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

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...

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Autores principales: Anna E. Coghill, Jianwen Fang, Zhiwei Liu, Chien-Jen Chen, Ruth F. Jarrett, Henrik Hjalgrim, Carla Proietti, Kelly J. Yu, Wan-Lun Hsu, Pei-Jen Lou, Chen-Ping Wang, Yingdong Zhao, Denise L. Doolan, Allan Hildesheim
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Publicado: Elsevier 2022
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Acceso en línea:https://doaj.org/article/bb033c0992f74958a4dbcc75d7993452
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spelling oai:doaj.org-article:bb033c0992f74958a4dbcc75d79934522021-11-26T04:24:33ZIdentifying Epstein–Barr virus peptide sequences associated with differential IgG antibody response1201-971210.1016/j.ijid.2021.10.054https://doaj.org/article/bb033c0992f74958a4dbcc75d79934522022-01-01T00:00:00Zhttp://www.sciencedirect.com/science/article/pii/S1201971221008420https://doaj.org/toc/1201-9712ABSTRACT: 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.Anna E. CoghillJianwen FangZhiwei LiuChien-Jen ChenRuth F. JarrettHenrik HjalgrimCarla ProiettiKelly J. YuWan-Lun HsuPei-Jen LouChen-Ping WangYingdong ZhaoDenise L. DoolanAllan HildesheimElsevierarticleEpstein–Barr virusIgG antibody arrayLMP1/2EBNA proteinInfectious and parasitic diseasesRC109-216ENInternational Journal of Infectious Diseases, Vol 114, Iss , Pp 65-71 (2022)
institution DOAJ
collection DOAJ
language EN
topic Epstein–Barr virus
IgG antibody array
LMP1/2
EBNA protein
Infectious and parasitic diseases
RC109-216
spellingShingle Epstein–Barr virus
IgG antibody array
LMP1/2
EBNA protein
Infectious and parasitic diseases
RC109-216
Anna E. Coghill
Jianwen Fang
Zhiwei Liu
Chien-Jen Chen
Ruth F. Jarrett
Henrik Hjalgrim
Carla Proietti
Kelly J. Yu
Wan-Lun Hsu
Pei-Jen Lou
Chen-Ping Wang
Yingdong Zhao
Denise L. Doolan
Allan Hildesheim
Identifying Epstein–Barr virus peptide sequences associated with differential IgG antibody response
description 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.
format article
author Anna E. Coghill
Jianwen Fang
Zhiwei Liu
Chien-Jen Chen
Ruth F. Jarrett
Henrik Hjalgrim
Carla Proietti
Kelly J. Yu
Wan-Lun Hsu
Pei-Jen Lou
Chen-Ping Wang
Yingdong Zhao
Denise L. Doolan
Allan Hildesheim
author_facet Anna E. Coghill
Jianwen Fang
Zhiwei Liu
Chien-Jen Chen
Ruth F. Jarrett
Henrik Hjalgrim
Carla Proietti
Kelly J. Yu
Wan-Lun Hsu
Pei-Jen Lou
Chen-Ping Wang
Yingdong Zhao
Denise L. Doolan
Allan Hildesheim
author_sort Anna E. Coghill
title Identifying Epstein–Barr virus peptide sequences associated with differential IgG antibody response
title_short Identifying Epstein–Barr virus peptide sequences associated with differential IgG antibody response
title_full Identifying Epstein–Barr virus peptide sequences associated with differential IgG antibody response
title_fullStr Identifying Epstein–Barr virus peptide sequences associated with differential IgG antibody response
title_full_unstemmed Identifying Epstein–Barr virus peptide sequences associated with differential IgG antibody response
title_sort identifying epstein–barr virus peptide sequences associated with differential igg antibody response
publisher Elsevier
publishDate 2022
url https://doaj.org/article/bb033c0992f74958a4dbcc75d7993452
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