Identifying Epstein–Barr virus peptide sequences associated with differential IgG antibody response

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;Hildesheim, Allan

Carla Proietti Denise Doolan

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.

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International Journal of Infectious Diseases

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114

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1878-3511

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Elsevier

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DOI

10.1016/j.ijid.2021.10.054