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Perez Lab

Mechanistic biology of cell wall assembly in pathogenic bacteria

Welcome to the Perez Lab

The bacterial cell wall is a complex matrix assembled through the activity of multiple pathways involving membrane proteins. Understanding their molecular mechanism is essential to unravel the mysteries behind the most important defense barrier of pathogenic bacteria. My laboratory aims to elucidate the mechanism of transporters, flippases and polymerases involved in the assembly of the cell wall, reveal how their function influences bacterial adaptation, discover molecules that inhibit the development of new antimicrobials and redirect the activity of these proteins towards applications in the synthesis of glycoconjugates. Read more on our Research page.

Selected Publications

Receptor-recognition and antiviral mechanisms of retrovirus-derived human proteins. Link to publication in NSMB In collaboration with the Reyes Lab we present cryo-electron microscopy structures and functional characterization of human ASCT2 in complexes with the receptor-binding domains of syncytin-1 and suppressyn, cellular proteins of retroviral origin involved in cell–cell fusion events to establish the maternal–fetal interface in the placenta. Our work uncovers a common ASCT2 recognition mechanism by a large group of endogenous and disease-causing retroviruses, and provides high-resolution views on how placental human proteins exert morphological and immunological functions.

Mechanistic basis of choline import involved in teichoic acids and lipopolysaccharide modification 
Link to publication in Sci. Adv.


We determined the structure and mechanism of LicB, a choline transporter involved in the cell wall biosynthesis of Streptococcus pneumoniae. We used a multidisciplinary approach including structure determination by cryo-EM and X-ray crystallography, electrophysiology, in-vitro transport assays, sybody generation in collaboration with the Seeger Lab, and in- vivo assays in collaboration with the Veening Lab.

Evidence for a trap-and-flip mechanism in a proton-dependent lipid transporter
Link to publication in Nat. Comm.

We investigated the flipping mechanism of LtaA, a proton-dependent MFS lipid transporter essential for lipoteichoic acid biosynthesis in the pathogen Staphylococcus aureus. Combining cysteine disulfide trapping, mutagenesis, transport assays in vitro and in vivo, and molecular dynamics simulations in collaboration with the Mehdipour Lab and Hummer Lab, we revealed that LtaA catalyzes lipid translocation by a trap-and-flip mechanism.

Structure of a proton-dependent lipid transporter involved in lipoteichoic acids biosynthesis
Link to publication in NSMB


We elucidated the first structure a lipid transporter from the MFS superfamily of transporters.  LtaA,  a flippase involved in lipoteichoic acid assembly in Staphylococcus aureus, catalyse lipid export by import of protons, which contributes to the adaptation of S. aureus to acidic stress conditions.

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Upcoming talks

September 2024     FASEB Microbial Glycobiology Conference, Southbridge MA, USA

July 2024     Biozentrum Discovery Seminar, Basel, Switzerland

July 2024     Gordon Research Conference Membrane Transport Proteins, Newry, ME, USA 

June 2024     Departmental Retreat, BMB, UGA

Latest Lab News

June 2024. New commentary in PNAS.

May 2024. New paper in mBio.

April 2024. New paper in Nat. Str. Mol. Biol.

January 2024. The Perez Lab arrives at UGA

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