillette, D., Bartosch, B., Cosset, F. L., Ball, J. K., & Patel, A. H. (2005). Monoclonal antibody AP33 defines a broadly neutralizing epitope on the hepatitis C virus E2 envelope glycoprotein. Journal of Virology, 79(17), 11095-11104. https://doi.org/10.1128/JVI.79.17.11095-11104.2005

Hepatitis C virus (HCV) remains a significant threat to the general health of the world's population, and there is a pressing need for the development of new treatments and preventative vaccines. Here, we describe the generation of retrovirus-based p... Read More about Monoclonal antibody AP33 defines a broadly neutralizing epitope on the hepatitis C virus E2 envelope glycoprotein.

Analysis of the binding of hepatitis C virus genotype 1a and 1b E2 glycoproteins to peripheral blood mononuclear cell subsets (2005)
Journal Article
Yamada, E., Montoya, M., Schuettler, C. G., Hickling, T. P., Tarr, A. W., Vitelli, A., Dubuisson, J., Patel, A. H., Ball, J. K., & Borrow, P. (2005). Analysis of the binding of hepatitis C virus genotype 1a and 1b E2 glycoproteins to peripheral blood mononuclear cell subsets. Journal of General Virology, 86(9), 2507-2512. https://doi.org/10.1099/vir.0.81169-0

Hepatitis C virus (HCV) binding to hepatocytes is thought to be mediated via interaction of the E2 glycoprotein with (co-)receptors including CD81 and scavenger receptor class B type I (SR-BI). Here, the expression of CD81 and SR-BI was analysed on p... Read More about Analysis of the binding of hepatitis C virus genotype 1a and 1b E2 glycoproteins to peripheral blood mononuclear cell subsets.

Evolutionary dynamics of hepatitis C virus envelope genes during chronic infection (2005)
Journal Article
Brown, R. J., Juttla, V. S., Tarr, A. W., Finnis, R., Irving, W. L., Hemsley, S., Flower, D. R., Borrow, P., & Ball, J. K. (2005). Evolutionary dynamics of hepatitis C virus envelope genes during chronic infection. Journal of General Virology, 86(7), 1931-1942. https://doi.org/10.1099/vir.0.80957-0

Hepatitis C virus (HCV) envelope glycoproteins E1 and E2 are important targets for the host immune response. The genes encoding these proteins exhibit a high degree of variability that gives rise to differing phenotypic traits, including alterations... Read More about Evolutionary dynamics of hepatitis C virus envelope genes during chronic infection.

Characterization of host-range and cell entry properties of the major genotypes and subtypes of hepatitis C virus (2005)
Journal Article
Lavillette, D., Tarr, A. W., Voisset, C., Donot, P., Bartosch, B., Bain, C., Patel, A. H., Dubuisson, J., Ball, J. K., & Cosset, F. L. (2005). Characterization of host-range and cell entry properties of the major genotypes and subtypes of hepatitis C virus. Hepatology, 41(2), 265-274. https://doi.org/10.1002/hep.20542

Because of the lack of a robust cell culture system, relatively little is known about the molecular details of the cell entry mechanism for hepatitis C virus (HCV). Recently, we described infectious HCV pseudo-particles (HCVpp) that were generated by... Read More about Characterization of host-range and cell entry properties of the major genotypes and subtypes of hepatitis C virus.

Tagged polymerase chain reaction subtractive hybridization for the enrichment of phage display random peptide libraries (2005)
Journal Article
Tarr, A. W., Boneham, S. P., Grabowska, A. M., & Ball, J. K. (2005). Tagged polymerase chain reaction subtractive hybridization for the enrichment of phage display random peptide libraries. Analytical Biochemistry, 339(1), 61-68. https://doi.org/10.1016/j.ab.2004.12.020

Affinity selection of phage display peptide libraries is routinely used for isolating peptides capable of binding a range of molecules, including antibodies and receptors. This process is most successful when the selecting molecule is relatively pure... Read More about Tagged polymerase chain reaction subtractive hybridization for the enrichment of phage display random peptide libraries.