Synthesis and processing of bovine herpesvirus 1 glycoproteins

Hurk, Sylvia van Drunen Littel‐van den; Babiuk, L A

doi:10.1128/jvi.59.2.401-410.1986

Cited by 107 publications

(47 citation statements)

References 51 publications

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“…7b) to monitor the reactions. According to the enzymes used, the electrophoretic mobilities of virion-associated gD increased as expected (41), and no differences were detected in comparison to the reaction products of immunoprecipitated virion gD (Fig. 7b and c), indicating the presence of sufficient enzymatic activity for complete deglycosylation within the respective probes.…”

Section: Transcription Of the Brsv G Ori And Brsv G Syn Orfs In Recomsupporting

confidence: 70%

The Class II Membrane Glycoprotein G of Bovine Respiratory Syncytial Virus, Expressed from a Synthetic Open Reading Frame, Is Incorporated into Virions of Recombinant Bovine Herpesvirus 1

Kühnle

Heinze

Schmitt

et al. 1998

J Virol

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The bovine herpesvirus 1 (BHV-1) recombinants BHV-1/eG ori and BHV-1/eG syn were isolated after insertion of expression cassettes which contained either a genomic RNA-derived cDNA fragment (BHV-1/eG ori ) or a modified, chemically synthesized open reading frame (ORF) (BHV-1/eG syn ), which both encode the attachment glycoprotein G of bovine respiratory syncytial virus (BRSV), a class II membrane glycoprotein. Northern blot analyses and nuclear runoff transcription experiments indicated that transcripts encompassing the authentic BRSV G ORF were unstable in the nucleus of BHV-1/eG ori -infected cells. In contrast, high levels of BRSV G RNA were detected in BHV-1/eG syn -infected cells. Immunoblots showed that the BHV-1/eG syn -expressed BRSV G glycoprotein contains N-and O-linked carbohydrates and that it is incorporated into the membrane of infected cells and into the envelope of BHV-1/eG syn virions. The latter was also demonstrated by neutralization of BHV-1/eG syn infectivity by monoclonal antibodies or polyclonal anti-BRSV G antisera and complement. Our results show that expression of the BRSV G glycoprotein by BHV-1 was dependent on the modification of the BRSV G ORF and indicate that incorporation of class II membrane glycoproteins into BHV-1 virions does notnecessarily require BHV-1-specific signals. This raises the possibility of targeting heterologous polypeptides to the viral envelope, which might enable the construction of BHV-1 recombinants with new biological properties and the development of improved BHV-1-based live and inactivated vector vaccines.

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Section: Transcription Of the Brsv G Ori And Brsv G Syn Orfs In Recomsupporting

confidence: 70%

The Class II Membrane Glycoprotein G of Bovine Respiratory Syncytial Virus, Expressed from a Synthetic Open Reading Frame, Is Incorporated into Virions of Recombinant Bovine Herpesvirus 1

Kühnle

Heinze

Schmitt

et al. 1998

J Virol

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“…5, panel gIV), indicating that it entered the normal secretory pathway through the Golgi apparatus, where N-linked oligosaccharides on gIV were modified from the high-mannose to the complex type prior to transport of gIV to the cell surface. These results suggest that the gIV produced by recombinant VV (STgIV) is processed in a way similar to that in which gIV is produced during BHV-1 infection (23).…”

Section: Methodsmentioning

confidence: 90%

“…Earlier studies have shown the presence of both N-linked and 0-linked oligosaccharides in gIV (23). In BHV-1-infected cells, N-linked oligosaccharides are processed from high-mannose oligosaccharides present on precursor gIV to complex oligosaccharides of mature gIV, which is transported to the surface of an infected cell and also incorporated into the virion envelope (14,20).…”

Section: Discussionmentioning

confidence: 99%

“…Nucleotide sequence analysis of the BHV-1 gIV-encoding gene predicted that gIV was a typical transmembrane glycoprotein of 417 amino acids (20). The protein contains a signal sequence of 18 amino acids (20) which is cleaved during processing to yield a mature protein of 399 amino acids with a molecular mass of 71 kDa (23). In addition, gIV contains N-linked oligosaccharides (21,23), 0-linked carbohydrates (23), and a hydrophobic transmembrane anchor sequence near the carboxy terminus (20).…”

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confidence: 99%

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Analysis of bovine herpesvirus 1 glycoprotein gIV truncations and deletions expressed by recombinant vaccinia viruses

Tikoo

Zamb

Babiuk

1993

J Virol

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Glycoprotein gIV is an envelope component of bovine herpesvirus type 1 and appears to be involved in attachment, penetration, and cell fusion. Four antigenic domains which include both continuous and discontinuous epitopes have been previously defined by competition binding assays using gIV-specific monoclonal antibodies (MAbs). Here we describe the construction of C-terminal truncations and internal deletions in the gIV-encoding gene and analyses of the effects of these mutations on the synthesis, processing, transport, and antigenicity of glycoprotein glV as expressed by recombinant vaccinia viruses. Wild-type glV expressed by recombinant vaccinia virus STg1V was indistinguishable from authentic glV produced in bovine herpesvirus 1-infected cells with respect to molecular weight, processing, transport, and antigenicity. Analysis of the mutant proteins showed that the binding sites for MAbs 9D6 and 3D9S, which recognize linear epitopes, lie between amino acids 164 and 216 and amino acids 320 and 355, respectively. Discontinuous epitopes recognized by MAbs 3E7, 4C1, 2C8, and 3C1 were located between amino acids 19 and 320, whereas amino acids 320 to 355 were critical for binding of MAb 136. All mutant proteins containing amino acids 245 to 320 were processed, possess endo-13-N-acetylglucosaminidase H-resistant oligosaccharides, and were transported to antigenicity and extent of processing of herpes simplex virus type 1 glycoprotein D.

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“…Glycoprotein gB, gC and gD have been identified as the major immunogens. These are expressed at high levels on the virion envelope and on the plasma membrane of virus infected cells (2). Their biological properties have been reviewed (3).…”

Section: Introductionmentioning

confidence: 99%

Cloning and expression of bovine herpesvirus‐1 glycoprotein C

et al. 1999

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Glycoprotein C (gC) of Bovine Herpesvirus-1 (BHV-1) is expressed at high levels on surface of infected cells ~nd on virus envelope. It is relatively immunodominant in antibody response to BHV-1 infection and protective in immunized bovines against BHV-1 challenge. In an attempt to express gC in mammalian cells, the 2.4 kb BamHI-EcoRI fragment, containing complete coding sequence of the gC gene was excised from a recombinant plasmid and cloned under the control of RSV-LTR. The resultant plasmid pRSV-gC was transfected into MDBK cells and expression of gC was detected by indirect immunofluorescence. The non-permeabilized cells revealed surface expression of gC.

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Synthesis and processing of bovine herpesvirus 1 glycoproteins

Cited by 107 publications

References 51 publications

The Class II Membrane Glycoprotein G of Bovine Respiratory Syncytial Virus, Expressed from a Synthetic Open Reading Frame, Is Incorporated into Virions of Recombinant Bovine Herpesvirus 1

The Class II Membrane Glycoprotein G of Bovine Respiratory Syncytial Virus, Expressed from a Synthetic Open Reading Frame, Is Incorporated into Virions of Recombinant Bovine Herpesvirus 1

Analysis of bovine herpesvirus 1 glycoprotein gIV truncations and deletions expressed by recombinant vaccinia viruses

Cloning and expression of bovine herpesvirus‐1 glycoprotein C

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