Synthesis of fusion proteins with multiple copies of an antigenic determinant of foot-and-mouth disease virus antibodies

Broekhuijsen, Martien; Blom, T; Rijn, Jaap van; Pouwels, Peter H.; Klasen, Erik A.; Fasbender, Marianne; Enger-Valk, B.E.

doi:10.1016/0378-1119(86)90279-9

Cited by 29 publications

(9 citation statements)

References 10 publications

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“…In earlier work, it was demonstrated that the major epitopes of VP1 resides in the region 141-160 and to a lesser extent (2,12) and that synthetic peptides of these regions can elicit virus-neutralizing antibodies in experimental animals (2,3). The direct binding studies using polyclonal and monoclonal antibodies showed that the 40-residue peptide contained VP1 sequences 200-213 linked to residues 141-158 contains at least one B-cell epitope (8).…”

Section: Discussionmentioning

confidence: 99%

“…However, the immunogenicity of the VP1 protein isolated from either the virus or the same protein expressed in Escherichia coli cells (10) by DNA recombinant techniques is very low compared to the intact virus particle. An alternative approach to increase the immunogenicity of foot-and-mouth disease virus (FMDV) is using synthetic peptides containing residues of amino acids 141-160 and 200-213 of VP1, which has been found to induce much higher levels of neutralizing antibodies (2,3,19). A peptide corresponding to amino acids 21-40 of VP1 protein of OIK FMDV was shown to be a T-cell epitope recognized by cattle cells.…”

Section: Introductionmentioning

confidence: 99%

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Recombinant Fusion Protein and DNA Vaccines Against Foot and Mouth Disease Virus Infection in Guinea Pig and Swine

Huang

Yang²,

Xu³

et al. 1999

Viral Immunology

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In this study, we provide evidence that a recombinant fusion protein containing beta-galactosidase and a tandem repeat peptide of immunogenic dominant epitope of foot-and-mouth disease virus (FMDV) VP1 protein elicits high levels of neutralizing antibody and protects both guinea pigs and swine against infection. Vaccination with this fusion protein induced a FMDV-specific proliferative T-cell response and a neutralizing antibody response. The immunized guinea pigs and swine were protected against FMD type O virus infection. Two DNA plasmids expressing genes of foot-and-mouth disease were constructed. Both plasmids pBO1 and pCO1 contain a signal sequence of the swine immunoglobulin G (IgG) gene and fusion protein gene of pXZ84. The signal sequence and fusion protein gene were under the control of a metallothionein promoter in the case of the pBO1 plasmid and under the control of a cytomegalovirus immediate early promoter in the case of pCO1 plasmid. When pBO1 and pCO1 were inoculated intramuscularly into guinea pigs, both plasmids elicited a neutralizing antibody response and spleen cell proliferation increased following stimulation with FMDV antigen, but animals were not protected from viral challenge.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Recombinant Fusion Protein and DNA Vaccines Against Foot and Mouth Disease Virus Infection in Guinea Pig and Swine

Huang

Yang²,

Xu³

et al. 1999

Viral Immunology

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“…Despite negative results with canine parvovirus [1123, infectious bursal disease virus [8] and bovine rotavirus [373, there are several reports about expression products that did induce in vitro neutralizing sera. Examples are the gp 120 sequence from HIV [90], the VP7 sequence from simian rotavirus [6], the VP7c sequence from bovine rotavirus [713, the major antigenic site on VP 1 from foot-and-mouth-disease virus [14,15,138], the VP 1 regions 52-302 and 24-129 from poliovirus I [493, the VP2 sequence from infectious pancreatic necrosis virus [643, and the N-terminal gD sequence from herpex simplex virus I [56, 583. More spectacular is the induction of protective immunity.…”

Section: Immunogenicity Of Expression Productsmentioning

confidence: 99%

Mapping of viral epitopes with prokaryotic expression products

Lenstra

Kusters

Zeijst

1990

Archives of Virology

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Several systems are available for the expression of foreign gene sequences in Escherichia coli. We describe the use of prokaryotic expression products of viral gene fragments in order to identify the regions that specify the binding sites of antibodies. This approach is particularly successful if the antigenicity does not depend on the native protein, but only on the amino acid sequence, i.e., if the epitope is sequential. Combining prokaryotic expression with the use of synthetic peptides often permits a fast and accurate mapping of an epitope. The occurrence of immunodominant sequential epitopes on the surfaces of viruses seems to be a widespread phenomenon.

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“…The fusion proteins P71, P72, P74 and P81 were produced and purified as described by Broekhuijsen et al (1986b). A yield of 20 to 30 mg of fusion protein was usualy obtained from a bacterial culture of 6 1.…”

Section: Construction Of Expression Plasmidsmentioning

confidence: 99%

“…In preliminary experiments in rabbits we have shown that proteins consisting of flgalactosidase plus two or four copies of the sequence 137 to 162 situated at the N terminus elicit higher levels of virus-specific antibody than the protein containing only one copy of the peptide (Broekhuijsen et al, 1986b). Furthermore, Kleid et al (1985) have provided evidence that two copies of the determinant, expressed in E. coli as a fusion protein with TrpLE, elicited high levels of neutralizing antibody in cattle and protected them from infection.…”

Section: Introductionmentioning

confidence: 99%

Fusion Proteins with Multiple Copies of the Major Antigenic Determinant of Foot-and-Mouth Disease Virus Protect both the Natural Host and Laboratory Animals

Broekhuijsen

Rijn

Blom

et al. 1987

Journal of General Virology

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SUMMARYProteins consisting of one, two or four copies of the amino acid sequence 137 to 162, which contains the major immunogenic site of VP1 of foot-and-mouth disease virus, attached to the N-terminus of fl-galactosidase have been expressed in Escherichia coli cells. In guinea-pigs the protein containing one copy (P71) of the viral determinant elicited only low levels of neutralizing antibody whereas protective levels were elicited by the proteins containing two (P72) or four (P74) copies of the determinant. Single inoculations of the P72 and P74 proteins containing as little as 2 ~tg or 0-8 gg of peptide respectively were sufficient to protect all the animals against challenge infection. Moreover, the equivalent of 40 gg of peptide in P74 protected pigs against challenge infection after one inoculation.

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Synthesis of fusion proteins with multiple copies of an antigenic determinant of foot-and-mouth disease virus antibodies

Cited by 29 publications

References 10 publications

Recombinant Fusion Protein and DNA Vaccines Against Foot and Mouth Disease Virus Infection in Guinea Pig and Swine

Recombinant Fusion Protein and DNA Vaccines Against Foot and Mouth Disease Virus Infection in Guinea Pig and Swine

Mapping of viral epitopes with prokaryotic expression products

Fusion Proteins with Multiple Copies of the Major Antigenic Determinant of Foot-and-Mouth Disease Virus Protect both the Natural Host and Laboratory Animals

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