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Biology subjects

Azizi, B.

Publications and source records attributed to Azizi, B..

2 recordsLinked to original sources

A Generative Neuro-Symbolic AI for Protein Sequence Design

Deep learning has revolutionized computational protein design, enabling the generation of sequences that fold onto target backbones with unprecedented accuracy. However, state-of-the-art inverse folding tools largely rely on auto-regressive sampling. While powerful, this paradigm is increasingly recognized for its inability to "think ahead", a crucial capacity to reliably create the complex, long-range inter-residue dependencies essential for most biological functions. To overcome these fundamental limitations, we introduce EffieDes, a generative neuro-symbolic AI framework that synergizes the predictive capabilities of deep learning with the logical precision of automated reasoning. EffieDes leverages deep learning to encode the target backbones fitness landscape into Effie-- a fully decomposable probabilistic graphical model (Potts model). This landscape is then rigorously explored by an automated reasoning prover to identify sequences that simultaneously satisfy complex design constraints and optimize backbone fitness. We validated this neuro-symbolic approach through the design of orthogonal sequence pairs that adopt identical folds but exhibit selective self-assembly, as well as the design of a de novo selective nanobody with nanomolar affinity for an immune-evasive SARS-CoV-2 variant. EffieDes provides a robust architecture for precisely dissecting learned fitness landscapes, offering a new path toward proteins with highly optimized performances and sophisticated functional objectives.

bioengineering↗

Promiscuous structural cross-compatibilities between major shell components of Klebsiella pneumoniae bacterial microcompartments

Bacterial microcompartments (BMC) are submicrometric reactors that encapsulate dedicated metabolic activities. BMC-H hexamers, the most abundant components of BMC shells, play major roles for shell plasticity and permeability. In part, chemical exchanges between the BMC lumen and the cellular cytosol will be defined by the disposition of amino acids lining the central BMC-H pores. Current models attribute to BMC-H a homo-oligomeric nature. The hexagonal symmetry of corresponding pores, however, would break down if hetero-hexamers formed, a possibility suggested by the frequent presence of multiple paralogs within BMC operons. Here, we gauged the degree of structural promiscuity between the 11 BMC-H paralogs from Klebsiella pneumoniae, a potential human pathogen endowed with the capacity to express three different BMC types. Concomitant activation of transcription of several BMC operons was first shown to be possible. By leveraging an adapted tripartite GFP technology, all possible BMC-H pair combinations were screened in E. coli. Multiple structural cross-compatibilities were pinpointed between homologs arising not only from the same BMC operon, but also from different BMC types, results supported by Alphafold and ESMFold predictions. The structural stability and assembly propensity of selected hetero-associations was established by biochemical means. In light of these results, we reinterpreted published lysine cross-linking mass spectrometry data to demonstrate that one of these hetero-hexamers, involving PduA and PduJ, was already detected to form in the shell of a recombinantly-expressed 1,2-propanediol utilization compartment from Salmonella enterica. Altogether, this study points to the need to embrace an augmented structural complexity in BMC shells.

biochemistry↗