Identifying Epstein-Barr virus peptide sequences associated with differential IgG antibody response
Journal
International Journal of Infectious Diseases
Journal Volume
114
Pages
65-71
Date Issued
2022
Author(s)
Coghill A.E.
Fang J.
Liu Z.
Chen C.-J.
Jarrett R.F.
Hjalgrim H.
Proietti C.
Yu K.J.
Hsu W.-L.
Wang C.-P.
Zhao Y.
Doolan D.L.
Hildesheim A.
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.
SDGs
Publisher
Elsevier B.V.
Type
journal article