Inferring context-specific site variation with evotuned protein language models

Multiple sequence alignments (MSAs) have been traditionally used for making inferences about site-specific diversity in proteins. Recent advancements in the field of artificial intelligence have highlighted the potential of protein language models (pLMs) to capture similar protein properties. Unlike MSAs, pLMs can make inferences from single sequences, without the need for a set of aligned sequences. In this study, we introduce a variation of the Context-Dependent Entropy metric, based on pLM embeddings instead of MSA input, to assess protein site conservation and variability. We test this metric using versions of two popular pLMs (ESM-2 and protT5) fine-tuned on the diversity of different Influenza A virus subtype hemagglutinin proteins. Our study demonstrates how our pLM entropy metric can capture which sites are more likely to change in a specific sequence context and how fine-tuning pLMs on a set of evolutionarily related proteins (evotuning) can improve the models' understanding of the group's diversity.

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Publication Details

Journal
NAR Genomics and Bioinformatics
Published
2026-01-06
DOI
https://doi.org/10.1093/nargab/lqag018
Primary Topic
RNA and protein synthesis mechanisms
Type
article
Field-Weighted Citation Impact
0.00
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article

Inferring context-specific site variation with evotuned protein language models

K. Sato, Adam Strange, Jumpei Ito, Spyros Lytras
NAR Genomics and Bioinformatics
RNA and protein synthesis mechanisms
article

Inferring context-specific site variation with evotuned protein language models

K. Sato, Adam Strange, Jumpei Ito, Spyros Lytras
article en

Abstract

Multiple sequence alignments (MSAs) have been traditionally used for making inferences about site-specific diversity in proteins. Recent advancements in the field of artificial intelligence have highlighted the potential of protein language models (pLMs) to capture similar protein properties. Unlike MSAs, pLMs can make inferences from single sequences, without the need for a set of aligned sequences. In this study, we introduce a variation of the Context-Dependent Entropy metric, based on pLM embeddings instead of MSA input, to assess protein site conservation and variability. We test this metric using versions of two popular pLMs (ESM-2 and protT5) fine-tuned on the diversity of different Influenza A virus subtype hemagglutinin proteins. Our study demonstrates how our pLM entropy metric can capture which sites are more likely to change in a specific sequence context and how fine-tuning pLMs on a set of evolutionarily related proteins (evotuning) can improve the models' understanding of the group's diversity.

NAR Genomics and BioinformaticsVol. 8(1)
National Institute of Infectious Diseases (JP), Saitama International Medical Center (JP), MRC University of Glasgow Centre for Virus Research (GB), The University of Tokyo (JP), Kumamoto University (JP)
Openalex Percentile: Top 63%
RNA and protein synthesis mechanisms
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Inferring context-specific site variation with evotuned protein language models — K. Sato, Adam Strange, et al. · NAR Genomics and Bioinformatics (2026) | TGRS Research Map | TGRS