Antigenic variants of bovine leukemia virus (BLV) are defined by amino acid substitutions in the NH2 part of the envelope glycoprotein gp51

Portetelle, Daniel; Couez, Dominique; Bruck, Claudine; Kettmann, Richard; Mammerickx, Marc; Maaten, M Van der; Brasseur, Robert; Burny, Arsène

doi:10.1016/0042-6822(89)90037-8

Cited by 52 publications

(63 citation statements)

References 13 publications

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“…Bruck et al (1984a) have demonstrated that the biologically active form of gp51 is dependent upon protein glycosylation. All eight potential glycosylation sites in gp51 are present in the same positions as described for the other BLV variants (Portetelle et al, 1989). The majority of these occur within the two invariant stretches of amino acids described above.…”

Section: Discussionmentioning

confidence: 60%

“…DNA sequence comparisons between BLV variants and differential reactivities of gp51 fragments with monoclonal antibodies suggest that these three epitopes occur within the first 150 amino acids from the amino terminus of the env protein. Seven amino acid changes were detected in this region in the four BLV variants studied by Portetelle et al (1989), whereas the number of changes observed between Australian, Japanese and Belgian isolates was four, demonstrating a high level of amino acid conservation in this biologically important region of the protein. The importance of disulphide bridges in maintaining the native structure of gp51 has been demonstrated (Bruck et al, 1984b).…”

Section: Discussionmentioning

confidence: 98%

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Molecular Cloning and Sequencing of an Australian Isolate of Proviral Bovine Leukaemia Virus DNA: Comparison with other Isolates

Coulston

Naif

Brandon

et al. 1990

Journal of General Virology

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Section: Discussionmentioning

confidence: 60%

Section: Discussionmentioning

confidence: 98%

Molecular Cloning and Sequencing of an Australian Isolate of Proviral Bovine Leukaemia Virus DNA: Comparison with other Isolates

Coulston

Naif

Brandon

et al. 1990

Journal of General Virology

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“…This region (Fig. 1) forms the epitopes F, G, and H (5), which are designated conformational because their recognition by specific monoclonal antibodies depends on disulfide bonding (48) and glycosylation (7). Antibodies from naturally infected cattle also recognize only the glycosylated form of SU, suggesting a specificity for conformation-dependent epitopes in vivo (47).…”

mentioning

confidence: 99%

“…Evidence that the N-terminal half of mature gp51-SU plays an important role in virus infectivity and syncytium formation (6,48) suggests that it most probably contains the receptor-binding domain (RBD), analogous to the RBD of gammaretroviruses. This region (Fig.…”

mentioning

confidence: 99%

Envelope Proteins Containing Single Amino Acid Substitutions Support a Structural Model of the Receptor-Binding Domain of Bovine Leukemia Virus Surface Protein

Johnston

Albritton

Radke

2002

J Virol

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Functional domains of the strikingly conserved envelope (Env) glycoproteins of bovine leukemia virus (BLV) and its close relative, human T-cell leukemia virus type 1 (HTLV-1), are still being defined. We have used BLV Env protein variants to gain insights into the structure and function of this important determinant of viral infectivity. Each of 23 different single amino acid variants found in cDNA clones of env transcripts present after short-term culture of peripheral blood mononuclear cells from BLV-infected sheep was expressed in COS-1 cells and tested for the ability to mediate cell fusion and to be cleaved to surface (SU) and transmembrane (TM) protein subunits. Of 11 Env variants that failed to induce syncytia or did so poorly, 7 contained changes in amino acids identical or chemically conserved in the HTLV-1 Env protein. These seven included the four variants that showed aberrant proteolytic cleavage and poor cell surface expression, underscoring their importance for Env structure. Ten of 12 variants that retained wild-type syncytium-inducing ability clustered in the N-terminal half of BLV SU, which forms the putative receptor-binding domain (RBD). Several variants in the RBD showed evidence of subtle misfolding, as judged by reduced binding to monoclonal antibodies recognizing conformational epitopes F, G, and H formed by the N terminus of SU. We modeled the BLV RBD by aligning putative structural elements with known elements of the ecotropic Friend murine leukemia virus RBD monomer. All the variant RBD residues but one are exposed on the surface of this BLV model. These variants as well as function-altering, antibody-reactive residues defined by other investigators group on one face of the molecular model. They are strikingly absent from the opposite face, implying that it is likely to face inward in Env complexes. This surface might interact with the C-terminal domain of SU or with an adjacent monomer in the Env oligomer. This location suggests an orientation for the monomer of ecotropic Friend murine leukemia virus RBD.Envelope (Env) proteins confer infectivity on retroviral particles. Oligomers of these proteins bind to receptors on the surfaces of host cells and mediate entry of the viral genome into the cell. The Env protein complex is composed of surface glycoprotein (SU) subunits, which are anchored to virions by their association with transmembrane (TM) protein subunits. SU molecules recognize and bind to cellular receptors, thereby initiating a complex series of conformational changes that lead to fusion of viral and cellular membranes by TM oligomers (reviewed in reference 30). Upon successful synthesis of the DNA provirus and its integration into host cell DNA, expression of viral genes ensues. When the newly synthesized polyprotein Env precursor is cleaved in the Golgi apparatus of the virus-producing host cell, SU and TM subunits remain associated in a metastable state (18). Oligomers of mature Env proteins are transported to the cell surface membrane, where they can be incorporated into b...

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“…The sequence of the env gene is highly conserved. 14 In the present experiment the OL-3 and OL-4 primers originating from the gag gene region were more sensitive. The results indicate that the criteria commonly used to select these primers, such as high conservatism of the sequence and the lack of complementarity between sense and antisense primers at the 3Ј end, do not eliminate false-negative results in PCR caused by the target template mutations.…”

Section: ј-Gctgacaaccttcccgacgg-3ј 5ј-gacagtctcgtttccaatgg-3јmentioning

confidence: 80%

Simultaneous Use of Two Primer Pairs Increases the Efficiency of Polymerase Chain Reaction Assay in the Diagnosis of Bovine Leukemia Virus Infection

Reichert

Stec

1999

J VET Diagn Invest

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Antigenic variants of bovine leukemia virus (BLV) are defined by amino acid substitutions in the NH2 part of the envelope glycoprotein gp51

Cited by 52 publications

References 13 publications

Molecular Cloning and Sequencing of an Australian Isolate of Proviral Bovine Leukaemia Virus DNA: Comparison with other Isolates

Molecular Cloning and Sequencing of an Australian Isolate of Proviral Bovine Leukaemia Virus DNA: Comparison with other Isolates

Envelope Proteins Containing Single Amino Acid Substitutions Support a Structural Model of the Receptor-Binding Domain of Bovine Leukemia Virus Surface Protein

Simultaneous Use of Two Primer Pairs Increases the Efficiency of Polymerase Chain Reaction Assay in the Diagnosis of Bovine Leukemia Virus Infection

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