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

Bolin, Steven R.; Moennig, V.; Gourley, N. E. K.; Ridpath, Julia F.

doi:10.1007/bf01311029

Cited by 130 publications

(84 citation statements)

References 16 publications

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“…As the M r of the doublet corresponds with that of the E1 protein, as determined by Enzmann & Weiland (1978), and because eight of the above 13 MAbs neutralize HCV strain Brescia, we conclude that the gp54-gp51 doublet is the envelope protein E1 of HCV strain Brescia. Protein E1 of strains Brescia and Alfort had identical M r values, but E1 of strain C had a slightly higher Mr. BVDV is reportedly neutralized by MAbs directed against a 53K to 55K glycoprotein (Magar et al, 1988), against a heterogeneous 56K glycoprotein (Bolin et al, 1988), and against a 56K to 58K glycoprotein (Donis et al, 1988). Thus, we can safely conclude that E1 of the pestiviruses is heterogeneous, has an Mr of approximately 51K to 58K, and induces neutralizing antibodies.…”

Section: Discussionmentioning

confidence: 83%

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

Wensvoort¹,

Boonstra²,

Bodzinga³

1990

Journal of General Virology

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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.

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Section: Discussionmentioning

confidence: 83%

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

Wensvoort¹,

Boonstra²,

Bodzinga³

1990

Journal of General Virology

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“…The boundaries of the structural proteins have been directly determined by N-terminal sequencing Stark et al, 1993 ;Elbers et al, 1996). Two of the envelope proteins, namely E rns and E2, are capable of inducing neutralizing antibodies (Bolin et al, 1988 ;Donis et al, 1988 ;Wensvoort et al, 1989 ;Corapi et al, 1990 ;Greiser-Wilke et al, 1990 ;Weiland et al, 1990Weiland et al, , 1992.…”

Section: Introductionmentioning

confidence: 99%

Localization of pestiviral envelope proteins E(rns) and E2 at the cell surface and on isolated particles.

Weiland

Unger

et al. 1999

Journal of General Virology

100

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The glycoproteins E rns of classical swine fever virus (CSFV) and E rns and E2 of bovine viral diarrhoea virus (BVDV) are shown to be located at the surface of infected cells by the use of indirect immunofluorescence and by cytofluorometric analysis. The positive immunostaining of the cell surface was further analysed by immunogold electron microscopy and it could be shown that only extracellular virions were labelled. Gold granules were not seen at the cellular plasma membrane. In contrast to BVDV E2, the CSFV E2 of virions sticking to the plasma membrane was not accessible to the respective monoclonal antibodies. However, CSFV particles isolated from culture supernatant were able to bind both monoclonal anti-E rns and anti-E2 antibodies. For CSFV and BVDV, binding of anti-E rns antibodies to the virions was more pronounced than that of anti-E2. This finding was unexpected since E2 is considered to be the immunodominant glycoprotein.

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“…The isolation and initial characterization of MAbs BVD/C 12, BVD/C16 and BVD/C38 (Peters et al, 1986;Greiser-Wilke et al, 1991) and BVD/CA3 (Bolin et al, 1988) have been described. MAbs BVD/C42 and BVD/C46 were generated using the same method (Peters et al, 1986).…”

mentioning

confidence: 99%

Immunofluorescence Studies of Biotype-Specific Expression of Bovine Viral Diarrhoea Virus Epitopes in Infected Cells

Greiser‐Wilke¹,

Dittmar

Ließ³

et al. 1991

Journal of General Virology

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

Abstract: Isolates of bovine viral diarrhea (BVD) virus were differentiated by monoclonal antibodies (MoAbs) reactive with the 56 kD viral polypeptide. Patterns of neutralizing activity of the MoAbs indicate that multiple epitopes are involved in virus neutralization.

Cited by 130 publications

References 16 publications

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

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

Localization of pestiviral envelope proteins E(rns) and E2 at the cell surface and on isolated particles.

Immunofluorescence Studies of Biotype-Specific Expression of Bovine Viral Diarrhoea Virus Epitopes in Infected Cells

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