Serologic and molecular comparisons of several equine herpesvirus type 1 strains.
Abstract: The molecular and serologic relatedness of 2 recent respiratory tract isolates of equine herpesvirus type 1, designated T1 and T2, were compared with the Army 183, Kentucky-A hamster-adapted (KyA-ha), and L-M cell-adapted (KyA-LM) strains. Electrophoresis in polyacrylamide gels revealed differences in virion structural proteins among 4 purified strains. Seven envelope glycoproteins (molecular weight of 93,000, 65,000, 62,000, 60,000, 36,000, 20,000, and 18,000) corresponding to virion proteins 13, 16, 17, 18, 23, 25, and 26a, respectively, found in both the Army 183 and KyA-ha strains had slightly different molecular weight counterparts in both the T1 and T2 isolates, which had identical structural protein profiles. virion protein 19 (58,000 daltons), a nonglycosylated protein, was present in reduced amounts in the respiratory tract isolates, whereas virion protein 8a (200,000 daltons) was absent. Virion protein 8a, an envelope glycoprotein, was only present in the KyA-ha strain. The T1 and T2 isolates were not neutralized by equine herpesvirus type 2 antiserum and revealed little cross-neutralizatio with the Army 183 and KyA-ha strains in plaque-reduction neutralization tests. Restriction endonuclease cleavage maps of viral DNA revealed a similar, but not identical, number and size of DNA fragments between T1 and T2 isolates. Likewise, DNa profiles of Army 183, KyA-ha, and KyA-LM were also similar to each other, but vastly different from the respiratory tract isolates.
Publication Date: 1981-12-01 PubMed ID: 6280520
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- Comparative Study
- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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This study analyzes the molecular and serologic characteristics of two new strains of equine herpesvirus type 1, labeled T1 and T2, and compares them with three other previously known strains. It outlines the differences in virion structural proteins and how these strains react to equine herpesvirus type 2 antiserum and neutralization tests.
Molecular and Serologic Comparisons
- The study compares two recent respiratory isolates, T1 and T2 of equine herpesvirus type 1, with the Army 183, KyA-ha, and KyA-LM strains that are previously known.
- These comparisons are made based on molecular structures and serologic analysis, with the objective of uncovering potential differences and similarities.
Findings in Virion Structural Proteins
- During electrophoresis in polyacrylamide gels, differences in virion’s (a virus particle) structural proteins among the strains were noticed.
- In the Army 183 and KyA-ha strains, seven envelope glycoproteins were identified; these proteins matched slightly different molecular weight versions in the T1 and T2 isolates, which demonstrated identical structural protein profiles.
Difference in Protein Presence
- Virion protein 19, a non-glycosylated protein, was found to be present in reduced amounts in the T1 and T2 strains.
- Virion protein 8a was absent entirely, but it was present in the KyA-ha strain.
Reactions with Antiserum and Neurotization Tests
- In assays using equine herpesvirus type 2 antiserum, the T1 and T2 isolates did not show any neutralization, suggesting a varied immune response.
- The T1 and T2 strains also showed reduced cross-neutralization with the Army 183 and KyA-ha strains during the plaque-reduction neutralization tests, indicating differences in viral characteristics.
Restriction Endonuclease Analysis
- Restriction endonuclease mapping, a method used to identify and map locations of specific bases in DNA, was used to find similar but not identical numbers and sizes of DNA fragments between T1 and T2 viruses.
- Comparison of these maps also revealed that profiles of Army 183, KyA-ha, and KyA-LM strains were similar to each other, but these were very different from those of the novel respiratory tract isolates (T1 and T2).
Cite This Article
APA
Turtinen LW, Allen GP, Darlington RW, Bryans JT.
(1981).
Serologic and molecular comparisons of several equine herpesvirus type 1 strains.
Am J Vet Res, 42(12), 2099-2104.
Publication
Researcher Affiliations
MeSH Terms
- Animals
- Antigens, Viral / immunology
- Cricetinae / embryology
- Glycoproteins / analysis
- Herpesviridae / analysis
- Herpesviridae Infections / microbiology
- Herpesviridae Infections / veterinary
- Herpesvirus 1, Equid / analysis
- Herpesvirus 1, Equid / immunology
- Herpesvirus 1, Equid / isolation & purification
- Horse Diseases / microbiology
- Horses
- Liver / microbiology
- Nasal Mucosa / microbiology
- Neutralization Tests
- Peptides / analysis
- Protein Conformation
- Viral Proteins / analysis
Citations
This article has been cited 17 times.- Oladunni FS, Horohov DW, Chambers TM. EHV-1: A Constant Threat to the Horse Industry.. Front Microbiol 2019;10:2668.
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