Differentiation of Sub‐types of Equine Herpesvirus I by Restriction Endonuclease Analysis

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129

SUMMARYThe genome of an Australian isolate of equine herpesvirus type 1 (equine abortion virus) has been analysed using the restriction endonucleases EcoRI, BglII and BamHI, and a physical map constructed. Terminal fragments were identified by exonuclease treatments, and linkage of fragments was deduced by a combination of single-and double-digest experiments and cross-blot hybridizations. The genome has a mol. wt. of 100 x 10 6 and is comprised of a short unique region bounded by repetitive sequences, which is present in both orientations in approximately equal amounts in the DNA population, and a long unique region existing in only one orientation.

Section: Bamhi/ecori Linkage Mapmentioning

confidence: 99%

Analysis of the Genome of Equine Herpesvirus Type 1: Arrangement of Cleavage Sites for Restriction Endonucleases EcoRI, BglII and BamHI

1981

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129

“…It is also associated with a neurological syndrome, neonatal foal disease and, more rarely, with coital exanthema. The existence of two subtypes of EHV-1 was indicated by serological (Shimizu et al, 1959;Burrows & Goodridge, 1973) and pathogenicity studies (Burrows & Goodridge, 1973), and was confirmed at the genomic level by examination of restriction endonuclease profiles (Sabine et al, 1981 ;Studdert et al, 1981). Both subtypes are respiratory pathogens, but only isolates with subtype 1 restriction endonuclease profiles are commonly associated with abortion.…”

Section: Introductionmentioning

confidence: 99%

Characterization of the Genome of Equine Herpesvirus 1 Subtype 2

Cullinane

Rixon

Davison

1988

SUMMARYThe genome structure of equine herpesvirus 1 (EHV-1) subtype 2 was shown by electron microscopic studies and restriction endonuclease site mapping to comprise two covalently linked segments (L, 109 kbp; S, 35 kbp). The S segment contains a unique sequence (Us) flanked by a substantial inverted repeat (TRs/IRs). Thus, the genome structure of EHV-1 subtype 2 is similar to that published previously for EHV-1 subtype 1, but the two subtypes differ in the occurrences of EcoRI and BamHI restriction sites. Hybridization studies using cloned EHV-1 DNA showed that the genome of EHV-1 subtype 2 is colinear with the genomes of EHV-1 subtype 1 and herpes simplex virus type 1. DNA sequence data for four EHV-1 subtype 2 genes, including one potentially encoding a glycoprotein, were obtained by sequencing a 4574 bp BamHI fragment containing the junction between Us and TRs. The genome structure, hybridization and sequence data confirm that EHV-1 subtype 2 is of the alphaherpesvirus lineage.

“…It has now become clear that there are two distinct subtypes, 1 and 2, demonstrated by restriction endonuclease digestion of purified virus DNA (Sabine et al, 1981 ;Studdert et al, 1981 ;Allen & Turtinen, 1982). EHV-1 subtype 1 is responsible for respiratory disease, abortion and paralysis, whereas the subtype 2 appears to cause only rhinopneumonitis (Allen & Bryans, 1986).…”

Section: Introductionmentioning

confidence: 99%

Identification of the gB Homologues of Equine Herpesvirus Types 1 and 4 as Disulphide-linked Heterodimers and Their Characterization Using Monoclonal Antibodies

Meredith

Stocks

Whittaker

et al. 1989

SUMMARYEquine herpesvirus types 1 and 4 (EHV-1 and EHV-4) labelled with [14C]glucosamine were purified from infected cell culture medium and profiles of their structural proteins were obtained that enabled identification of the major glycoproteins. Nine glycosylated polypeptides were identified for each virus. Preparations of the purified viruses each contained a glycoprotein which was linked by disulphide bonds, as determined by diagonal gel electrophoresis under reducing/non-reducing conditions. High Mr forms of this glycoprotein were detected for EHV-1 when the sample was not heated. The EHV-1 protein consisted of three polypeptides of Mr 108K, 76K and 58K and the EHV-4 protein consisted of three polypeptides of Mr 112K, 74K and 61K. Western blotting and immunoprecipitation with monoclonal antibodies confirmed that the EHV-1 gB homologue migrates with an apparent Mr of 108K (140K under nonreducing conditions) but is cleaved to give glycoproteins of 76K and 58K which are held together by disulphide bonds. The EHV-4 gB homologue consists of a l12K glycoprotein which is cleaved to give glycoproteins of 74K and 61K which are also linked by disulphide bonds.