Andrés Rivas-Pardo, PhD.

Principal Investigator and Assistant Professor

Mechanical Biology Laboratory

PhD in Sciences, Universidad de Chile, Chile.

jaime.rivas@umayor.cl

Líneas de Investigación

Titin elasticity

Bacterial adhesion

Cell-Cell communication

Mechanical Biology Laboratory

Our group is interested in determining how mechanical forces modulate several critical biological processes, from cell-cell communication to bacterial adhesion. Specifically, we aim to understand the evolutional perspective, genes involved, and the responses implemented within the cell in response to multiple mechanical cues.

Recently, we have implemented several experiments that aim to determine how a gene family highly conserved in nature—adhesin gene—, is involved in bacterial adhesion to human epithelia. We analyze the evolutive differences found in the sequences, and how these changes are translated to protein structure and modify the adhesion mechanisms.

In the last year, we established a mechanical assay that allows us to characterize the giant protein of striated muscle, titin (Nature Comm 11; 2060). These experiments will help us to contribute to determining the emerging role that this gene and protein play in the myocyte.

Our research lines:

  1. Titin elasticity: we use protein engineering to study a short segment of the titin gene, involved in familial cardiomyopathies. This portion of the TTN gene includes an immunoglobulin-like domain, which shows a mutation that has been related to changes in the elastic properties of the muscle cell (Rivas-Pardo, ETLS 2018).
  2. Bacterial adhesion: we proposed a comparative study of the genes involved in the adhesion of Gram-positive pathogenic bacteria. In the lab, we use multiple genes that coded for the proteins involved in the adhesion of bacteria. Our study model are based on the mechanisms used by Streptococcus pyogenes, Corynebacterium diphtheriae and Gram-negatives Salmonella enterica y Escherichia coli. Furthermore, we are working on the implementation of strategies that interfere with the folding of these adhesins (Rivas-Pardo et al PNAS 2018).
  3. Cell-Cell communication: alpha- and beta-catenin are cell mechanotransducers, which are in charge of transmitting mechanical cues from and to the cytoskeleton. Our research group aims to understand how these mechanotransducers mediate several responses from the membrane cadherin and their interaction with other auxiliary proteins recruited during the mechanical solicitation.

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Biography

Jaime Andrés Rivas Pardo graduated from the biochemistry program at Universidad Santiago de Chile. Under the supervision of Emilio Cardemil, he studied gluconeogenic enzymes using fluorescence and classic enzymology for the optimization of yeast metabolic pathways. Later, he joined the Molecular Cell Biology Ph.D. Program at Universidad de Chile, where he joined the laboratory of Biochemistry and Molecular Biology lead by Victoria Guixé. Combining enzyme kinetics, strategies based in X-rays, and single-molecule spectroscopy, Dr. Rivas Pardo studied glycolytic enzymes from archaea organisms. His studies included experiments that carried out in Chile and also through collaborations and scholar exchanges with Universidad de Sao Paulo (Brazil), Synchrotron-LNLS (Brazil), and Columbia University (USA). After finishing his graduate studies, Dr. Rivas Pardo joined Julio Fernandez´s lab at the Department of Biological Sciences (CU, USA), where he was trained in protein engineering and biophysics of biomolecules, in particular of the elastic proteins. In the lab, he learned Force Spectroscopy instrumentation, Atomic Force Microscopy, and Magnetic Tweezers-based, novel technologies for the manipulation of single molecules. Finally, Dr. Rivas Pardo moved back to Chile and joined to the Soft Matter Research Center (SMAT-C) lead by Francisco Melo at the Physics Department, Universidad de Santiago. In SMAT-C he worked in the design of mechanical-fluorescent probes on AFM cantilevers and bacterial adhesion mechanism. In March of 2019, Dr. Rivas Pardo joined the Center for Genomics and Bioinformatics at Universidad Mayor, starting with his lab in the emerging topic of Mechano-Biology. His lab aims to understand how the force modulates biological processes.

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Selected publications

  1. Fernanda Contreras and Jaime Andrés Rivas-Pardo (2020). Interfering With the Folding of Group A Streptococcal Pili Proteins. Methods Mol Biol 2136:347-364.
  2. Jaime Andrés Rivas-Pardo, Yong Li, Zsolt Martonflavi, Rafael Tapia-Rojo, Andreas Unger, Angel Fernandez-Trasancos, Eléas Guerrero-Galán, Diana Velázquez-Carrera, Julio M. Fernández, Wolfgang Linke, and Jorge Alegre-Cebollada (2020). A HaloTag-TEV genetic cassette for mechanical phenotyping of proteins from tissues. Nature Communicatios 11:2060.
  3. Jaime Andrés Rivas-Pardo, Carmen L. Badilla, Rafael Tapia-Rojo, Alvaro Alonso-Caballero, and Julio M. Fernández (2018). Molecular strategy for blocking isopeptide bond formation in nascent pilin proteins. Proc Natl Acad Sci U S A. 2018 115:9222-9227. PMID: 30150415.
  4. Jaime Andrés Rivas-Pardo, Edward C. Eckels, Ionel Popa, Pallav Kosuri, Wolfgang A Linke, and Julio M Fernández. (2016). Work Done by Titin Protein Folding Assists Muscle Contraction. Cell Reports 14, 1339-47. PMID: 26854230.
  5. Jaime Andrés Rivas-Pardo, Jorge Alegre-Cebollada, César A. Ramírez-Sarmiento, Julio M. Fernandez, and Victoria Guixé (2015). Identifying Sequential Substrate Binding at the Single-Molecule Level by Enzyme Mechanical Stabilization. ACS Nano 9, 3996-4005. PMID: 25840594.
  6. Jessica Valle-Orero J*, Jaime Andrés Rivas-Pardo*, Rafael Tapia-Rojo, Ionel Popa, Daniel J. Echelman, Shubhasis Haldar, and Julio M. Fernández. (2017). Mechanical Deformation Accelerates Protein Ageing. Angewandte Chemie, 56(33):9741-9746. NIHMSID: NIHMS874251 PMID: 28470663 PMCID: PMC5540753. *co-first author
  7. Jorge Alegre-Cebollada, Pallav Kosuri, David Giganti, Edward Eckels, Jaime Andrés Rivas-Pardo, Nazha Hamdani, Chad M. Warren, R. John Solaro, Wolfgang A. Linke, and Julio M. Fernandez (2014). S- Glutathionylation of Cryptic Cysteines Enhances Titin Elasticity by Blocking Protein Folding. Cell 156, 1235–1246, PMCID: PMC398984.
  8. Jorge Alegre-Cebollada, Pallav Kosuri, Jaime Andrés Rivas-Pardo, and Julio M. Fernandez (2014). Direct Observation of Disulfide Isomerization in a Single Protein. Nat Chem ;3(11):882-7.

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Contact

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