Chemical basis of antigenic variation in foot-and-mouth disease virus

Rowlands, David J.; Clarke, Berwyn; Carroll, Anthony R.; Brown, F.; Nicholson, Bruce H.; Bittle, James L.; Houghten, Richard A.; Lerner, Richard A.

doi:10.1038/306694a0

Cited by 178 publications

(85 citation statements)

References 20 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It is also becoming apparent that the antigenic status of type O FMDV may be rather more complex than in other serotypes of this virus. Rowlands et al (1983) showed that in A12 some natural variants were altered at residues 148 and 153 (site 1) and were recognized differently by convalescent guinea-pig sera suggesting that this site was immunodominant. Although only limited sequencing of these A1 z variants has been reported, further sequencing of the whole P1 region has failed to find other differences between these variants (S. E. Newton & D. J.…”

Section: Discussionmentioning

confidence: 99%

Evidence for At Least Four Antigenic Sites on Type O Foot-and-Mouth Disease Virus Involved in Neutralization; Identification by Single and Multiple Site Monoclonal Antibody-resistant Mutants

McCahon

Crowther

Belsham

et al. 1989

Journal of General Virology

View full text Add to dashboard Cite

SUMMARYNeutralizing monoclonal antibodies raised against type 0 foot-and-mouth disease virus have been characterized on the basis of their reactivity with a panel of single site monoclonal antibody-resistant mutants which had defined three antigenic sites. Five antibodies neutralized all these mutants, but by selecting further single site mutants with one of these antibodies it was possible to define a fourth site involved in virus neutralization. Two monoclonal antibodies still neutralized these mutants and all multiple site resistant mutants. One multiple site resistant mutant was resistant to neutralization at each of four antigenic sites but was still efficiently neutralized by type 0 convalescent cattle sera. The relationship between sites recognized by different monoclonal antibodies generated in different laboratories is discussed. INTRODUCTIONStudies on the antigenic structure of two picornaviruses, poliovirus and rhinovirus, have been considerably enhanced by the solving of their three-dimensional crystal structure (Hogle et al., 1985;Rossmann et al., 1985) and the isolation and sequence analysis of monoclonal antibody (MAb) escape mutants (Minor et al., 1986;Sherry et al., 1986). Crystallographic studies on footand-mouth disease virus (FMDV), another picornavirus, are also in progress (Fox et al., 1987) and a number of laboratories have generated MAbs capable of neutralizing type O virus. characterized some 30 MAb-resistant mutants of the O1 Kaufbeuren strain of FMDV isolated using five different neutralizing MAbs. Three distinct antigenic sites were involved in virus neutralization. In this context the term antigenic site is used to describe an area of the virus surface which may contain several MAb epitopes; if one epitope is changed and this affects the ability of a second MAb to neutralize the virus then it is considered that the second MAb recognizes an epitope in the same antigenic site as that changed.Recently Stave et al. (1988) have used different MAbs to define three sites of neutralization. In this communication we now use the panel of mutants generated by Xie et al. (1987) to map the binding sites of MAbs generated in different laboratories and then use these antibodies to show the existence of further sites involved in the neutralization of type O FMDV. We have also generated multiple site mutants which are resistant to neutralization at each of two, three or four sites.

show abstract

Section: Discussionmentioning

confidence: 99%

Evidence for At Least Four Antigenic Sites on Type O Foot-and-Mouth Disease Virus Involved in Neutralization; Identification by Single and Multiple Site Monoclonal Antibody-resistant Mutants

McCahon

Crowther

Belsham

et al. 1989

Journal of General Virology

View full text Add to dashboard Cite

show abstract

“…On the basis of these serological tests the viruses were grouped into two distinct pairs, A with C and B with USA (Table 1). The same grouping was also obtained using antisera raised against synthetic peptides corresponding to sequences 141 -160 of the four viruses (Rowlands et al 1983).…”

mentioning

confidence: 99%

“…These serological differences can be correlated with sequence changes at positions 148 and 153 of VP1 (Rowlands et al 1983;Rowlands, 1985). On the basis of these serological tests the viruses were grouped into two distinct pairs, A with C and B with USA (Table 1).…”

mentioning

confidence: 99%

See 1 more Smart Citation

Correlations between the conformations elucidated by CD spectroscopy and the antigenic properties of four peptides of the foot‐and‐mouth disease virus

Siligardi

Drake

Mascagni

et al. 1991

European Journal of Biochemistry

View full text Add to dashboard Cite

The conformational features of four related antigenic peptides (A, B, C and USA) from the foot-and-mouth disease virus ( F M D V ) (VP1; 141 -160 of serotype A, subtype 12), assessed by CD, were found to correlate with the serological properties of these peptides. The C D spectra of the four peptides, obtained under cryogenic and solvent titration conditions, were consistent with three conformational components (a left-handed extended helix, an a-helix and a 3,0 helix) for peptides A and C and four components (a /?-turn of type 11, an a-helix, a y-turn and a 310 helix) for peptides B and USA. The amino acid substitutions at positions 148 and 153, which distinguish the peptides, are therefore responsible for both their conformational and antigenic differences.

show abstract

“…Recombinant clones from the At0 subtype were constructed using a synthetic oligonucleotide primer (Celltech, Slough, U.K.) which had previously been used for primer extension sequencing (Carroll et al, 1984). First-strand cDNA synthesis was performed as described by Rowlands et al (1983). cDNA transcripts were then made double-stranded and cloned in Escherichia coli strain MC1061 (Casadaban & Cohen, 1980) using Clal-digested pAT153 and Clal linkers (Amersham) by standard procedures.…”

Section: Methodsmentioning

confidence: 99%

Two Initiation Sites for Foot-and-Mouth Disease Virus Polyprotein in vivo

Clarke¹,

Sangar²,

Burroughs

et al. 1985

Journal of General Virology

Self Cite

View full text Add to dashboard Cite

SUMMARYTypically, the translation of eukaryotic mRNAs into protein is initiated at a single site. However, we have recently shown that not one but two primary products, P20a and P I6, are translated from the 5' end of the coding region of the genome of foot-andmouth disease virus (FMDV). In this paper we show by partial protease digestion of these proteins that they differ only at their N termini, thus confirming the presence of two initiation sites for translation of FMDV RNA. Sequence analysis of two subtypes of the virus (Al0 and A12) confirms the presence of two initiator AUG codons in the expected position on the genome. By correlation with protein synthesis data from these subtypes it appears that the relative use of each initiation site is dependent on its surrounding nucleotide sequence. In addition, the ratio of the two proteins when synthesized in vitro differs markedly from that when they are synthesized in vivo, suggesting the presence of a control mechanism for synthesis of P20a in vivo which may be absent in vitro. We also show that the cleavage site between these two proteins and the structural protein precursor, P88, is located closer to the N terminus of the polyprotein than has previously been reported.

show abstract

Chemical basis of antigenic variation in foot-and-mouth disease virus

Cited by 178 publications

References 20 publications

Evidence for At Least Four Antigenic Sites on Type O Foot-and-Mouth Disease Virus Involved in Neutralization; Identification by Single and Multiple Site Monoclonal Antibody-resistant Mutants

Evidence for At Least Four Antigenic Sites on Type O Foot-and-Mouth Disease Virus Involved in Neutralization; Identification by Single and Multiple Site Monoclonal Antibody-resistant Mutants

Correlations between the conformations elucidated by CD spectroscopy and the antigenic properties of four peptides of the foot‐and‐mouth disease virus

Two Initiation Sites for Foot-and-Mouth Disease Virus Polyprotein in vivo

Contact Info

Product

Resources

About