Biophysics and Biochemistry of Macromolecular Interactions Laboratory

Group leader
Cesar Martin and Helena Ostolaza
Phone
+34 94 601 8052 / +34 94 601 5538
Research goal

We are an interdisciplinary research group combining biophysical, cell biology, biochemistry and molecular biology methodologies. Two are our main research focuses are:

  • The study of the molecular mechanisms that underlie protein-protein and protein-membrane interactions, using bacterial toxins as a model system, in particular, the adenylate cyclase toxins, which are essential virulence factors produced by different bacterial pathogens (e.g. Bordetella pertussis, Escherichia coli).
  • Understanding the molecular mechanism that leads to genetic/hereditary hypercholesterolemia and cardiovascular disease. We do translational research by assessing pathogenic variants of LDLR, ApoB-100 and PCSK9 to provide a certain genetic diagnosis of the disease.
Group members
Postdoctoral Fellow
University Lecturer
University Professor
Publications

Galicia-Garcia, U., Benito-Vicente, A., Uribe, K.B., Jebari, S., Larrea-Sebal, A., Alonso-Estrada, R., Aguilo-Arce, J., Ostolaza, H., Palacios, L., Martin, C.

Mutation type classification and pathogenicity assignment of sixteen missense variants located in the EGF-precursor homology domain of the LDLR (2020) Scientific reports, 10 (1), p. 1727. DOI: 10.1038/s41598-020-58734-9

Sánchez-Hernández, R.M., Di Taranto, M.D., Benito-Vicente, A., Uribe, K.B., Lamiquiz-Moneo, I., Larrea-Sebal, A., Jebari, S., Galicia-Garcia, U., Nóvoa, F.J., Boronat, M., Wägner, A.M., Civeira, F., Martín, C., Fortunato, G.

The Arg499His gain-of-function mutation in the C-terminal domain of PCSK9 (2019) Atherosclerosis, 289, pp. 162-172. DOI: 10.1016/j.atherosclerosis.2019.08.020

Ostolaza, H., González-Bullón, D., Uribe, K.B., Martín, C., Amuategi, J., Fernandez-Martínez, X.

Membrane permeabilization by pore-forming rtx toxins: What kind of lesions do these toxins form? (2019) Toxins, 11 (6). DOI: 10.3390/toxins11060354

González-Bullón, D., Uribe, K.B., Largo, E., Guembelzu, G., García-Arribas, A.B., Martín, C., Ostolaza, H.

Membrane permeabilization by bordetella adenylate cyclase toxin involves pores of tunable size (2019) Biomolecules, 9 (5). DOI: 10.3390/biom9050183

Etxaniz, A., González-Bullón, D., Martín, C., Alonso, M.T., Ostolaza, H.

Irreversible versus repairable membrane poration: differences in permeabilization elicited by Bordetella Adenylate Cyclase Toxin and its hemolysin domain in macrophages (2019) FEBS Journal, DOI: 10.1111/febs.15106

Banerjee, P., Chan, K.-C., Tarabocchia, M., Benito-Vicente, A., Alves, A.C., Uribe, K.B., Bourbon, M., Skiba, P.J., Pordy, R., Gipe, D.A., Gaudet, D., Martin, C.

Functional analysis of LDLR (low-density lipoprotein receptor) variants in patient lymphocytes to assess the effect of evinacumab in homozygous familial hypercholesterolemia patients with a spectrum of LDLR activity (2019) Arteriosclerosis, Thrombosis, an

González-Bullón, D., Martín, C., Ostolaza, H.

Characterization of the intrinsic phospholipase A1 activity of bordetella pertussis adenylate cyclase toxin (2018) Toxins, 10 (12), DOI: 10.3390/toxins10120514

Benito-Vicente, A., Siddiqi, H., Uribe, K.B., Jebari, S., Galicia-Garcia, U., Larrea-Sebal, A., Stef, M., Ostolaza, H., Palacios, L., Martin, C. p.(Asp47Asn) and p.(Thr62Met)

non deleterious LDL receptor missense variants functionally characterized in vitro (2018) Scientific Reports, 8 (1), DOI: 10.1038/s41598-018-34715-x

Benito-Vicente, A., Uribe, K.B., Jebari, S., Galicia-Garcia, U., Ostolaza, H., Martin, C.

Validation of LDLr activity as a tool to improve genetic diagnosis of familial hypercholesterolemia: A retrospective on functional characterization of LDLr variants (2018) International Journal of Molecular Sciences, 19 (6), DOI: 10.3390/ijms19061676

González-Bullón D, Uribe KB, Martín C, Ostolaza H.

Phospholipase A activity of adenylate cyclase toxin mediates translocation of its adenylate cyclase domain. (2017).Proc Natl Acad Sci U S A. 114(33):E6784-E6793. doi:10.1073/pnas.1701783114