Synthesis of fusion proteins containing antigenic determinants of foot-and-mouth disease virus

Broekhuijsen, Martien; Blom, T; Kottenhagen, M.J.; Pouwels, Peter H.; Meloen, Rob H.; Barteling, S. J.; Enger-Valk, B.E.

doi:10.1016/0264-410x(86)90050-2

Cited by 20 publications

(12 citation statements)

References 20 publications

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“…However Winther and his colleagues (1986) showed that this fusion protein was no more immunogenic for mice or guinea pigs than the chemically linked peptide. Broekhuijsen et al (1986) reported similar results.…”

Section: Attachment Of the Peptide To The N Terminus Ofe-galactosidasesupporting

confidence: 63%

Immunological Adjuvants and Vaccines

Gregoriadis¹,

Allison²,

Poste³

1989

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All rights reservedNo part of this book may be reproduced, stored in a retrieval system, or transmitted in any form or by any means, electronic, mechanical, photocopying, microfilming, recording, or otherwise, without written permission from the Publisher PREFACE Vaccination, chiefly responsible for the eradication of smallpox and the control of poliomyelitis and German measles in man and of foot-andmouth, Marek's and Newcastle disease in domestic animals, remains the best answer to infectious diseases. Early vaccines were live wild type organisms but these have been largely replaced by attenuated or killed organisms or by purified components (subunits) thereof. More recently, developments in recombinant DNA techniques, the advent of monoclonal antibodies and progress in our understanding of the immunological structure of proteins, have laid the foundations for a new generation of vaccines. For instance, subuni t vaccines have been produced through gene cloning and a number of peptides mimicking small regions of proteins on the outer coat of viruses and capable of eliciting virus neutralizing antibodies, have been synthesized. Such vaccines are defined at the molecular level, can elicit immune responses controlling specific infectious organisms and are, thus, potentially free of the problems inherent in conventional ones. However, because subunit and peptide vaccines are only weakly or non-immunogenic, they require the presence of immunological adjuvants. These are a diverse array of agents that promote specific humoural and/or cell-mediated immunity responses to antigens. This book contains the proceedings of the 1st NATO Advanced Studies Institute "Immunological Adjuvants and Vaccines" held in Cape Sounion Beach, Greece during 24 June-5 July, 1988. It deals with traditional and modern immunological adjuvants as applied to a variety of conventional and new generation vaCCines, mechanisms of adjuvanticity and related immune responses as well as optimization of such responses by the use of appropriate adjuvant formulations. We express appreciation to Professors Ruth Arnon and J.H.L. Playfair for their advice in the planning of the ASI, to Dr. G. Deliconstantinos Wl10, as Chairman of the local committee, contributed most effectively to its success, and to Mrs. A. Massaro for her help with practical aspects of the ASI. We are particularly grateful to Hrs. Susan

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Section: Attachment Of the Peptide To The N Terminus Ofe-galactosidasesupporting

confidence: 63%

Immunological Adjuvants and Vaccines

Gregoriadis¹,

Allison²,

Poste³

1989

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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 construction of plasmids pM01-71, p M01-72 and pM01-74 has been described before (Broekhuijsen et al, 1986a, b). These plasmids encode fusion proteins P71, P72 and P74, containing one, two and four copies of amino acids 137 to 162 from VP1 of FMDV, type O1 BFS, fused to the N terminus of/~-galactosidase.…”

Section: Construction Of Expression Plasmidsmentioning

confidence: 99%

“…This approach has been used independently by Broekhuijsen et al (1986a) and Winther et al (1986). Both groups used an expression vector into which the genes coding for amino acids 137 to 162 or 142 to 160 of the viral protein were fused to the gene coding for fl-galactosidase and expressed in E. coli cells, fl-Galactosidase was chosen because it had been shown that antibodies are formed against foreign proteins which are located at the amino terminus of such fusion proteins.…”

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 containing antigenic determinants of foot-and-mouth disease virus

Cited by 20 publications

References 20 publications

Immunological Adjuvants and Vaccines

Immunological Adjuvants and Vaccines

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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