---
title: "Positive selection targets exposed extracellular surfaces and host–pathogen interaction modules"
id: "biorxiv-0-positive-selection-tends-to-act-on-exposed-extracellular-regions-and-delineate"
canonical_url: "https://medichelpline.com/clinical-feed/biorxiv-0-positive-selection-tends-to-act-on-exposed-extracellular-regions-and-delineate"
content_type: "clinical_feed_article"
specialty: "Infectious Disease"
source_name: "bioRxiv (Biomedical Preprints)"
source_url: "https://www.biorxiv.org/content/10.64898/2026.09.21.753075v1?rss=1"
published_at: "2026-09-22T12:00:00.000Z"
evidence_level: "Verified Feed"
license: "CC-BY-NC-4.0 / Informational Use"
---
# Positive selection targets exposed extracellular surfaces and host–pathogen interaction modules
## Provenance & Clinical Metadata
- **Canonical URL:** https://medichelpline.com/clinical-feed/biorxiv-0-positive-selection-tends-to-act-on-exposed-extracellular-regions-and-delineate
- **Specialty:** [Infectious Disease](https://medichelpline.com/clinical-feed/infectious-disease.md)
- **Primary Source:** bioRxiv (Biomedical Preprints)
- **Source URL:** [Original Journal Publication](https://www.biorxiv.org/content/10.64898/2026.09.21.753075v1?rss=1)
- **Published At:** 2026-09-22T12:00:00.000Z
- **Evidence Rating:** Verified Feed
## Executive GIST (TL;DR)
- The authors performed a comprehensive analysis of human positively selected genes (PSGs) and positively selected residues (PSRs), including a large-scale dataset restricted to proteins with experimental structures. - **Positive selection** in humans is concentrated in **secreted** and **cell membrane proteins**, with PSRs preferentially located in **extracellular regions** and on **solvent-exposed** surfaces. - PSRs are enriched in **coil** secondary structure and at **protein–protein interaction interfaces**, and they tend to form spatially localized surface clusters (surface patches). - Neither annotated protein **domains** nor **intrinsically disordered regions (IDRs)** showed enrichment for PSRs in the datasets analyzed. - Integration with host–pathogen interaction data showed that adaptive changes recurrently affect extracellular molecular recognition surfaces and particular pathogen-interacting membrane protein families and domain types. - PSRs are enriched specifically in residues that are in direct contact with pathogenic proteins at human–pathogen interaction interfaces, indicating pathogen pressure as a driver of adaptive evolution. - Analysis of human variation data found PSRs are enriched in **benign** variants but depleted in **pathogenic** substitutions, consistent with prior observations of elevated missense variation in PSGs. - PSGs in the large-scale dataset are enriched among clinical-stage drug targets, suggesting a possible link between adaptive evolution and pharmacological relevance. - The authors present a refined structural model in which extracellular exposed molecular recognition surfaces and human–pathogen interfaces are recurrent hotspots of positive selection and propose that precise PSR mapping could delineate host–pathogen interfaces and identify therapeutic targets.
## Clinical Analysis & Structured Key Points
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Laszlo Dobson 1 Institute of Molecular Life Sciences, Research Centre for Natural Sciences; * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Laszlo%2BDobson%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Dobson%20L&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3ALaszlo%2BDobson%2B) * [ORCID record for Laszlo Dobson](http://orcid.org/0000-0003-2765-3872 "Open in new tab") * For correspondence: dobson.laszlo@ttk.hu Eva Schad 1 Institute of Molecular Life Sciences, Research Centre for Natural Sciences; * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Eva%2BSchad%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Schad%20E&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3AEva%2BSchad%2B) * [ORCID record for Eva Schad](http://orcid.org/0000-0002-3006-2910 "Open in new tab") Erzsebet Ficho 2 Department of Bioinformatics, Cytocast Hungary Kft * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Erzsebet%2BFicho%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Ficho%20E&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3AErzsebet%2BFicho%2B) * [ORCID record for Erzsebet Ficho](http://orcid.org/0000-0002-3965-8438 "Open in new tab") Agnes Tantos 1 Institute of Molecular Life Sciences, Research Centre for Natural Sciences; * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Agnes%2BTantos%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Tantos%20A&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3AAgnes%2BTantos%2B) * [ORCID record for Agnes Tantos](http://orcid.org/0000-0003-1273-9841 "Open in new tab") Andras Szabo 1 Institute of Molecular Life Sciences, Research Centre for Natural Sciences; * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Andras%2BSzabo%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Szabo%20A&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3AAndras%2BSzabo%2B) Gabor E Tusnady 1 Institute of Molecular Life Sciences, Research Centre for Natural Sciences; * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Gabor%2BE%2BTusnady%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Tusnady%20GE&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3AGabor%2BE%2BTusnady%2B) * [ORCID record for Gabor E Tusnady](http://orcid.org/0000-0001-8105-0285 "Open in new tab") Rita Pancsa 1 Institute of Molecular Life Sciences, Research Centre for Natural Sciences; * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Rita%2BPancsa%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Pancsa%20R&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3ARita%2BPancsa%2B) * [ORCID record for Rita Pancsa](http://orcid.org/0000-0003-0849-9312 "Open in new tab") * [Abstract](https://www.biorxiv.org/content/10.64898/2026.09.21.753075v1)[](https://www.biorxiv.org/panels_ajax_tab/biorxiv_tab_art/node:5800685/1) * [Info/History](https://www.biorxiv.org/content/10.64898/2026.09.21.753075v1.article-info)[](https://www.biorxiv.org/panels_ajax_tab/biorxiv_tab_info/node:5800685/1) * [Metrics](https://www.biorxiv.org/content/10.64898/2026.09.21.753075v1.article-metrics)[](https://www.biorxiv.org/panels_ajax_tab/article_tab_metrics/node:5800685/1) * [Supplementary material](https://www.biorxiv.org/content/10.64898/2026.09.21.753075v1.supplementary-material)[](https://www.biorxiv.org/panels_ajax_tab/biorxiv_tab_data/node:5800685/1) * [ Preview PDF](https://www.biorxiv.org/content/10.64898/2026.09.21.753075v1.full.pdf+html)[](https://www.biorxiv.org/panels_ajax_tab/biorxiv_tab_pdf/node:5800685/1) ![Loading](https://www.biorxiv.org/sites/all/modules/contrib/panels_ajax_tab/images/loading.gif) ## Abstract Background: Positive selection shapes protein function by favoring amino acid substitutions that increase fitness. Although numerous studies have identified positively selected genes (PSGs), the structural principles underlying residue-level positive selection remain incompletely understood and previous studies have produced conflicting conclusions, particularly regarding the role of intrinsically disordered regions. In order to resolve these issues and to better understand the driving forces underlying positive selection in human proteins in general, we performed a comprehensive analysis on a manually curated, high quality collection of PSGs and positively selected residues (PSRs) as well as on a large-scale PSR dataset restricted to proteins with experimental structures. Results: Human PSRs were significantly enriched in secreted and cell membrane proteins and preferentially localized to extracellular regions, solvent-exposed surfaces, coil structures, and protein-protein interaction interfaces, whereas neither domains nor intrinsically disordered regions showed an enrichment. Spatial clustering analysis reinforced that PSRs accumulate within localized surface patches. Integration of host-pathogen interaction data highlighted that adaptive changes preferentially affect extracellular molecular recognition surfaces, recurrently appearing in certain pathogen-interacting membrane protein families and particular domain types. Additionally, PSRs showed an enrichment in the residues of human-pathogen interaction interfaces that are in direct contact with pathogenic proteins, implying that neutralizing pathogen attacks is one of the driving forces behind the adaptive evolution of human proteins. By analysing human variation data we found that PSRs are enriched in benign but depleted in pathogenic substitutions, extending previous observations that positively selected genes contain elevated levels of missense variation. Notably, PSGs of the large-scale dataset were also enriched among clinical-stage drug targets, suggesting a potential link between positive selection and pharmacological relevance. Conclusion: Together, our results provide a refined structural model of adaptive evolution in human proteins and identify extracellular exposed molecular recognition surfaces and human-pathogen interaction interfaces as recurrent hotspots of positive selection. Our results point to the direction that precise identification of human PSRs could delineate important host-pathogen interfaces that exert evolutionary selection pressure on humans and appoint novel targets with therapeutic potential. ### Competing Interest Statement E.F. is an employee of Cytocast Hungary Kft. Furthermore, E.F. owns equities or stocks of the company. All other authors declare no competing interest. ## Funder Information Declared Ministry of Culture and Innovation of Hungary, K-146314, FK-142285, PD-146564, STARTING-152403, ADVANCED-152119, K-142851 Hungarian Academy of Sciences, BO/00549/26/8, BO/00056/26 Copyright The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a [CC-BY 4.0 International license](http://creativecommons.org/licenses/by/4.0/). bioRxiv and medRxiv thank the following for their generous financial support: > The Chan Zuckerberg Initiative, Cold Spring Harbor Laboratory, the Sergey Brin Family Foundation, California Institute of Technology, Centre National de la Recherche Scientifique, Fred Hutchinson Cancer Center, Imperial College London, Massachusetts Institute of Technology, Stanford University, The University of Edinburgh, University of Washington, and Vrije Universiteit Amsterdam. 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[ Download PDF](https://www.biorxiv.org/content/10.64898/2026.09.21.753075v1.full.pdf) Print/Save Options [Download PDF](https://www.biorxiv.org/content/biorxiv/early/2026/09/22/2026.09.21.753075.full.pdf)Full Text & In-line FiguresXML [More Info](https://www.biorxiv.org/about/FAQ#PrintOptions "More Information on Print/Save Options") [Supplementary Material ](https://www.biorxiv.org/content/10.64898/2026.09.21.753075v1.supplementary-material) [ Email](https://www.biorxiv.org/ "Email this Article") [ Share](https://www.biorxiv.org/) Positive selection tends to act on exposed extracellular regions and delineate interaction modules targeted by pathogens Laszlo Dobson, Eva Schad, Erzsebet Ficho, Agnes Tantos, Andras Szabo, Gabor E Tusnady, Rita Pancsa bioRxiv 2026.09.21.753075; doi: https://doi.org/10.64898/2026.09.21.753075 This article is a preprint and has not been certified by peer review [[what does this mean?](https://www.biorxiv.org/about/FAQ#unrefereed)]. 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