Evidence map›Paper›PMID 38995916›Full record

ArticlePloS one2024

Antibody reactions of horses against various domains of the EHV-1 receptor-binding protein gD1.

Andreina Schramm, Mathias Ackermann, Catherine Eichwald, Claudio Aguilar, Cornel Fraefel, Julia Lechmann

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Article in PloS one, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

6 authors.

Andreina SchrammInstitute of Virology, Vetsuisse Faculty, University of Zurich, Zurich, Switzerland.
Mathias AckermannInstitute of Virology, Vetsuisse Faculty, University of Zurich, Zurich, Switzerland.ORCID 0000-0001-5268-1467
Catherine EichwaldInstitute of Virology, Vetsuisse Faculty, University of Zurich, Zurich, Switzerland.ORCID 0000-0003-0001-4843
Claudio AguilarInstitute of Virology, Vetsuisse Faculty, University of Zurich, Zurich, Switzerland.
Cornel FraefelInstitute of Virology, Vetsuisse Faculty, University of Zurich, Zurich, Switzerland.ORCID 0000-0001-7221-6706
Julia LechmannInstitute of Virology, Vetsuisse Faculty, University of Zurich, Zurich, Switzerland.ORCID 0000-0002-7389-846X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Equid alphaherpesviruses 1 (EHV-1) and 4 (EHV-4) are closely related and both endemic in horses worldwide. Both viruses replicate in the upper respiratory tract, but EHV-1 may additionally lead to abortion and equine herpesvirus myeloencephalopathy (EHM). We focused on antibody responses in horses against the receptor-binding glycoprotein D of EHV-1 (gD1), which shares a 77% amino acid identity with its counterpart in EHV-4 (gD4). Both antigens give rise to cross-reacting antibodies, including neutralizing antibodies. However, immunity against EHV-4 is not considered protective against EHM. While a diagnostic ELISA to discriminate between EHV-1 and EHV-4 infections is available based on type-specific fragments of glycoprotein G (gG1 and gG4, respectively), the type-specific antibody reaction against gD1 has not yet been sufficiently addressed. Starting from the N-terminus of gD1, we developed luciferase immunoprecipitation system (LIPS) assays, using gD1-fragments of increasing size as antigens, i.e. gD1_83 (comprising the first 83 amino acids), gD1_160, gD1_180, and gD1_402 (the full-length molecule). These assays were then used to analyse panels of horse sera from Switzerland (n = 60) and Iceland (n = 50), the latter of which is considered EHV-1 free. We detected only one true negative horse serum from Iceland, whereas all other sera in both panels were seropositive for both gG4 (ELISA) and gD1 (LIPS against gD1_402). In contrast, seropositivity against gG1 was rather rare (35% Swiss sera; 14% Icelandic sera). Therefore, a high percentage of antibodies against gD1 could be attributed to cross-reaction and due to EHV-4 infections. In contrast, the gD1_83 fragment was able to identify sera with type-specific antibodies against gD1. Interestingly, those sera stemmed almost exclusively from vaccinated horses. Although it is uncertain that the N-terminal epitopes of gD1 addressed in this communication are linked to better protection, we suggest that in future vaccine developments, type-common antigens should be avoided, while a broad range of type-specific antigens should be favored.

Indexed as

Antibodies, ViralHerpesvirus 1, EquidHorse DiseasesViral Envelope ProteinsAnimalsAntibodies, NeutralizingCross ReactionsEnzyme-Linked Immunosorbent AssayHerpesviridae InfectionsHerpesvirus 4, EquidHorsesProtein DomainsAntibodies, NeutralizingAntibodies, Viralglycoprotein D, Equid herpesvirus 1Viral Envelope Proteins

Identifiers

PMID38995916
PMCPMC11244823

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.