Biotechnology

Structural Biotechnology

Antimicrobial Resistance (AMR)

IgY Avian Antibodies

Antibodies

Virulence Factors

Membrane Proteins

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Leader

Ricardo Pires

Researcher


Research lines

Antimicrobial resistance mechanisms

Anti-infective Immunotherapies

Avian IgY antibodies

Biologics and Biopharmaceutical drugs

Antibody Biotechnology to Health and Food Sciences

Overview

The Structural Biotechnology Group aims to explore alternative strategies to combat infectious diseases with a strong focus on research and development of protein and antibody-based antimicrobial and antiviral solutions. The group envisages namely the design of novel strategies to target surface-exposed virulent factors, including membrane transporters, channels and enzymes, responsible for infections and diseases caused by pathogenic microorganisms and viruses. We integrate biochemical and biophysical approaches for the structural and functional characterization of such proteins and protein complexes with a direct role in pathogenic processes.

A prominent approach of the group is to explore avian antibodies as alternative biological drugs to target microbial and viral pathogens. This is a reemerging approach in the pharmaceutical industry since the use of hens enables generation of highly robust and specific polyclonal antibodies and importantly provides a scalable, low-cost, high-yield production system due to antibody deposition in hen eggs. Moreover, generation of combinatorial antibody phage-display libraries from avian sources is simplified over mammalian systems given the unique organization of avian immunoglobulin genes, thus favoring screening and engineering strategies to develop target-specific monoclonal antibodies for therapy. Importantly, the group coordinates the logistics and activities of CNC AVIAN TECHNOLOGICAL UNIT (CNC-ATU), a unit fully designed to support translational and applied research and development on the competitive and fast-growing field of Biologicals and Biopharmaceutical drugs.

Publications

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Information about journal articles, updated at 05-12-2021, from platform CIÊNCIAVITAE.

I Rest My Case! The Possibilities and Limitations of Blockchain- Based IP Protection

Barata, Sofia Lopes; Vieira-Pires, Ricardo S.; Cunha, Paulo Rupino, 2020. Lecture Notes in Information Systems and Organization. 2020. submitted Lecture Notes in Information Systems and Organization

Antibody discovery using Japanese quail: towards new anti-infective strategies

Ochôa-Pires, Tiago; Rosa, Marguerita; Laranjeira, João; Francisco, Rafael; Silva, Diana; Vieira-Pires, Ricardo S., 2020. Ecronicon Microbiology. 29 - 36. 6. 16. 2020. https://www.ecronicon.com/ecmi/pdf/ECMI-16-00936.pdf . published Ecronicon Microbiology

Chicken egg yolk antibody (IgY) as diagnostics and therapeutics in parasitic infections – A review

Thirumalai, Diraviyam; Visaga Ambi, Senthil; Vieira-Pires, Ricardo S.; Xiaoying, Zhang; Sekaran, Saravanan; Krishnan, Umamaheswari, 2019. International Journal of Biological Macromolecules. 755 - 763. 136. 2019. http://dx.doi.org/10.1016/j.ijbiomac.2019.06.118 . 10.1016/j.ijbiomac.2019.06.118 . International Journal of Biological Macromolecules

Dissecting the Molecular Mechanism of Nucleotide-Dependent Activation of the KtrAB K+ Transporter

Szollosi, Andras; Vieira-Pires, Ricardo S.; Teixeira-Duarte, Celso M.; Rocha, Rita; Morais-Cabral, João H., 2016. PLOS Biology. 1. 14. 2016. http://dx.doi.org/10.1371/journal.pbio.1002356 . 10.1371/journal.pbio.1002356 . PLOS Biology

The Structure of the KtrAB Potassium Transporter

Vieira-Pires, Ricardo; Szollosi, Andras; Morais-Cabral, João, 2013. Biophysical Journal. 2. 104. 2013. http://dx.doi.org/10.1016/j.bpj.2012.11.162 . 10.1016/j.bpj.2012.11.162 . Biophysical Journal

Functional Characterization of the KtrAB Potassium Transport System

Szollosi, Andras; Vieira-Pires, Ricardo S.; Morais-Cabral, João H., 2013. Biophysical Journal. 2. 104. 2013. http://dx.doi.org/10.1016/j.bpj.2012.11.650 . 10.1016/j.bpj.2012.11.650 . Biophysical Journal

The structure of the KtrAB potassium transporter

Vieira-Pires, Ricardo S.; Szollosi, Andras; Morais-Cabral, João H., 2013. Nature. 323 - 328. 7445. 496. 2013. http://dx.doi.org/10.1038/nature12055 . 10.1038/nature12055 . Nature

Structural and Biochemical Characterization of a Cyclic Nucleotide Binding Domain from the EAG Family

Marques Carvalho, Maria J.; Vieira Pires, Ricardo S.; Gabant, Guillaume; Cadene, Martine; Morais Cabral, João H., 2012. Biophysical Journal. 3. 102. 2012. http://dx.doi.org/10.1016/j.bpj.2011.11.1809 . 10.1016/j.bpj.2011.11.1809 . Biophysical Journal

Structural, Biochemical, and Functional Characterization of the Cyclic Nucleotide Binding Homology Domain from the Mouse EAG1 Potassium Channel

Marques-Carvalho, Maria J.; Sahoo, Nirakar; Muskett, Frederick W.; Vieira-Pires, Ricardo S.; Gabant, Guillaume; Cadene, Martine; Schönherr, Roland; Morais-Cabral, João H., 2012. Journal of Molecular Biology. 34 - 46. 1. 423. 2012. http://dx.doi.org/10.1016/j.jmb.2012.06.025 . 10.1016/j.jmb.2012.06.025 . Journal of Molecular Biology

310 helices in channels and other membrane proteins

Vieira-Pires, Ricardo Simão; Morais-Cabral, João Henrique, 2010. The Journal of General Physiology. 585 - 592. 6. 136. 2010. http://dx.doi.org/10.1085/jgp.201010508 . 10.1085/jgp.201010508 . The Journal of General Physiology

Structure and function of ESCRT-III

Lata, Suman; Schoehn, Guy; Solomons, Julianna; Pires, Ricardo; Göttlinger, Heinrich G.; Weissenhorn, Winfried, 2009. Biochemical Society Transactions. 156 - 160. 1. 37. 2009. http://dx.doi.org/10.1042/bst0370156 . 10.1042/bst0370156 . Biochemical Society Transactions

A Crescent-Shaped ALIX Dimer Targets ESCRT-III CHMP4 Filaments

Pires, Ricardo; Hartlieb, Bettina; Signor, Luca; Schoehn, Guy; Lata, Suman; Roessle, Manfred; Moriscot, Christine; et al, 2009. Structure. 843 - 856. 6. 17. 2009. http://dx.doi.org/10.1016/j.str.2009.04.007 . 10.1016/j.str.2009.04.007 . Structure

Helical Structures of ESCRT-III Are Disassembled by VPS4

Lata, S.; Schoehn, G.; Jain, A.; Pires, R.; Piehler, J.; Gottlinger, H. G.; Weissenhorn, W., 2008. Science. 1354 - 1357. 5894. 321. 2008. http://dx.doi.org/10.1126/science.1161070 . 10.1126/science.1161070 . Science

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