{"title":"针对病毒糖蛋白融合前状态的精确疫苗设计:结构疫苗学的进展。","authors":"Reetesh Kumar , Somnath Maji , Savitri Tiwari , Jyotsna Misra , Jyoti Gupta , Naveen Kumar , Rohan Gupta , Niraj Kumar Jha","doi":"10.1016/j.bcp.2025.117349","DOIUrl":null,"url":null,"abstract":"<div><div>The prefusion conformation of viral glycoproteins is a key target for vaccine development because it can induce strong neutralizing antibody responses. Nevertheless, these structures are frequently metastable and susceptible to conformational alterations that diminish immunogenic efficacy. Progress in structural vaccinology has facilitated the meticulous design of viral proteins to maintain their prefusion conformation, thus improving vaccination effectiveness. This study emphasizes essential methodologies in precision vaccine design focused on preserving the structural integrity, solubility, and immunogenicity of viral glycoproteins. Methods include cavity-filling mutations, proline insertions, and disulfide bond engineering have demonstrated efficacy in enhancing structural stiffness and inhibiting unwanted post-fusion rearrangements. Hydrophobic surface residues are frequently substituted with polar or charged residues to boost solubility and minimize aggregation, while the development of salt bridges and helix-stabilizing substitutions further augment heat stability. The removal of proteolytic cleavage sites and the enhancement of hydrophobic core packing facilitate sustained conformational integrity. Alterations to the fusion peptide, an essential conserved area for viral entry, can inhibit early conformational changes, whereas charge-balancing alterations mitigate electrostatic stress. Glycan shielding conceals non-neutralizing or immunodominant epitopes, steering immune reactions towards conserved, protective areas. Collectively, these structure-guided interventions constitute a thorough molecular toolset, facilitating the creation of prefusion-stabilized immunogens for advanced vaccines. Successfully implemented in vaccine candidates for Respiratory Syncytial Virus (RSV), Human Immunodeficiency Virus (HIV), and Severe Acute Respiratory Syndrome Coronavirus-2 (SARS-CoV-2), these methodologies establish a solid basis for the swift and logical generation of vaccines against emerging viral threats.</div></div>","PeriodicalId":8806,"journal":{"name":"Biochemical pharmacology","volume":"242 ","pages":"Article 117349"},"PeriodicalIF":5.6000,"publicationDate":"2025-09-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Precision vaccine design targeting the prefusion state of viral glycoproteins: advances in structural vaccinology\",\"authors\":\"Reetesh Kumar , Somnath Maji , Savitri Tiwari , Jyotsna Misra , Jyoti Gupta , Naveen Kumar , Rohan Gupta , Niraj Kumar Jha\",\"doi\":\"10.1016/j.bcp.2025.117349\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><div>The prefusion conformation of viral glycoproteins is a key target for vaccine development because it can induce strong neutralizing antibody responses. Nevertheless, these structures are frequently metastable and susceptible to conformational alterations that diminish immunogenic efficacy. Progress in structural vaccinology has facilitated the meticulous design of viral proteins to maintain their prefusion conformation, thus improving vaccination effectiveness. This study emphasizes essential methodologies in precision vaccine design focused on preserving the structural integrity, solubility, and immunogenicity of viral glycoproteins. Methods include cavity-filling mutations, proline insertions, and disulfide bond engineering have demonstrated efficacy in enhancing structural stiffness and inhibiting unwanted post-fusion rearrangements. Hydrophobic surface residues are frequently substituted with polar or charged residues to boost solubility and minimize aggregation, while the development of salt bridges and helix-stabilizing substitutions further augment heat stability. The removal of proteolytic cleavage sites and the enhancement of hydrophobic core packing facilitate sustained conformational integrity. Alterations to the fusion peptide, an essential conserved area for viral entry, can inhibit early conformational changes, whereas charge-balancing alterations mitigate electrostatic stress. Glycan shielding conceals non-neutralizing or immunodominant epitopes, steering immune reactions towards conserved, protective areas. Collectively, these structure-guided interventions constitute a thorough molecular toolset, facilitating the creation of prefusion-stabilized immunogens for advanced vaccines. Successfully implemented in vaccine candidates for Respiratory Syncytial Virus (RSV), Human Immunodeficiency Virus (HIV), and Severe Acute Respiratory Syndrome Coronavirus-2 (SARS-CoV-2), these methodologies establish a solid basis for the swift and logical generation of vaccines against emerging viral threats.</div></div>\",\"PeriodicalId\":8806,\"journal\":{\"name\":\"Biochemical pharmacology\",\"volume\":\"242 \",\"pages\":\"Article 117349\"},\"PeriodicalIF\":5.6000,\"publicationDate\":\"2025-09-17\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochemical pharmacology\",\"FirstCategoryId\":\"3\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0006295225006148\",\"RegionNum\":2,\"RegionCategory\":\"医学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"PHARMACOLOGY & PHARMACY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochemical pharmacology","FirstCategoryId":"3","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0006295225006148","RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"PHARMACOLOGY & PHARMACY","Score":null,"Total":0}
Precision vaccine design targeting the prefusion state of viral glycoproteins: advances in structural vaccinology
The prefusion conformation of viral glycoproteins is a key target for vaccine development because it can induce strong neutralizing antibody responses. Nevertheless, these structures are frequently metastable and susceptible to conformational alterations that diminish immunogenic efficacy. Progress in structural vaccinology has facilitated the meticulous design of viral proteins to maintain their prefusion conformation, thus improving vaccination effectiveness. This study emphasizes essential methodologies in precision vaccine design focused on preserving the structural integrity, solubility, and immunogenicity of viral glycoproteins. Methods include cavity-filling mutations, proline insertions, and disulfide bond engineering have demonstrated efficacy in enhancing structural stiffness and inhibiting unwanted post-fusion rearrangements. Hydrophobic surface residues are frequently substituted with polar or charged residues to boost solubility and minimize aggregation, while the development of salt bridges and helix-stabilizing substitutions further augment heat stability. The removal of proteolytic cleavage sites and the enhancement of hydrophobic core packing facilitate sustained conformational integrity. Alterations to the fusion peptide, an essential conserved area for viral entry, can inhibit early conformational changes, whereas charge-balancing alterations mitigate electrostatic stress. Glycan shielding conceals non-neutralizing or immunodominant epitopes, steering immune reactions towards conserved, protective areas. Collectively, these structure-guided interventions constitute a thorough molecular toolset, facilitating the creation of prefusion-stabilized immunogens for advanced vaccines. Successfully implemented in vaccine candidates for Respiratory Syncytial Virus (RSV), Human Immunodeficiency Virus (HIV), and Severe Acute Respiratory Syndrome Coronavirus-2 (SARS-CoV-2), these methodologies establish a solid basis for the swift and logical generation of vaccines against emerging viral threats.
期刊介绍:
Biochemical Pharmacology publishes original research findings, Commentaries and review articles related to the elucidation of cellular and tissue function(s) at the biochemical and molecular levels, the modification of cellular phenotype(s) by genetic, transcriptional/translational or drug/compound-induced modifications, as well as the pharmacodynamics and pharmacokinetics of xenobiotics and drugs, the latter including both small molecules and biologics.
The journal''s target audience includes scientists engaged in the identification and study of the mechanisms of action of xenobiotics, biologics and drugs and in the drug discovery and development process.
All areas of cellular biology and cellular, tissue/organ and whole animal pharmacology fall within the scope of the journal. Drug classes covered include anti-infectives, anti-inflammatory agents, chemotherapeutics, cardiovascular, endocrinological, immunological, metabolic, neurological and psychiatric drugs, as well as research on drug metabolism and kinetics. While medicinal chemistry is a topic of complimentary interest, manuscripts in this area must contain sufficient biological data to characterize pharmacologically the compounds reported. Submissions describing work focused predominately on chemical synthesis and molecular modeling will not be considered for review.
While particular emphasis is placed on reporting the results of molecular and biochemical studies, research involving the use of tissue and animal models of human pathophysiology and toxicology is of interest to the extent that it helps define drug mechanisms of action, safety and efficacy.