Identifying Epstein–Barr virus peptide sequences associated with differential IgG antibody response. (January 2022)

• Record Type: Journal Article
• Authors: Coghill, Anna E.; Fang, Jianwen; Liu, Zhiwei; Chen, Chien-Jen; Jarrett, Ruth F.; Hjalgrim, Henrik; Proietti, Carla; Yu, Kelly J.; Hsu, Wan-Lun; Lou, Pei-Jen; Wang, Chen-Ping; Zhao, Yingdong; Doolan, Denise L.; Hildesheim, Allan
• Is Part Of: International journal of infectious diseases. Volume 114(2022)
• Page Start: 65
• Page End: 71
• Publication Date: 2022-01
• Subjects: Epstein–Barr virus -- IgG antibody array -- LMP1/2 -- EBNA protein; Communicable diseases -- Periodicals; Communicable Diseases -- Periodicals; Communicable diseases; Periodicals; Electronic journals; 616.9
• DOI: 10.1016/j.ijid.2021.10.054
• Languages: English
• ISSNs: 1201-9712

Abstract

Highlights: This study is the largest serological survey of the anti-Epstein–Barr virus (EBV) peptide immunoglobulin G (IgG) antibody response. Three EBV proteins with one segment associated with the IgG response were identified. Five EBV proteins with amino acid changes associated with the IgG response were identified. The inclusion of geographically distinct populations increases the relevance of this study. ABSTRACT: Background: Epstein–Barr virus (EBV) infection contributes to cancers in a fraction of seropositive individuals, but much remains to be learned about variation in EBV-directed humoral immunity in cancer-free adults. Methods: A protein microarray was used to probe serum from 175 Taiwanese and 141 Northern European adults for immunoglobulin G (IgG) antibody responses to 115 different peptide sequences, representing protein segments or protein variants, from 45 EBV proteins. It was posited that this antibody-based approach could identify EBV peptide sequences representing immunodominant regions relevant for B-cell immunity. Results: Analyses of 45 EBV proteins with multiple protein segments or variants printed on the array identified eight EBV peptide sequences that appear to play a role in immunogenicity. This included: (1) three proteins with segments/regions associated with IgG reactivity (BALF5, LMP1, LMP2A); and (2) five proteins with sequence variants/amino acid changes associated with IgG reactivity (BDLF4, EBNA3A, EBNA3B, EBNA-LP, LF1). Conclusion: This examination of IgG antibody responses against 115 EBV peptide sequences in 316 cancer-free adults represents an important step toward identifying specific EBV protein sequences that play a role in generating B-cell immunity in humans.