Evidence map›Paper›PMID 41670831›Full record

ArticleBiotechnology letters2026

Bioinformatic evaluation of ClpP as a vaccine target in Streptococcus pneumoniae.

Yanying Huang, Liyan Zhu, Weihua Li, Shilei Dong

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Article in Biotechnology letters, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

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0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

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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

4 authors.

Yanying HuangDepartment of Pathology, Hangzhou Red Cross Hospital, Hangzhou, 310003, Zhejiang, China.ORCID http://orcid.org/0000-0003-3141-7936
Liyan ZhuDepartment of Pathology, Hangzhou Red Cross Hospital, Hangzhou, 310003, Zhejiang, China.
Weihua LiDepartment of Pathology, Hangzhou Red Cross Hospital, Hangzhou, 310003, Zhejiang, China. raliweihua@126.com.
Shilei DongDepartment of Clinical Laboratory Medicine, Zhejiang Hospital, Hangzhou, 310013, Zhejiang, China. dsl166@126.com.

Funding

Zhejiang Provincial Science and Technology Planning Project for Medicine and Health Care 2025KY543Zhejiang Provincial Science and Technology Planning Project for Medicine and Health Care No. 2023KY971
6 · The paper itself

Abstract

purposeTo conduct a comprehensive bioinformatic analysis to assess the immunogenicity and conservation profiles of ClpP in Streptococcus pneumoniae, thereby verifying its feasibility as a candidate vaccine target.

methodsThe nucleotide and amino acid sequences of the clpP gene were obtained from the NCBI database. The fundamental characterizations of ClpP were retrieved from the public database PneumoWiki. NetPhos was used to predict phosphorylation sites, whereas SOPMA, Swiss-Model and STRING were employed to analyze secondary/tertiary structures and functional interaction network, respectively. Antigenic epitope mapping was carried out using DNASTAR, SYFPEITHI, NetMHCIIpan 4.0 and NetMHC. Multiple sequence alignment (MSA) was performed using Jalview software to analyze the conservation of the predicted epitopes across S. pneumoniae strains. Concurrently, a phylogenetic tree was constructed to evaluate the cross-species conservation of the ClpP protein.

resultsClpP (196 aa, pI 4.74) showed high hydrophobicity and without signal peptides/transmembrane domains. Phosphorylation sites (Ser/Thr/Tyr) were identified. The secondary structure of ClpP consists of 94 α-helices, 37 β-strands and 65 random coils. The functional interaction network of ClpP involves 10 interacting partners. Immunoinformatic analysis further detected immunodominant B-cell and T-cell epitopes within the ClpP sequence.

conclusionTaken together, these data suggest that ClpP exhibits robust immunogenicity and multiple antigenic epitopes, supporting its potential as a peptide-based vaccine candidate against S. pneumoniae.

Indexed as

Bacterial ProteinsComputational BiologyEndopeptidase ClpPneumococcal VaccinesStreptococcus pneumoniaeAmino Acid SequenceEpitope MappingEpitopesImmunoinformaticsPhylogenyProtein Subunit VaccinesSequence AlignmentBacterial ProteinsClpP protein, Streptococcus pneumoniaeEndopeptidase ClpEpitopesPneumococcal VaccinesProtein Subunit VaccinesBioinformatics analysisClpPEpitopesStreptococcus pneumoniaeVaccine

Identifiers

PMID41670831

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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.