Genetic characterization of the cell-adapted PanAsia strain of foot-and-mouth disease virus O/Fujian/CHA/5/99 isolated from swine

Bai, Xingwen; Bao, Huang; Li, Pinghua; Sun, Pu; Kuang, Wendong; Cao, Yimei; Lu, Zengjun; Liu, Zaixin; Liu, Xiangtao

doi:10.1186/1743-422x-7-208

Cited by 16 publications

(18 citation statements)

References 49 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…BHK-21, WT-CHO and pgsD-677 cell monolayers in 6-well plates were inoculated with the serial ten-fold dilutions of all the selected PanAsia-1 strains and rescued viruses, following the previously described procedures [46]. The values of plaque titrations of each virus were calculated as described previously [24].…”

Section: Methodsmentioning

confidence: 99%

Effects of two amino acid substitutions in the capsid proteins on the interaction of two cell-adapted PanAsia-1 strains of foot-and-mouth disease virus serotype O with heparan sulfate receptor

Bai

Bao

et al. 2014

Virol J

Self Cite

View full text Add to dashboard Cite

BackgroundSome cell-adapted strains of foot-and-mouth disease virus (FMDV) can utilize heparan sulfate (HS) as a receptor to facilitate viral infection in cultured cells. A number of independent sites on the capsid that might be involved in FMDV-HS interaction have been studied. However, the previously reported residues do not adequately explain HS-dependent infection of two cell-adapted PanAsia-1 strains (O/Tibet/CHA/6/99tc and O/Fujian/CHA/9/99tc) of FMDV serotype O.To identify the molecular determinant(s) for the interaction of O/Tibet/CHA/6/99tc and O/Fujian/CHA/9/99tc with HS receptor, several chimeric viruses and site-directed mutants were generated by using an infectious cDNA of a non-HS-utilizing rescued virus (Cathay topotype) as the genomic backbone. Phenotypic properties of these viruses were determined by plaque assays and virus adsorption and penetration assays in cultured cells.ResultsOnly two of the rescued viruses encoding VP0 of O/Tibet/CHA/6/99tc or VP1 of O/Fujian/CHA/9/99tc formed plaques on wild-type Chinese hamster ovary (WT-CHO; HS+) cells, but not on HS-negative pgsD-677 cells. The formation of plaques by these two chimeric viruses on WT-CHO cells could be abolished by the introduction of single amino acid mutations Gln-2080 → Leu in VP2 of O/Tibet/CHA/6/99tc and Lys-1083 → Glu in VP1 of O/Fujian/CHA/9/99tc, respectively. Nonetheless, the introduced mutation Leu-2080 → Gln in VP2 of O/Fujian/CHA/9/99tc for the construction of expectant recombinant plasmid led to non-infectious progeny virus in baby hamster kidney 21 (BHK-21) cells, and the site-directed mutant encoding Glu-1083 → Lys in VP1 of O/Tibet/CHA/6/99tc did not acquire the ability to produce plaques on WT-CHO cells.Significant differences in the inhibition of the infectivity of four HS-utilizing viruses by heparin and RGD-containing peptide were observed in BHK-21 cells.Interestingly, the chimeric virus encoding VP0 of O/Fujian/CHA/9/99tc, and the site-directed mutant encoding Gln-2080 → Leu in VP2 of O/Tibet/CHA/6/99tc could bind to HS, but there was no expression of the 3A protein of these two viruses in WT-CHO cells.ConclusionThe results suggest that the cooperation of certain specific amino acid residues in the capsid proteins of these two cell-adapted PanAsia-1 strains is essential for viral infectivity, the heparin affinity and the capability on FMDV-HS interaction.

show abstract

Section: Methodsmentioning

confidence: 99%

Effects of two amino acid substitutions in the capsid proteins on the interaction of two cell-adapted PanAsia-1 strains of foot-and-mouth disease virus serotype O with heparan sulfate receptor

Bai

Bao

et al. 2014

Virol J

Self Cite

View full text Add to dashboard Cite

show abstract

“…Residue 142 lies within the GH loop close to the RGD motif and modulates the spatial orientation of the GH loop depending on the amino acid at this position [63]. Substitutions at residue 142 have been reported for all Eurasian FMDV serotypes [51,53,55,57,63]. These substitutions are highly variable and differ depending on the cell line in which the virus was cultured [51,55,63].…”

Section: Virus Protein Vp1mentioning

confidence: 99%

“…Furthermore, changes in this part of VP2 are often described to occur in combination with substitutions in VP1 [58,63] during passaging in BHK cells [15,71]. Another well-described phenomenon for serotype A and O are amino acid exchanges at positions 133, 134, and 136 [13,15,51,54,57,72]. This region lies within the αB helix of VP2 (residues 133-138) and is part of the depression that is used for HS binding [48].…”

Section: Virus Protein Vp2mentioning

confidence: 99%

“…The K172N exchange described for a serotype A virus, on the other hand, reduced the positive charge of the region by substitution of a positively charged lysine with an uncharged asparagine [15,58]. A third exchange, K175R in the GH loop of VP2, described for serotype O retained the positive charge at this position [57]. Variations in VP2 are often accompanied by amino acid exchanges in either VP1 or VP3.…”

Section: Virus Protein Vp2mentioning

confidence: 99%

See 1 more Smart Citation

Cell culture propagation of foot-and-mouth disease virus: adaptive amino acid substitutions in structural proteins and their functional implications

Dill

Eschbaumer

2019

Virus Genes

View full text Add to dashboard Cite

Foot-and-mouth disease is endemic in livestock in large parts of Africa and Asia, where it is an important driver of food insecurity and a major obstacle to agricultural development and the international trade in animal products. Virtually all commercially available vaccines are inactivated whole-virus vaccines produced in cell culture, but the adaptation of a field isolate of the virus to growth in culture is laborious and time-consuming. This is of particular concern for the development of vaccines to newly emerging virus lineages, where long lead times from virus isolate to vaccine can delay the implementation of effective control programs. High antigen yields in production cells are also necessary to make vaccines affordable for less developed countries in endemic areas. Therefore, a rational approach to cell culture adaptation that combines prior knowledge of common adaptive mutations and reverse genetics techniques is urgently required. This review provides an overview of amino acid exchanges in the viral capsid proteins in the context of adaptation to cell culture.

show abstract

“…The tissue culture adapted virus, which utilizes heparin sulfate (HS) receptor, was shown to be relatively avirulent in cattle compared with wild-type virus that utilizes integrin receptors (28,36). It was also found that the plaques produced by the HS-binding virus on BHK-21 cells are smaller than the integrin-binding virus (2). The role of 3A protein in viral virulence has also been demonstrated.…”

Section: Discussionmentioning

confidence: 93%

Influence of Foot-and-Mouth Disease Virus O/CHN/Mya98/33-P Strain Leader Protein on Viral Replication and Host Innate Immunity

Jiang

Bai

et al. 2015

Viral Immunology

Self Cite

View full text Add to dashboard Cite

Foot-and-mouth disease virus (FMDV) O/CHN/Mya98/33-P strain was isolated from the esophageal-pharyngeal fluid sample of cattle, and was shown to cause persistent infection. Its leader protein contains 200 amino acids with one amino acid deletion, which is upstream and next to the second initiation codon compared with the majority of FMDV Mya98 strains. The FMDV genome includes two initiation codons that can produce two different leader proteins, Lab (from the first AUG) and Lb (from the second AUG). For convenience, the inter-AUG region was named as La. Previously, it was found that a recombinant virus with Lab of FMDV O/CHN/Mya98/33-P strain had higher proliferation efficiency, and better ability to inhibit the host innate immune response. Three full-length infectious cDNA clones-rHN33-Lb, rHN33-La, and rHNGSLX-Lb-containing the FMDV O/CHN/Mya98/33-P strain leader proteins Lb, La, or the FMDV O/GSLX/2010 strain leader protein Lb, respectively, were constructed based on an established infectious clone r-HN rescued from FMDV O/HN/CHN/93 strain. After infecting pig kidney primary cells, rHN33-La showed higher replication efficiency than r-HN, and rHN33-Lb displayed better ability to resist host innate immunity than rHNGSLX-Lb. These results demonstrated that the inter-AUG region of FMDV strain O/CHN/Mya98/33-P leader protein must be involved in increasing viral replication efficiency. Additionally, the Lb of FMDV O/CHN/Mya98/33-P must be involve in increasing its ability to inhibit host innate immune response, and the distinctive amino acids G56 and/or R118 of FMDV leader protein may play essential roles in it.

show abstract

Genetic characterization of the cell-adapted PanAsia strain of foot-and-mouth disease virus O/Fujian/CHA/5/99 isolated from swine

Cited by 16 publications

References 49 publications

Effects of two amino acid substitutions in the capsid proteins on the interaction of two cell-adapted PanAsia-1 strains of foot-and-mouth disease virus serotype O with heparan sulfate receptor

Effects of two amino acid substitutions in the capsid proteins on the interaction of two cell-adapted PanAsia-1 strains of foot-and-mouth disease virus serotype O with heparan sulfate receptor

Cell culture propagation of foot-and-mouth disease virus: adaptive amino acid substitutions in structural proteins and their functional implications

Influence of Foot-and-Mouth Disease Virus O/CHN/Mya98/33-P Strain Leader Protein on Viral Replication and Host Innate Immunity

Contact Info

Product

Resources

About