Temperature-sensitive mutants of foot-and-mouth disease virus with altered structural polypeptides. II. Comparison of recombination and biochemical maps

King, Andrew M. Q.; Slade, W. R.; Newman, John W.; McCahon, D.

doi:10.1128/jvi.34.1.67-72.1980

Cited by 29 publications

(15 citation statements)

References 17 publications

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“…Another important mechanism in the evolution of FMDV genomes is recombination [11][12][13]. Direct evidences of FMDV recombination date back 40 years ago [14,15]. Most recombination breakpoints are observed in non-structural proteins.…”

Section: Introductionmentioning

confidence: 99%

Pervasive within-host recombination and epistasis as major determinants of the molecular evolution of the foot-and-mouth disease virus capsid

et al. 2020

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Although recombination is known to occur in foot-and-mouth disease virus (FMDV), it is considered only a minor determinant of virus sequence diversity. Analysis at phylogenetic scales shows inter-serotypic recombination events are rare, whereby recombination occurs almost exclusively in non-structural proteins. In this study we have estimated recombination rates within a natural host in an experimental setting. African buffaloes were inoculated with a SAT-1 FMDV strain containing two major viral sub-populations differing in their capsid sequence. This population structure enabled the detection of extensive within-host recombination in the genomic region coding for structural proteins and allowed recombination rates between the two sub-populations to be estimated. Quite surprisingly, the effective recombination rate in VP1 during the acute infection phase turns out to be about 0.1 per base per year, i.e. comparable to the mutation/substitution rate. Using a high-resolution map of effective within-host recombination in the capsid-coding region, we identified a linkage disequilibrium pattern in VP1 that is consistent with a mosaic structure with two main genetic blocks. Positive epistatic interactions between co-evolved variants appear to be present both within and between blocks. These interactions are due to intra-host selection both at the RNA and protein level. Overall our findings show that during FMDV co-infections by closely related strains, capsid-coding genes recombine within the host at a much higher rate than expected, despite the presence of strong constraints dictated by the capsid structure. Although these intra-host results are not immediately translatable to a phylogenetic setting, recombination and epistasis must play a major and so far underappreciated role in the molecular evolution of the virus at all scales.

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Section: Introductionmentioning

confidence: 99%

Pervasive within-host recombination and epistasis as major determinants of the molecular evolution of the foot-and-mouth disease virus capsid

et al. 2020

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“…Three crosses, A, B, and C, were performed as shown in Table 1. The location of the ts mutation of tsl3gr was based on its map locus (25), which corresponded to the region of the genome encoding the capsid proteins (19). The other parent in cross A, 06-ts302gs, had a ts mutation that covaried with an electrophoretic change in P56a, encoded at the 3' end of the genome (17).…”

Section: Resultsmentioning

confidence: 99%

Recombination and oligonucleotide analysis of guanidine-resistant foot-and-mouth disease virus mutants

Saunders¹,

King²,

McCahon³

et al. 1985

J Virol

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Guanidine resistance (gr) mutations of foot-and-mouth disease virus were mapped by recombining pairs of temperature-sensitive mutants belonging to different subtypes. In each cross, one parent possessed a gr mutation. Recombinants were isolated by selection at the nonpermissive temperature and assayed for the ability to grow in the presence of guanidine. From the progeny of three crosses, four different types of recombinant were distinguished on the basis of protein composition and RNA fingerprint. The sequences of the RNase Tl-resistant oligonucleotides were determined and located in the full-length sequence of foot-and-mouth disease virus. The resulting maps show that (i) each recombinant was generated by a single genetic crossover, and (ii) both of the gr mutations studied were located within an internal 2.9-kilobase region which spans the P34 gene. This supports our hypothesis that guanidine inhibits the growth of foot-and-mouth disease virus by acting on nonstructural polypeptide P34. Additional evidence was provided by RNA fingerprinting gr mutants. In two of four cases the gr mutation was associated with a change in an oligonucleotide located near the 3' end of the P34 gene; in one of these the nucleotide substitution was identified.

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“…Suppression by a mutation that lies in a gene other than the site of the original mutation (extragenic) has been interpreted to mean that the two gene products interact with each other at either a structural or functional level or both. Identification of a number of such extragenic suppressor mutations has been useful in describing protein interactions in a variety of viruses (25,27,37,64). Extragenic suppression is the primary mechanism by which reovirus ts lesions are corrected (48).…”

Section: Discussionmentioning

confidence: 99%

Studies of the major reovirus core protein sigma 2: reversion of the assembly-defective mutant tsC447 is an intragenic process and involves back mutation of Asp-383 to Asn

Coombs

Mak

Petrycky-Cox

1994

J Virol

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The reovirus group C temperature-sensitive mutant tsC447, whose defect maps to the S2 gene, which encodes the major core protein r2, fails to assemble core particles at the nonpermissive temperature. To identify other proteins that may interact with (72 during assembly, we generated and examined 10 independent revertants of the mutant. To determine which gene(s) carried a compensatory suppressor mutation(s), we generated intertypic reassortants between wild-type reovirus serotype 1 Lang and each revertant and determined the temperature sensitivities of the reassortants by efficiency-of-plating assays. Results of the efficiency-of-plating analyses indicated that reversion of the tsC447 defect was an intragenic process in all revertants. To identify the region(s) of (r2 that had reverted, we determined the nucleotide sequences of the S2 genes. In all revertant sequences examined, the G at nucleotide position 1166 in tsC447 had reverted to the A present in the wild-type sequence. This reversion leads to the restoration of a wild-type asparagine (in place of a mutant aspartic acid) at amino acid 383 in the (r2 sequence. These results collectively indicate that the functional lesion in tsC447 is Asp-383 and that this lesion cannot be corrected by alterations in other core proteins. These observations suggest that this region of ff2, which may be important in mediating assembly of the core particle, does not interact significantly with other reovirus proteins.

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Temperature-sensitive mutants of foot-and-mouth disease virus with altered structural polypeptides. II. Comparison of recombination and biochemical maps

Cited by 29 publications

References 17 publications

Pervasive within-host recombination and epistasis as major determinants of the molecular evolution of the foot-and-mouth disease virus capsid

Pervasive within-host recombination and epistasis as major determinants of the molecular evolution of the foot-and-mouth disease virus capsid

Recombination and oligonucleotide analysis of guanidine-resistant foot-and-mouth disease virus mutants

Studies of the major reovirus core protein sigma 2: reversion of the assembly-defective mutant tsC447 is an intragenic process and involves back mutation of Asp-383 to Asn

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