Detection of three polypeptides in preparations of bovine viral diarrhoea virus

Matthaeus, W.

doi:10.1007/bf01317470

Cited by 28 publications

(15 citation statements)

References 16 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The genome of BVDV has been shown to be single stranded RIgA of positive polarity (6) although its size has been estimated as either 8.2 kb (19) or 12.5 kb (21). There have also been conflicting reports on the number and size of the virion proteins and virus encoded intraeellular polypeptides (4,15,18,20).…”

Section: Introductionmentioning

confidence: 98%

Variation in the intracellular polypeptide profiles from different isolates of bovine virus diarrhoea virus

Pocock¹,

Howard²,

Clarke³

et al. 1987

Archives of Virology

106

View full text Add to dashboard Cite

Variation of the intracellular polypeptides induced in calf testis cells by 5 cloned isolates of bovine virus diarrhoea virus (BVDV) was examined. Three of the isolates were cytopathic (NADL, C 2415 and Pe 515 c) and two were non-cytopathic (C 1226 and Pe 515 nc) in these cells. The isolates Pe 515 c and Pe 515 nc were both isolated from an animal with clinical signs of mucosal disease. In cells infected with NADL, 8 virus specific proteins (vp 1 to vp 8) with molecular weights ranging from 120,000 (vp 1) to 23,000 (vp 8) were detected. Isolates C 2415 and Pe 515 c gave a similar array of polypeptides to NADL, but the 3 cytopathic isolates could be distinguished by the variation in the molecular weights of some of the proteins. The non-cytopathic isolates could also be distinguished from each other by this type of molecular variation; however, one feature that characterised these strains, when compared to the cytopathic isolates, was the absence of vp 2. Comparison of the polypeptides induced by Pe 515 c and Pe 515 nc showed that apart from the lack of vp 2 in the Pe 515 nc virus profile, the molecular weights of the other viral proteins were similar. This supports serological evidence that for mucosal disease to occur the pair of cytopathic and non-cytopathic viruses must be closely related. Four of the polypeptides induced by Pe 515 c were shown to be glycoproteins.

show abstract

Section: Introductionmentioning

confidence: 98%

Variation in the intracellular polypeptide profiles from different isolates of bovine virus diarrhoea virus

Pocock¹,

Howard²,

Clarke³

et al. 1987

Archives of Virology

106

View full text Add to dashboard Cite

show abstract

“…At least three structural proteins are thought to be involved : two envelope glycoproteins with Mr values of 55 000 (55K) and 46000 (46K) and a non-glycosylated core protein with an Mr of 36000 (36K) were identified for HCV (Enzmann & Weiland,t978). Similar proteins have been identified as structural proteins of BVDV (Matthaeus, 1979). The three structural proteins of the pestiviruses have been tentatively named E1 (55K to 57K), E2 (44K to 46K), and C (34K to 36K) (Westaway et al, 1985 a); however, full evidence that these proteins are indeed the two envelope proteins and the one nucleocapsid protein has never been presented.…”

Section: Introductionmentioning

confidence: 99%

Immunoaffinity purification and characterization of the envelope protein E1 of hog cholera virus

Wensvoort¹,

Boonstra²,

Bodzinga³

1990

Journal of General Virology

View full text Add to dashboard Cite

The envelope protein E1 of hog cholera virus (HCV) was isolated by immunoaffinity purification with monoclonal antibodies (MAbs) directed against HCV. E1 consisted of a doublet of glycoproteins which varied in size from 51K to 56K between the three strains tested. E1 contains major antigenic determinants of HCV which are conserved, and are involved in neutralization by MAbs. In infected ceils, E 1 was found always connected with a glycoprotein of 31K. When Nlinked glycans were removed, E1 had a polypeptide backbone of approximately 47K. After proteolytic cleavage of E1 with Staphylococcus protease V8 and after electrophoresis and electrotransfer, peptide fragments containing different antigenic domains of E1 were detected with MAbs directed against HCV.

show abstract

“…Those antibodies only neutralize certain BVD viruses and precipitate a polypeptide of approximately 56 kD (Bolin, in press). There is a general agreement that the 56 kD polypeptide is glycosylated and a component of the viral envelope [5,16,19]. Thus, antiserum from persistently infected cattle detects significant antigenic variation among BVD viruses in epitopes involved with neutralization and, considering the relatively large size of the viral structural protein involved, there is a possibility of several epitopes associated with antibody induced neutralization.…”

mentioning

confidence: 97%

Monoclonal antibodies with neutralizing activity segregate isolates of bovine viral diarrhea virus into groups

Bolin

Moennig

Gourley

et al. 1988

Archives of Virology

130

View full text Add to dashboard Cite

show abstract

Detection of three polypeptides in preparations of bovine viral diarrhoea virus

Cited by 28 publications

References 16 publications

Variation in the intracellular polypeptide profiles from different isolates of bovine virus diarrhoea virus

Variation in the intracellular polypeptide profiles from different isolates of bovine virus diarrhoea virus

Immunoaffinity purification and characterization of the envelope protein E1 of hog cholera virus

Monoclonal antibodies with neutralizing activity segregate isolates of bovine viral diarrhea virus into groups

Contact Info

Product

Resources

About