Strain-dependent neutralization reveals antigenic variation of human parechovirus 3

Eveliina Karelehto; Sabine van der Sanden; James A. Geraets; Aušra Domanska; Lonneke van der Linden; Dionne Hoogendoorn; Gerrit Koen; Hetty van Eijk; Shabih Shakeel; Tim Beaumont; Menno de Jong; Dasja Pajkrt; Sarah J. Butcher; Katja C. Wolthers

doi:https://doi.org/10.1038/s41598-017-12458-5

Strain-dependent neutralization reveals antigenic variation of human parechovirus 3

Eveliina Karelehto, Sabine van der Sanden, James A. Geraets, Aušra Domanska, Lonneke van der Linden, Dionne Hoogendoorn, Gerrit Koen, Hetty van Eijk, Shabih Shakeel, Tim Beaumont, Menno de Jong, Dasja Pajkrt, Sarah J. Butcher, Katja C. Wolthers

Research output: Contribution to journal › Article › Academic › peer-review

17 Citations (Scopus)

Abstract

Human parechovirus 3 (HPeV3), a member of the Picornavirus family, is frequently detected worldwide. However, the observed seropositivity rates for HPeV3 neutralizing antibodies (nAbs) vary from high in Japan to low in the Netherlands and Finland. To study if this can be explained by technical differences or antigenic diversity among HPeV3 strains included in the serological studies, we determined the neutralizing activity of Japanese and Dutch intravenous immunoglobulin batches (IVIG), a rabbit HPeV3 hyperimmune polyclonal serum, and a human HPeV3-specific monoclonal antibody (mAb) AT12-015, against the HPeV3 A308/99 prototype strain and clinical isolates from Japan, the Netherlands and Australia, collected between 1989 and 2015. The rabbit antiserum neutralized all HPeV3 isolates whereas the neutralization capacity of the IVIG batches varied, and the mAb exclusively neutralized the A308/99 strain. Mapping of the amino acid variation among a subset of the HPeV3 strains on an HPeV3 capsid structure revealed that the majority of the surface-exposed amino acid variation was located in the VP1. Furthermore, amino acid mutations in a mAb AT12-015-resistant HPeV3 A308/99 variant indicated the location for potential antigenic determinants. Virus aggregation and the observed antigenic diversity in HPeV3 can explain the varying levels of nAb seropositivity reported in previous studies

Original language	English
Pages (from-to)	12075
Journal	Scientific reports
Volume	7
Issue number	1
DOIs	https://doi.org/10.1038/s41598-017-12458-5
Publication status	Published - 2017

Access to Document

https://doi.org/10.1038/s41598-017-12458-5

Cite this

Karelehto, E., van der Sanden, S., Geraets, J. A., Domanska, A., van der Linden, L., Hoogendoorn, D., Koen, G., van Eijk, H., Shakeel, S., Beaumont, T., de Jong, M., Pajkrt, D., Butcher, S. J., & Wolthers, K. C. (2017). Strain-dependent neutralization reveals antigenic variation of human parechovirus 3. Scientific reports, 7(1), 12075. https://doi.org/10.1038/s41598-017-12458-5

@article{2b2b3a4bd0a041a29f6c5a9a50b45be9,

title = "Strain-dependent neutralization reveals antigenic variation of human parechovirus 3",

abstract = "Human parechovirus 3 (HPeV3), a member of the Picornavirus family, is frequently detected worldwide. However, the observed seropositivity rates for HPeV3 neutralizing antibodies (nAbs) vary from high in Japan to low in the Netherlands and Finland. To study if this can be explained by technical differences or antigenic diversity among HPeV3 strains included in the serological studies, we determined the neutralizing activity of Japanese and Dutch intravenous immunoglobulin batches (IVIG), a rabbit HPeV3 hyperimmune polyclonal serum, and a human HPeV3-specific monoclonal antibody (mAb) AT12-015, against the HPeV3 A308/99 prototype strain and clinical isolates from Japan, the Netherlands and Australia, collected between 1989 and 2015. The rabbit antiserum neutralized all HPeV3 isolates whereas the neutralization capacity of the IVIG batches varied, and the mAb exclusively neutralized the A308/99 strain. Mapping of the amino acid variation among a subset of the HPeV3 strains on an HPeV3 capsid structure revealed that the majority of the surface-exposed amino acid variation was located in the VP1. Furthermore, amino acid mutations in a mAb AT12-015-resistant HPeV3 A308/99 variant indicated the location for potential antigenic determinants. Virus aggregation and the observed antigenic diversity in HPeV3 can explain the varying levels of nAb seropositivity reported in previous studies",

author = "Eveliina Karelehto and {van der Sanden}, Sabine and Geraets, {James A.} and Au{\v s}ra Domanska and {van der Linden}, Lonneke and Dionne Hoogendoorn and Gerrit Koen and {van Eijk}, Hetty and Shabih Shakeel and Tim Beaumont and {de Jong}, Menno and Dasja Pajkrt and Butcher, {Sarah J.} and Wolthers, {Katja C.}",

year = "2017",

doi = "https://doi.org/10.1038/s41598-017-12458-5",

language = "English",

volume = "7",

pages = "12075",

journal = "Scientific reports",

issn = "2045-2322",

publisher = "Springer Nature",

number = "1",

}

Karelehto, E, van der Sanden, S, Geraets, JA, Domanska, A, van der Linden, L, Hoogendoorn, D, Koen, G, van Eijk, H, Shakeel, S, Beaumont, T , de Jong, M , Pajkrt, D, Butcher, SJ & Wolthers, KC 2017, 'Strain-dependent neutralization reveals antigenic variation of human parechovirus 3', Scientific reports, vol. 7, no. 1, pp. 12075. https://doi.org/10.1038/s41598-017-12458-5

TY - JOUR

T1 - Strain-dependent neutralization reveals antigenic variation of human parechovirus 3

AU - Karelehto, Eveliina

AU - van der Sanden, Sabine

AU - Geraets, James A.

AU - Domanska, Aušra

AU - van der Linden, Lonneke

AU - Hoogendoorn, Dionne

AU - Koen, Gerrit

AU - van Eijk, Hetty

AU - Shakeel, Shabih

AU - Beaumont, Tim

AU - de Jong, Menno

AU - Pajkrt, Dasja

AU - Butcher, Sarah J.

AU - Wolthers, Katja C.

PY - 2017

Y1 - 2017

N2 - Human parechovirus 3 (HPeV3), a member of the Picornavirus family, is frequently detected worldwide. However, the observed seropositivity rates for HPeV3 neutralizing antibodies (nAbs) vary from high in Japan to low in the Netherlands and Finland. To study if this can be explained by technical differences or antigenic diversity among HPeV3 strains included in the serological studies, we determined the neutralizing activity of Japanese and Dutch intravenous immunoglobulin batches (IVIG), a rabbit HPeV3 hyperimmune polyclonal serum, and a human HPeV3-specific monoclonal antibody (mAb) AT12-015, against the HPeV3 A308/99 prototype strain and clinical isolates from Japan, the Netherlands and Australia, collected between 1989 and 2015. The rabbit antiserum neutralized all HPeV3 isolates whereas the neutralization capacity of the IVIG batches varied, and the mAb exclusively neutralized the A308/99 strain. Mapping of the amino acid variation among a subset of the HPeV3 strains on an HPeV3 capsid structure revealed that the majority of the surface-exposed amino acid variation was located in the VP1. Furthermore, amino acid mutations in a mAb AT12-015-resistant HPeV3 A308/99 variant indicated the location for potential antigenic determinants. Virus aggregation and the observed antigenic diversity in HPeV3 can explain the varying levels of nAb seropositivity reported in previous studies

AB - Human parechovirus 3 (HPeV3), a member of the Picornavirus family, is frequently detected worldwide. However, the observed seropositivity rates for HPeV3 neutralizing antibodies (nAbs) vary from high in Japan to low in the Netherlands and Finland. To study if this can be explained by technical differences or antigenic diversity among HPeV3 strains included in the serological studies, we determined the neutralizing activity of Japanese and Dutch intravenous immunoglobulin batches (IVIG), a rabbit HPeV3 hyperimmune polyclonal serum, and a human HPeV3-specific monoclonal antibody (mAb) AT12-015, against the HPeV3 A308/99 prototype strain and clinical isolates from Japan, the Netherlands and Australia, collected between 1989 and 2015. The rabbit antiserum neutralized all HPeV3 isolates whereas the neutralization capacity of the IVIG batches varied, and the mAb exclusively neutralized the A308/99 strain. Mapping of the amino acid variation among a subset of the HPeV3 strains on an HPeV3 capsid structure revealed that the majority of the surface-exposed amino acid variation was located in the VP1. Furthermore, amino acid mutations in a mAb AT12-015-resistant HPeV3 A308/99 variant indicated the location for potential antigenic determinants. Virus aggregation and the observed antigenic diversity in HPeV3 can explain the varying levels of nAb seropositivity reported in previous studies

U2 - https://doi.org/10.1038/s41598-017-12458-5

DO - https://doi.org/10.1038/s41598-017-12458-5

M3 - Article

C2 - 28935894

SN - 2045-2322

VL - 7

SP - 12075

JO - Scientific reports

JF - Scientific reports

IS - 1

ER -