Evidence map›Paper›PMID 41267098›Full record

ArticleCell & bioscience2025

RNA-binding protein PTBP1 mediates HSV-1 attachment and infection through regulation of heparan sulfate 3-O-sulfotransferase gene expression.

Weikang Sun, Mengyu Zhang, Ruilin Wang, Jie Yang, Ameena Tur Rasool, Renjie Luo, Xiangdong Liu, Peng Cao, Erguang Li

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell & bioscience, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Weikang Sun *State Key Laboratory of Pharmaceutical Biotechnology, Medical School, Nanjing University, Jiangsu, 210093, Nanjing, China.
Mengyu Zhang *State Key Laboratory of Pharmaceutical Biotechnology, Medical School, Nanjing University, Jiangsu, 210093, Nanjing, China.
Ruilin Wang *State Key Laboratory of Pharmaceutical Biotechnology, Medical School, Nanjing University, Jiangsu, 210093, Nanjing, China.
Jie YangJiangsu Key Laboratory of Molecular Medicine, Medical School, Nanjing University, Jiangsu, Nanjing, China.
Ameena Tur RasoolState Key Laboratory of Pharmaceutical Biotechnology, Medical School, Nanjing University, Jiangsu, 210093, Nanjing, China.
Renjie LuoState Key Laboratory of Pharmaceutical Biotechnology, Medical School, Nanjing University, Jiangsu, 210093, Nanjing, China.
Xiangdong LiuCollege of Synthetic Biology Industry, Changde Center for Synthetic Biology Innovation, Hunan University of Arts and Science, Hunan, Changde, China.
Peng CaoJiangsu Provincial Medical Innovation Center, The Affiliated Hospital of Integrated Chinese and Western Medicine, Nanjing University of Chinese Medicine, Jiangsu, Nanjing, China. cao_peng@njmu.edu.cn.ORCID http://orcid.org/0000-0002-2044-3074
Erguang LiState Key Laboratory of Pharmaceutical Biotechnology, Medical School, Nanjing University, Jiangsu, 210093, Nanjing, China. erguang@nju.edu.cn.ORCID http://orcid.org/0000-0002-3065-1336

Funding

National Key R&D Program of China 2023YFC2308200National Natural Science Foundation of China 81871636
6 · The paper itself

Abstract

backgroundThe RNA-binding protein polypyrimidine tract-binding protein 1 (PTBP1), also known as heterogeneous nuclear ribonucleoprotein I (hnRNP I), mediates gene expression through splicing regulation. Its role in virus infection is undefined.

resultsWe show that genetic ablation of PTBP1 renders cell resistant to herpes simplex virus 1 (HSV-1) infection. HSV-1 utilizes 3-O-sulfated heparan sulfate proteoglycans (HSPGs) for attachment and for infection of epithelial cells. We found that knockout of PTBP1 expression resulted in loss of HS3ST3A1 and HS3ST3B1, heparan sulfate glucosaminyl 3-O-sulfotransferase genes for 3-O-sulfation of the heparan sulfate (HS) chains of HSPGs. Each of the HS3ST3A1/HS3ST3B1 genes is composed of 2 exons separated by an extraordinarily long intron whose removal requires PTBP1-associated looping. We found that PTBP1 interacted with the intronic region of HS3ST3A1/HS3ST3B1 pre-mRNAs and modulated their processing to mRNA. The essential role of PTBP1 in functional HS3ST3A1 expression and in HSV-1 infection was demonstrated by ectopic re-expression in the knockout (ko) cells. In addition, we showed that targeting PTBP1 expression by microRNA mimics reduced disease symptoms in a mouse herpetic stromal keratitis (HSK) model.

conclusionsThe results demonstrate that PTBP1 mediates HSV-1 infection of epithelial cells through splicing regulation of HS3ST3A1/HS3ST3B1. These studies provide a new area for novel therapeutic strategies through splicing regulation.

Indexed as

agomiR-124Alternative splicingHerpes simplex virus 1hnRNP IHS3ST3A1

Identifiers

PMID41267098
PMCPMC12632113

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.