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Biology subjects

Desautels, T. A.

Publications and source records attributed to Desautels, T. A..

2 recordsLinked to original sources

Unobserved Sequence Space Has Many Functional Proteins

The distribution of functional proteins across amino acid sequence space, and the proportion of functional space covered by existing proteins, remains unknown. Illuminating this distribution is integral to understanding protein evolution and advancing protein design. The recent explosion of AI/ML protein design tools presents an opportunity to explore protein sequence space distant from extant proteins, but these tools remain poorly validated. Here, we determine that portions of protein sequence space, despite being unobserved in nature, contains many functional proteins that cannot be predicted accurately in silico. We measure experimental fitness of highly diverse proteins across 3 families and assemble the largest known dataset of diverse, functionally labeled natural protein orthologs and new-to-nature proteins. For each family, we observe many functional, new-to-nature sequences with low amino acid identity to existing orthologs. Sequence-based scoring metrics, especially Potts models and protein language models, provide accurate but inconsistent and highly correlated function predictions. Empirical protein fitness landscapes are rugged, and predictions of function do not consistently capture either the local shape or global trends of the empirical fitness landscapes. Finally, we find extensive functional sequence space between existing proteins in each family, providing experimental support for the hypothesis that natural protein sequences explored by evolution represent a minuscule fraction of all possible functional sequences.

synthetic biology↗

Computationally restoring the potency of a clinical antibody against SARS-CoV-2 Omicron subvariants

The COVID-19 pandemic underscored the promise of monoclonal antibody-based prophylactic and therapeutic drugs1-3, but also revealed how quickly viral escape can curtail effective options4, 5. With the emergence of the SARS-CoV-2 Omicron variant in late 2021, many clinically used antibody drug products lost potency, including EvusheldTM and its constituent, cilgavimab4, 6. Cilgavimab, like its progenitor COV2-2130, is a class 3 antibody that is compatible with other antibodies in combination4 and is challenging to replace with existing approaches. Rapidly modifying such high-value antibodies with a known clinical profile to restore efficacy against emerging variants is a compelling mitigation strategy. We sought to redesign COV2-2130 to rescue in vivo efficacy against Omicron BA.1 and BA.1.1 strains while maintaining efficacy against the contemporaneously dominant Delta variant. Here we show that our computationally redesigned antibody, 2130-1-0114-112, achieves this objective, simultaneously increases neutralization potency against Delta and many variants of concern that subsequently emerged, and provides protection in vivo against the strains tested, WA1/2020, BA.1.1, and BA.5. Deep mutational scanning of tens of thousands pseudovirus variants reveals 2130-1-0114-112 improves broad potency without incurring additional escape liabilities. Our results suggest that computational approaches can optimize an antibody to target multiple escape variants, while simultaneously enriching potency. Because our approach is computationally driven, not requiring experimental iterations or pre-existing binding data, it could enable rapid response strategies to address escape variants or pre-emptively mitigate escape vulnerabilities.

microbiology↗