Identification of envelope and nucleocapsid proteins of infectious bovine rhinotracheitis virus by SDS-polyacrylamide gel electrophoresis

Bolton, David; Zee, Y. C.; Ardans, Alex

doi:10.1016/0378-1135(83)90019-6

Cited by 39 publications

(24 citation statements)

References 9 publications

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“…Bolton et al (1983) showed that if BHV-1 virions are disrupted with the detergent NP40, approximately half of the VP8 protein fractionates with the membranes and the other half fractionates with the nucleocapsids. Marshall et al (1986) confirmed these results with similar experiments but also iodinated the surface proteins of BHV-1 virions.…”

Section: Discussionmentioning

confidence: 99%

The Most Abundant Protein in Bovine Herpes 1 Virions is a Homologue of Herpes Simplex Virus Type 1 UL47

Carpenter

Misra

1991

Journal of General Virology

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The bovine herpesvirus type 1 (BHV-1) protein VP8 is present, in large amounts, in the tegument of virions. As a preliminary step towards determining the function of VP8 and the biological relevance for its abundant presence, we describe the mapping of the location of its gene and determination of its nucleotide sequence. The gene for VP8 was located between 0.088 and 0.108 map units on the BHV-1 genome and contained a 2226 bp reading frame encoding a 742 amino acid protein.The protein, produced in vitro by transcribing and translating the reading frame, was precipitated by monoclonal antibodies and polyclonal serum directed against VP8. The primary structure of VP8 showed considerable homology with the product of the UL47 reading frame of herpes simplex virus type 1.

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Section: Discussionmentioning

confidence: 99%

The Most Abundant Protein in Bovine Herpes 1 Virions is a Homologue of Herpes Simplex Virus Type 1 UL47

Carpenter

Misra

1991

Journal of General Virology

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“…The infected cells were fed with Eagle's minimum essential medium (3/IEM) containing 20 percent of the normal amount of methionine or 50 percent of the normal amount of glucose. The virus was purified by rate-zonal uttraeentrifugation in 10 to 30 percent (w/w) potassium tartrate linear gradients and by isopyenic ultraeent.rifugation in 15 to 45 percent (w/w) potassium tar@ate linear gradients as previously described (2). The protein concentrations were determined by the Bradford (Bio-Rad) protein assay (Bio-Rad Laboratories, I~iehmond, CA.)…”

Section: Labeling and Puri/ieation Of Virusmentioning

confidence: 99%

“…This i n f o r m a t i o n is e s s e n t i a l for t h e d e v e l o p m e n t of f u t u r e s u b u n i t vaccines. P r e v i o u s w o r k d o n e in t h i s l a b o r a t o r y a n d b y o t h e r i n v e s t i g a t o r s h a s i d e n t i f i e d a t l e a s t t h i r t y -t h r e e v i r a l p o l y p e p t i d e s of w h i c h e l e v e n could be l a b e l e d w i t h (3H)-glucosamine a n d are, t h e r e f o r e , g l y c o p r o t e i n s (2,24). A m o n o c l o n M a n t i b o d y to one of t h e s e g l y e o p r o t e i n s w a s s h o w n to b e i n v o l v e d in i m m u n e c y t o l y s i s of i n f e c t e d cells (25).…”

Section: Introductionmentioning

confidence: 98%

Neutralizing monoclonal antibodies directed to infectious bovine rhinotracheitis virus

Chang

Zee

Pritchett

et al. 1986

Archives of Virology

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Infectious bovine rhinotracheitis virus (IBRV) has been shown in this report to have thirty-three polypeptides. Ten of the eleven polypeptides which can be labeled with (3H)-glucosamine are located on the surface of the virus since they can be surface labeled with sodium boro(3H)hydride. In order to define the immunologically important viral proteins, monoclonal antibodies were prepared against the virus and selected for their ability to neutralize infectivity. Four such hybridoma lines were obtained for characterization of the antigens that elicit neutralizing antibodies. The viral polypeptides were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and the specificity of each monoclonal antibody was determined by "Western" blot analysis and/or by immunoprecipitation of (35S)-methionine and (3H)-glucosamine labeled infected cell lysates by the monoclonal antibodies. One monoclonal antibody reacted with two glycoproteins, gp135 and gp78a, on the "Western" blot but immunoprecipitated three glycoproteins, gp135, gp78a, and gp54 from labeled infected cell lysates. The other three monoclonal antibodies immunoprecipitated a single glycoprotein, gp78b, from (3H)-glucosamine labeled infected cell lysates but not from (35S)-methionine labeled infected cell lysates.

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“…Studdert [4] reclassified them as BHV-1.1 (respiratory form), BHV-1.2 (genital form) and BHV-1.3 (encephalitic form). BHV-1 consists of 25-33 polypeptides of which 11 are glycosylated [5][6][7] and associated with virus envelope [5,6]. The three sets of enveloped glycoproteins gI, gIII and gIV were characterized earlier which are involved in the immune response [7][8][9][10][11][12].…”

Section: Introductionmentioning

confidence: 99%

Herpesvirus in Bovines: Importance of Bovine Herpesvirus Type 1

Kaur¹,

Chandra²

2016

Herpesviridae

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The chapter aims at providing readers with the overview of the herpesvirus infection in bovines. It includes the detailed etiology of the infection, discussing the virus characteristics, virus structure, genome, viral proteins, types and subtypes of the virus. Then, the chapter discusses the transmission and pathogenesis of the virus, which are very important as they help to control the virus spread, viral latency and clinical signs observed in the affected animals. Later, the chapter discusses the diagnosis of herpesvirus infection in bovines to help the readers to gain knowledge about the techniques used earlier and nowadays for the diagnosis of the infection. Then, the chapter provides information on the procedures to be adopted for the prevention and control of the infection in bovines. Thus, the chapter provides complete information about the herpesvirus infection in bovines.

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Identification of envelope and nucleocapsid proteins of infectious bovine rhinotracheitis virus by SDS-polyacrylamide gel electrophoresis

Cited by 39 publications

References 9 publications

The Most Abundant Protein in Bovine Herpes 1 Virions is a Homologue of Herpes Simplex Virus Type 1 UL47

The Most Abundant Protein in Bovine Herpes 1 Virions is a Homologue of Herpes Simplex Virus Type 1 UL47

Neutralizing monoclonal antibodies directed to infectious bovine rhinotracheitis virus

Herpesvirus in Bovines: Importance of Bovine Herpesvirus Type 1

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