The use of peptides for deciphering the mechanism of EBV, HPV, and HCV invasion of human cells

Published: March 26, 2025

Epstein-Barr virus (EBV), human papillomavirus (HPV), and hepatitis C (HCV) are significant pathogens associated with various diseases, employing complex molecular mechanisms for cellular entry immune evasion. Peptide-based research, using more than 700 synthetic peptides, has deciphered some of the interactions between viral proteins host cell receptors, offering promising diagnostics therapeutic strategies. In EBV, binding peptides have been identified: 11382, 11389, 11416 derived from gp350/220; 11435, 11436, 11438 gp85 [glycoprotein H (gH)]; 11521 BNRF1/p140. Most these peptide sequences surface-exposed part contact regions making them candidates strategies aimed at inhibiting EBV invasion cells. Peptide 11382 is target neutralizing antibody 72A1; induce interleukin-6 production; 11435 binds to integrin αvβ6, triggers a cytokine storm. HPV L1 protein, major component capsid, 18283 18294 identified as epithelial cell-binding located on surface. Parts recognized by anti-HPV antibodies. These two along 18301, potential biomarkers infection because they antibodies elicited during natural infection, suitable targets serological detection. envelope E1 E2 HCV, five hepatocyte- CD81-positive identified. The contain linear B-cell epitopes antibodies, used develop tests determining HCV infection. approaches can lead innovative prevention, diagnosis, treatment diseases. Additionally, their be modulate response generate tools cancer theragnostic.

Language: Английский

Structure and Antigenicity of Kaposi's Sarcoma‐Associated Herpesvirus Glycoprotein B

Advanced Science, Journal Year: 2025, Volume and Issue: unknown

Published: April 26, 2025

Abstract Kaposi's sarcoma‐associated herpesvirus (KSHV), a member of the human γ‐herpesviruses family, exhibits extensive cellular tropism and is associated with sarcoma various B‐cell malignancies. Despite its clinical significance, no effective prophylactic vaccines or specific therapeutics are currently available to prevent treat KSHV infection. Similar other herpesviruses, depends on envelope glycoprotein B (gB) for host receptor recognition membrane fusion initiation, making gB prime target antiviral antibody vaccine development. In this study, high‐resolution cryo‐electron microscopy (cryo‐EM) structure presented, revealing unique trimeric conformation resembling postfusion state observed in herpesviruses. Additionally, non‐neutralizing monoclonal 2C4 bound domain IV resolved. The comparative sequence analyses reveal significant homology neutralizing epitopes between Epstein‐Barr virus (EBV) gB, indicating potential pathway development broad‐spectrum strategies. These findings provide foundation deeper understanding KSHV's infectious mechanism pave way creation universal interventions against γ‐herpesviruses.

Language: Английский