Protection against foot-and-mouth disease by immunization with a chemically synthesized peptide predicted from the viral nucleotide sequence

Bittle, James L.; Houghten, Richard A.; Alexander, Hannah; Shinnick, Thomas M.; Sutcliffe, J. Gregor; Lerner, Richard A.; Rowlands, David J.; Brown, F.

doi:10.1038/298030a0

Cited by 772 publications

(330 citation statements)

References 21 publications

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“…First, the FMDV structures determined by Stuart and colleagues (16)(17)(18)(19) revealed that, contrary to other picornaviruses, no canyon or pit was present on the smooth FMDV surface. Furthermore, the critical receptor recognition Arg-Gly-Asp domain was located on a highly mobile loop (the G-H loop of VP1), which was also a major antigenic site for the virus (20)(21)(22). Additional structural work by Fita and colleagues (23) further indicated that the ArgGly-Asp motif is not only part of the receptor recognition site but it also interacts directly with some anti-viral neutralizing antibodies.…”

mentioning

confidence: 96%

Evolution subverting essentiality: Dispensability of the cell attachment Arg-Gly-Asp motif in multiply passaged foot-and-mouth disease virus

Martı́nez

Verdaguer

Mateu

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

119

117

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Aphthoviruses use a conserved Arg-Gly-Asp triplet for attachment to host cells and this motif is believed to be essential for virus viability. Here we report that this triplet-which is also a widespread motif involved in cell-tocell adhesion-can become dispensable upon short-term evolution of the virus harboring it. Foot-and-mouth disease virus (FMDV), which was multiply passaged in cell culture, showed an altered repertoire of antigenic variants resistant to a neutralizing monoclonal antibody. The altered repertoire includes variants with substitutions at the Arg-Gly-Asp motif. Mutants lacking this sequence replicated normally in cell culture and were indistinguishable from the parental virus. Studies with individual FMDV clones indicate that amino acid replacements on the capsid surface located around the loop harboring the Arg-Gly-Asp triplet may mediate in the dispensability of this motif. The results show that FMDV quasispecies evolving in a constant biological environment have the capability of rendering totally dispensable a receptor recognition motif previously invariant, and to ensure an alternative pathway for normal viral replication. Thus, variability of highly conserved motifs, even those that viruses have adapted from functional cellular motifs, can contribute to phenotypic f lexibility of RNA viruses in nature.

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mentioning

confidence: 96%

Evolution subverting essentiality: Dispensability of the cell attachment Arg-Gly-Asp motif in multiply passaged foot-and-mouth disease virus

Martı́nez

Verdaguer

Mateu

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

119

117

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“…Antiviral responses to peptide immunogens have been extremely variable. The greatest progress has probably been achieved using peptides corresponding to the surface-exposed G-H loop of VP1 of foot-and-mouth disease virus (FMDV), which can elicit a neutralizing antibody response (Bittle et al, 1982;Pfaff et al, 1982) that is protective in target species (DiMarchi et al, 1986). Approximately 35 % of the antibodies induced by these peptides in laboratory animals also recognize virus (Parry et al, 1988) but, even so, the levels of protection attained in target species have been inconsistent.…”

Section: Introductionmentioning

confidence: 99%

Characterization of monoclonal antibodies raised against a synthetic peptide capable of inducing a neutralizing response to human rhinovirus type 2

Barnett

Rowlands

Parry

1993

Journal of General Virology

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Synthetic peptides incorporating the derived amino acid sequence of VP2 residues 156 to 170 of human rhinovirus type 2 (HRV2) have previously been shown to elicit antibodies that neutralize virus infectivity. The proportion of virus-reactive antibodies present in polyclonal antisera to these peptides is, however, very low. Moreover, neutralization titrations of such antisera correlate poorly with other assays of either anti-virus or anti-peptide activity, suggesting the presence of antibodies with different specificities. To investigate these findings further, we produced a panel of monoclonal antibodies (MAbs) to VP2 peptides of residues 156 to 170 and characterized their reactions with a range of antigens in ELISA, precipitation and neutralization titrations. All the MAbs obtained recognized the homologous peptide, but could be divided into four main reaction groups according to their specificity for viral antigens. Antibodies in the first group recognized and neutralized native virus, apparently by preventing attachment to cells. A second group of MAbs bound to intact particles with similar affinities to the first group, but failed to neutralize infectivity. Antibodies in the third group recognized virus only after capsid distortions incurred by heating or by previous reaction with polyclonal antibodies. The fourth group comprised MAbs that were mainly peptide-specific. Some possible applications of anti-peptide MAbs to improving the design of peptide immunogens are considered.

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“…The difference between the 2 isolates and O1K lies in the main VP1 antigenic domain on each side of the highly conserved arginine-glycine-aspartate sequence. 3 Changes in amino acid sequence in this region are most probably responsible for the subtype antigenic identity of the isolates. All the data presented here strongly suggest that the 2 events originated from the same virus subtype of the O serotype.…”

Section: Methodsmentioning

confidence: 99%

“…The virus genome is an 8.5-kilobase (kb) single strand of RNA in the plus orientation, carrying a poly A tract at its 3' end and a viral genome protein (VPg) at its 5' end. 3,6 The virion, an icosahedral capsid, consists of 60 copies of each of the four proteins, VP1-4, of which VP1 is the main protein determining antigenic identity. 1,10 The differences in VP1 sequences are the basis for developing reverse transcriptase polymerase chain reaction (RT-PCR) tests to identify different serotypes.…”

mentioning

confidence: 99%

Detection and Subtyping of Foot-and-Mouth Disease Virus in Infected Cattle by Polymerase chain Reaction and Amplified VP1 Sequencing

Stram¹,

Molad²,

Chai³

et al. 1995

J VET Diagn Invest

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Abstract. Fast and accurate detection of foot-and-mouth disease (FMD) outbreaks is needed to limit spread of the disease by proper vaccination. The use of the polymerase chain reaction (PCR) has revolutionized the way in which viral diseases are diagnosed. Sequence analysis of the amplified VP1 sequence can enable the classification of FMD virus detected in the morbid animal. PCR assays were carried out to identify the virus and its serotype in suspect animals from 2 outbreaks of FMD type O virus. Sequence analysis of the amplified VP1 cDNA showed 78% homology with O1K and over 95% homology between the samples. These findings suggest that the 2 outbreaks were due to infection with the same virus serosubtype.Foot-and-mouth disease virus (FMDV) is one of the most dangerous viruses of ruminants. The speed with which it spreads and its ability to change its antigenic identity makes it very threatening to the beef and dairy industries of many countries. There are 7 different virus serotypes that do not cross-react antigenically; these are the results of mutations within the VP1 gene (changes in nucleotide sequences 4,9,15 ). Each serotype consists of many subtypes, about 80 total. 2 The virus belongs to the genus Aphthovirus in the family Picornaviridae. The virus genome is an 8.5-kilobase (kb) single strand of RNA in the plus orientation, carrying a poly A tract at its 3' end and a viral genome protein (VPg) at its 5' end. 3,6 The virion, an icosahedral capsid, consists of 60 copies of each of the four proteins, VP1-4, of which VP1 is the main protein determining antigenic identity. 1,10 The differences in VP1 sequences are the basis for developing reverse transcriptase polymerase chain reaction (RT-PCR) tests to identify different serotypes. 12,14 These RT-PCR tests are based on differences in VP1 gene sequences among the many virus serotypes. Using methods developed previously, 14 2 outbreaks of infection with FMDV O serotype were diagnosed in Israel. In addition, the amplified VP1 segments were sequenced, showing that the outbreaks were caused by the same virus subtype that was first isolated in Oman in 1989. according to the manufacturer's instructions. VP1 primers are shown in Table 1, and RT-PCR conditions were as previously described. 14 Following PCR, amplified VP1 fragments were electrophoresed on 1.5% low-melting-point agarose and extracted as previously described. 13 The isolated fragments were sequenced using an automatic sequencer b with one of the PCR primers as the sequencing primer, and computer sequence analysis was done. c

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Protection against foot-and-mouth disease by immunization with a chemically synthesized peptide predicted from the viral nucleotide sequence

Cited by 772 publications

References 21 publications

Evolution subverting essentiality: Dispensability of the cell attachment Arg-Gly-Asp motif in multiply passaged foot-and-mouth disease virus

Evolution subverting essentiality: Dispensability of the cell attachment Arg-Gly-Asp motif in multiply passaged foot-and-mouth disease virus

Characterization of monoclonal antibodies raised against a synthetic peptide capable of inducing a neutralizing response to human rhinovirus type 2

Detection and Subtyping of Foot-and-Mouth Disease Virus in Infected Cattle by Polymerase chain Reaction and Amplified VP1 Sequencing

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