CD4+ Th immunogenicity of the Ascaris spp. secreted products

Ascaris spp. is a major health problem of humans and animals alike, and understanding the immunogenicity of its antigens is required for developing urgently needed vaccines. The parasite-secreted products represent the most relevant, yet complex (>250 proteins) antigens of Ascaris spp. as defining the pathogen-host interplay. We applied an in vitro antigen processing system coupled to quantitative proteomics to identify potential CD4+ Th cell epitopes in Ascaris-secreted products. This approach considerably restricts the theoretical list of epitopes using conventional CD4+ Th cell epitope prediction tools. We demonstrate the specificity and utility of our approach on two sets of candidate lists, allowing us identifying hits excluded by either one or both computational methods. More importantly, one of the candidates identified experimentally, clearly demonstrates the presence of pathogen-reactive T cells in healthy human individuals against these antigens. Thus, our work pipeline identifies the first human T cell epitope against Ascaris spp. and represents an easily adaptable platform for characterization of complex antigens, in particular for those pathogens that are not easily amenable for in vivo experimental validation

Design and synthesis of ruthenium(II) and iridium(III) metallopeptides to selectively interact with double stranded DNA

Sintesi di metallopeptidi di rutenio e iridio che abbiano la capacità di legarsi al DNA. Lo scopo è di creare sonde utilizzabili in vivo e in vitro che riescono a raggiungere il DNA della cellula e legarsi in specifiche sezion

Exploring monovalent and multivalent peptides for the inhibition of FBP21-tWW

The coupling of peptides to polyglycerol carriers represents an important route towards the multivalent display of protein ligands. In particular, the inhibition of low affinity intracellular protein–protein interactions can be addressed by this design. We have applied this strategy to develop binding partners for FBP21, a protein which is important for the splicing of pre-mRNA in the nucleus of eukaryotic cells. Firstly, by using phage display the optimized sequence WPPPPRVPR was derived which binds with KDs of 80 μM and 150 µM to the individual WW domains and with a KD of 150 μM to the tandem-WW1–WW2 construct. Secondly, this sequence was coupled to a hyperbranched polyglycerol (hPG) that allowed for the multivalent display on the surface of the dendritic polymer. This novel multifunctional hPG-peptide conjugate displayed a KD of 17.6 µM which demonstrates that the new carrier provides a venue for the future inhibition of proline-rich sequence recognition by FBP21 during assembly of the spliceosome

Custom‐Fit Ruthenium(II) Metallopeptides: A New Twist to DNA Binding With Coordination Compounds

This is the peer reviewed version of the following article: Gamba, I., Salvadó, I., Rama, G., Bertazzon, M., Sánchez, M. I., Sánchez‐Pedregal, V. M., Martínez‐Costas, J. , Brissos, R. F., Gamez , P., Mascareñas, J. L., Vázquez López, M. and Vázquez, M. E. (2013), Custom‐Fit Ruthenium(II) Metallopeptides: A New Twist to DNA Binding With Coordination Compounds. Chem. Eur. J., 19: 13369-13375, which has been published in final form at https://doi.org/10.1002/chem.201301629. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived VersionsUnknown funding agency. Grant Numbers: SAF2010–20822‐C02, CTQ2012–31341, CTQ2009–14431, CTQ2011–27929‐C02–01, SAF2007–61015 Xunta de Galicia. Grant Numbers: INCITE09 209 084PR, GRC2010/12, PGIDIT08CSA‐047209PR COST Action. Grant Number: CM1105 Fundación José Otero–Carmela Martínez Spanish Ministry of Science and Technology European Nanotechnology Laboratory (ENL)S